ID   SPIKE_CVHSA             Reviewed;        1255 AA.
AC   P59594; Q6QU82; Q7T696; Q7TA19; Q7TFA2; Q7TFB1; Q80BV6;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 1.
DT   17-JUN-2020, entry version 136.
DE   RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE            Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE   AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE   AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Contains:
DE     RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Contains:
DE     RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Contains:
DE     RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099};
DE   Flags: Precursor;
GN   Name=S {ECO:0000255|HAMAP-Rule:MF_04099}; ORFNames=2;
OS   Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome
OS   coronavirus).
OC   Viruses; Riboviria; Nidovirales; Cornidovirineae; Coronaviridae;
OC   Orthocoronavirinae; Betacoronavirus; Sarbecovirus.
OX   NCBI_TaxID=694009;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9675; Paguma larvata (Masked palm civet).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Urbani;
RX   PubMed=12730500; DOI=10.1126/science.1085952;
RA   Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R.,
RA   Icenogle J.P., Penaranda S., Bankamp B., Maher K., Chen M.-H., Tong S.,
RA   Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D., Erdman D.D.,
RA   Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E., Sanchez A., Liffick S.,
RA   Holloway B., Limor J., McCaustland K., Olsen-Rasmussen M., Fouchier R.,
RA   Guenther S., Osterhaus A.D.M.E., Drosten C., Pallansch M.A., Anderson L.J.,
RA   Bellini W.J.;
RT   "Characterization of a novel coronavirus associated with severe acute
RT   respiratory syndrome.";
RL   Science 300:1394-1399(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Tor2;
RX   PubMed=12730501; DOI=10.1126/science.1085953;
RA   Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A.,
RA   Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y.,
RA   Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L., Leach S.R.,
RA   Mayo M., McDonald H., Montgomery S.B., Pandoh P.K., Petrescu A.S.,
RA   Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E., Stott J.M.,
RA   Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N., Bernard K.,
RA   Booth T.F., Bowness D., Czub M., Drebot M., Fernando L., Flick R.,
RA   Garbutt M., Gray M., Grolla A., Jones S., Feldmann H., Meyers A.,
RA   Kabani A., Li Y., Normand S., Stroher U., Tipples G.A., Tyler S.,
RA   Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M., Petric M.,
RA   Skowronski D.M., Upton C., Roper R.L.;
RT   "The genome sequence of the SARS-associated coronavirus.";
RL   Science 300:1399-1404(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate CUHK-Su10, and Isolate CUHK-W1;
RX   PubMed=12853594; DOI=10.1056/nejm200307103490216;
RA   Tsui S.K.W., Chim S.S.C., Lo Y.M.D.;
RT   "Coronavirus genomic-sequence variations and the epidemiology of the severe
RT   acute respiratory syndrome.";
RL   N. Engl. J. Med. 349:187-188(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate HKU-39849;
RX   PubMed=12876307; DOI=10.1177/15353702-0322807-13;
RA   Zeng F.Y., Chan C.W., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C.C.,
RA   Hui R.K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B.,
RA   Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.;
RT   "The complete genome sequence of severe acute respiratory syndrome
RT   coronavirus strain HKU-39849 (HK-39).";
RL   Exp. Biol. Med. 228:866-873(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate GZ50, and Isolate HKU-36871;
RX   PubMed=12958366; DOI=10.1126/science.1087139;
RA   Guan Y., Zheng B.J., He Y.Q., Liu X.L., Zhuang Z.X., Cheung C.L., Luo S.W.,
RA   Li P.H., Zhang L.J., Guan Y.J., Butt K.M., Wong K.L., Chan K.W., Lim W.,
RA   Shortridge K.F., Yuen K.Y., Peiris J.S.M., Poon L.L.M.;
RT   "Isolation and characterization of viruses related to the SARS coronavirus
RT   from animals in southern China.";
RL   Science 302:276-278(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, and
RC   Isolate GD01;
RA   Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W., Jiang T.,
RA   Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y., Li X., Lu F.,
RA   Tan G., Yang R., Cao W.S., Wang J., Chen W., Cong L., Deng Y., Dong W.,
RA   Han Y., Hu W., Lei M., Li C., Li G., Li G., Li H., Li S., Li S., Li W.,
RA   Li W., Lin W., Liu J., Liu Z., Lu H., Ni P., Qi Q., Sun Y., Tang L.,
RA   Tong Z., Wang J., Wang X., Wu Q., Xi Y., Xu Z., Yang L., Ye C., Ye J.,
RA   Zhang B., Zhang F., Zhang J., Zhang X., Zhou J., Yang H.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Sin2500, Isolate Sin2677, Isolate Sin2679, Isolate Sin2748,
RC   and Isolate sin2774;
RX   PubMed=12781537; DOI=10.1016/s0140-6736(03)13414-9;
RA   Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
RA   Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
RA   Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M., Liu E.T.;
RT   "Comparative full-length genome sequence analysis of 14 SARS coronavirus
RT   isolates and common mutations associated with putative origins of
RT   infection.";
RL   Lancet 361:1779-1785(2003).
RN   [8]
RP   ERRATUM OF PUBMED:12781537.
RA   Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
RA   Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
RA   Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M., Liu E.T.;
RL   Lancet 361:1832-1832(2003).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate TW1;
RA   Yeh S.-H., Kao C.-L., Tsai C.-Y., Liu C.-J., Chen D.-S., Chen P.-J.;
RT   "The complete genome of SARS coronavirus clone TW1.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate FRA;
RA   Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K., Censini S.,
RA   Guidotti S., Masignani V., Scarselli M., Mora M., Donati C., Han J.,
RA   Song H.C., Abrignani S., Covacci A., Rappuoli R.;
RT   "SARS virus is a close relative of type II coronaviruses.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Frankfurt 1;
RX   PubMed=12917450; DOI=10.1099/vir.0.19424-0;
RA   Thiel V., Ivanov K.A., Putics A., Hertzig T., Schelle B., Bayer S.,
RA   Weissbrich B., Snijder E.J., Rabenau H., Doerr H.W., Gorbalenya A.E.,
RA   Ziebuhr J.;
RT   "Mechanisms and enzymes involved in SARS coronavirus genome expression.";
RL   J. Gen. Virol. 84:2305-2315(2003).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate TWC;
RA   Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee S.C., Lin Y.-C.,
RA   Hsu C.-K., Chen H.-Y., Chang J.G., Chen P.-J., Su I.-J.;
RT   "Genomic sequence of SARS isolate from the first fatal case in Taiwan.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate ZJ01;
RA   Cong L.-M., Ding G.-Q., Lu Y.-Y., Weng J.-Q., Yan J.-Y., Hu N.-P.,
RA   Wo J.-E., Chen S.-Y., Zhang Y.-J., Mei L.-L., Wang Z.-G., Yao J.,
RA   Zhu H.-P., Lu Q.-Y., Li M.-H., Gong L.-M., Shi W., Li L.-J.;
RT   "SARS coronavirus ZJ01 isolate spike glycoprotein.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Shanghai LY;
RA   Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Taiwan TC1, Isolate Taiwan TC2, and Isolate Taiwan TC3;
RA   Chang J.-G.C., Lin T.-H., Chen C.-M., Lin C.-S., Chan W.-L., Shih M.-C.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [16]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate TWH, Isolate TWJ, Isolate TWK, Isolate TWS, and Isolate TWY;
RA   Shu H.Y., Wu K.M., Tsai S.F.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [17]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate HSR 1;
RA   Canducci F., Clementi M., Poli G., Vicenzi E.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [18]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate TWC2, and Isolate TWC3;
RA   Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee H.-C., Lin Y.-C.,
RA   Hsu C.-K., Chen H.-Y., Chen P.-J., Su I.-J.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [19]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate AS;
RA   Balotta C., Corvasce S., Violin M., Galli M., Moroni M., Vigevani G.M.,
RA   Ruan Y.J., Salemi M.;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [20]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Shanghai QXC1;
RA   Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
RT   "Analysis of SARS coronavirus genome in Shanghai isolates.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [21]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate GD03;
RX   PubMed=15695582; DOI=10.1073/pnas.0409608102;
RA   Song H.D., Tu C.C., Zhang G.W., Wang S.Y., Zheng K., Lei L.C., Chen Q.X.,
RA   Gao Y.W., Zhou H.Q., Xiang H., Zheng H.J., Chern S.W., Cheng F., Pan C.M.,
RA   Xuan H., Chen S.J., Luo H.M., Zhou D.H., Liu Y.F., He J.F., Qin P.Z.,
RA   Li L.H., Ren Y.Q., Liang W.J., Yu Y.D., Anderson L., Wang M., Xu R.H.,
RA   Wu X.W., Zheng H.Y., Chen J.D., Liang G., Gao Y., Liao M., Fang L.,
RA   Jiang L.Y., Li H., Chen F., Di B., He L.J., Lin J.Y., Tong S., Kong X.,
RA   Du L., Hao P., Tang H., Bernini A., Yu X.J., Spiga O., Guo Z.M., Pan H.Y.,
RA   He W.Z., Manuguerra J.C., Fontanet A., Danchin A., Niccolai N., Li Y.X.,
RA   Wu C.I., Zhao G.P.;
RT   "Cross-host evolution of severe acute respiratory syndrome coronavirus in
RT   palm civet and human.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:2430-2435(2005).
RN   [22]
RP   INTERACTION WITH HUMAN ACE2, AND CHARACTERIZATION OF CELLULAR RECEPTOR.
RX   PubMed=14647384; DOI=10.1038/nature02145;
RA   Li W., Moore M.J., Vasilieva N., Sui J., Wong S.-K., Berne M.A.,
RA   Somasundaran M., Sullivan J.L., Luzuriaga K., Greenough T.C., Choe H.,
RA   Farzan M.;
RT   "Angiotensin-converting enzyme 2 is a functional receptor for the SARS
RT   coronavirus.";
RL   Nature 426:450-454(2003).
RN   [23]
RP   FUNCTION, INTERACTION WITH HUMAN ACE2, AND MUTAGENESIS OF CYS-323; CYS-348;
RP   GLU-452; ASP-454; ASP-463; CYS-467; CYS-474 AND ASP-480.
RX   PubMed=14670965; DOI=10.1074/jbc.c300520200;
RA   Wong S.K., Li W., Moore M.J., Choe H., Farzan M.;
RT   "A 193-amino acid fragment of the SARS coronavirus S protein efficiently
RT   binds angiotensin-converting enzyme 2.";
RL   J. Biol. Chem. 279:3197-3201(2004).
RN   [24]
RP   CHARACTERIZATION OF HEPTAD REPEAT REGIONS.
RX   PubMed=15518555; DOI=10.1021/bi049101q;
RA   Xu Y., Zhu J., Liu Y., Lou Z., Yuan F., Liu Y., Cole D.K., Ni L., Su N.,
RA   Qin L., Li X., Bai Z., Bell J.I., Pang H., Tien P., Gao G.F., Rao Z.;
RT   "Characterization of the heptad repeat regions, HR1 and HR2, and design of
RT   a fusion core structure model of the spike protein from severe acute
RT   respiratory syndrome (SARS) coronavirus.";
RL   Biochemistry 43:14064-14071(2004).
RN   [25]
RP   CLEAVAGE.
RX   PubMed=15450134; DOI=10.1038/sj.cr.7290240;
RA   Wu X.D., Shang B., Yang R.F., Yu H., Ma Z.H., Shen X., Ji Y.Y., Lin Y.,
RA   Wu Y.D., Lin G.M., Tian L., Gan X.Q., Yang S., Jiang W.H., Dai E.H.,
RA   Wang X.Y., Jiang H.L., Xie Y.H., Zhu X.L., Pei G., Li L., Wu J.R., Sun B.;
RT   "The spike protein of severe acute respiratory syndrome (SARS) is cleaved
RT   in virus infected Vero-E6 cells.";
RL   Cell Res. 14:400-406(2004).
RN   [26]
RP   FUNCTION, AND INTERACTION WITH HUMAN CLEC4M/DC-SIGNR.
RX   PubMed=15496474; DOI=10.1073/pnas.0403812101;
RA   Jeffers S.A., Tusell S.M., Gillim-Ross L., Hemmila E.M., Achenbach J.E.,
RA   Babcock G.J., Thomas W.D. Jr., Thackray L.B., Young M.D., Mason R.J.,
RA   Ambrosino D.M., Wentworth D.E., Demartini J.C., Holmes K.V.;
RT   "CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome
RT   coronavirus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15748-15753(2004).
RN   [27]
RP   HOMOTRIMERIZATION.
RX   PubMed=15313178; DOI=10.1016/j.bbrc.2004.07.084;
RA   Xiao X., Feng Y., Chakraborti S., Dimitrov D.S.;
RT   "Oligomerization of the SARS-CoV S glycoprotein: dimerization of the N-
RT   terminus and trimerization of the ectodomain.";
RL   Biochem. Biophys. Res. Commun. 322:93-99(2004).
RN   [28]
RP   CHARACTERIZATION OF FUSION PEPTIDE.
RX   PubMed=15890958; DOI=10.1128/jvi.79.11.7195-7206.2005;
RA   Sainz B. Jr., Rausch J.M., Gallaher W.R., Garry R.F., Wimley W.C.;
RT   "Identification and characterization of the putative fusion peptide of the
RT   severe acute respiratory syndrome-associated coronavirus spike protein.";
RL   J. Virol. 79:7195-7206(2005).
RN   [29]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15831954; DOI=10.1099/vir.0.80671-0;
RA   Nal B., Chan C., Kien F., Siu L., Tse J., Chu K., Kam J., Staropoli I.,
RA   Crescenzo-Chaigne B., Escriou N., van der Werf S., Yuen K.Y., Altmeyer R.;
RT   "Differential maturation and subcellular localization of severe acute
RT   respiratory syndrome coronavirus surface proteins S, M and E.";
RL   J. Gen. Virol. 86:1423-1434(2005).
RN   [30]
RP   CHARACTERIZATION OF VARIANTS ARG-344; SER-360; LYS-479 AND SER-487.
RX   PubMed=15791205; DOI=10.1038/sj.emboj.7600640;
RA   Li W., Zhang C., Sui J., Kuhn J.H., Moore M.J., Luo S., Wong S.-K.,
RA   Huang I.-C., Xu K., Vasilieva N., Murakami A., He Y., Marasco W.A.,
RA   Guan Y., Choe H., Farzan M.;
RT   "Receptor and viral determinants of SARS-coronavirus adaptation to human
RT   ACE2.";
RL   EMBO J. 24:1634-1643(2005).
RN   [31]
RP   PROTEOLYSIS BY HUMAN CTSL.
RX   PubMed=16081529; DOI=10.1073/pnas.0505577102;
RA   Simmons G., Gosalia D.N., Rennekamp A.J., Reeves J.D., Diamond S.L.,
RA   Bates P.;
RT   "Inhibitors of cathepsin L prevent severe acute respiratory syndrome
RT   coronavirus entry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11876-11881(2005).
RN   [32]
RP   INTERACTION WITH ACCESSORY PROTEIN 3A.
RX   PubMed=15194747; DOI=10.1128/jvi.78.13.6723-6734.2004;
RA   Tan Y.-J., Teng E., Shen S., Tan T.H.P., Goh P.-Y., Fielding B.C.,
RA   Ooi E.-E., Tan H.-C., Lim S.G., Hong W.;
RT   "A novel severe acute respiratory syndrome coronavirus protein, U274, is
RT   transported to the cell surface and undergoes endocytosis.";
RL   J. Virol. 78:6723-6734(2004).
RN   [33]
RP   INTERACTION WITH ACCESSORY PROTEIN 7A.
RX   PubMed=16840309; DOI=10.1128/jvi.00414-06;
RA   Huang C., Ito N., Tseng C.-T.K., Makino S.;
RT   "Severe acute respiratory syndrome coronavirus 7a accessory protein is a
RT   viral structural protein.";
RL   J. Virol. 80:7287-7294(2006).
RN   [34]
RP   MUTAGENESIS OF ARG-667 AND LYS-672.
RX   PubMed=16519916; DOI=10.1016/j.virol.2006.02.003;
RA   Follis K.E., York J., Nunberg J.H.;
RT   "Furin cleavage of the SARS coronavirus spike glycoprotein enhances cell-
RT   cell fusion but does not affect virion entry.";
RL   Virology 350:358-369(2006).
RN   [35]
RP   PALMITOYLATION.
RX   PubMed=17134730; DOI=10.1016/j.virol.2006.10.034;
RA   Petit C.M., Chouljenko V.N., Iyer A., Colgrove R., Farzan M., Knipe D.M.,
RA   Kousoulas K.G.;
RT   "Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus
RT   spike glycoprotein is important for spike-mediated cell fusion.";
RL   Virology 360:264-274(2007).
RN   [36]
RP   ENDOPLASMIC RETICULUM RETENTION MOTIF, AND MUTAGENESIS OF LYS-1251 AND
RP   HIS-1253.
RX   PubMed=17166901; DOI=10.1128/jvi.02146-06;
RA   McBride C.E., Li J., Machamer C.E.;
RT   "The cytoplasmic tail of the severe acute respiratory syndrome coronavirus
RT   spike protein contains a novel endoplasmic reticulum retrieval signal that
RT   binds COPI and promotes interaction with membrane protein.";
RL   J. Virol. 81:2418-2428(2007).
RN   [37]
RP   CLEAVAGE, AND FUNCTION.
RX   PubMed=19321428; DOI=10.1073/pnas.0809524106;
RA   Belouzard S., Chu V.C., Whittaker G.R.;
RT   "Activation of the SARS coronavirus spike protein via sequential
RT   proteolytic cleavage at two distinct sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5871-5876(2009).
RN   [38]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20861307; DOI=10.1091/mbc.e10-04-0338;
RA   Teoh K.T., Siu Y.L., Chan W.L., Schlueter M.A., Liu C.J., Peiris J.S.,
RA   Bruzzone R., Margolis B., Nal B.;
RT   "The SARS coronavirus E protein interacts with PALS1 and alters tight
RT   junction formation and epithelial morphogenesis.";
RL   Mol. Biol. Cell 21:3838-3852(2010).
RN   [39]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 900-948.
RX   PubMed=15345712; DOI=10.1074/jbc.m408782200;
RA   Xu Y., Lou Z., Liu Y., Pang H., Tien P., Gao G.F., Rao Z.;
RT   "Crystal structure of severe acute respiratory syndrome coronavirus spike
RT   protein fusion core.";
RL   J. Biol. Chem. 279:49414-49419(2004).
RN   [40]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 895-972 AND 1142-1180.
RX   PubMed=15604146; DOI=10.1073/pnas.0406128102;
RA   Supekar V.M., Bruckmann C., Ingallinella P., Bianchi E., Pessi A.,
RA   Carfi A.;
RT   "Structure of a proteolytically resistant core from the severe acute
RT   respiratory syndrome coronavirus S2 fusion protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:17958-17963(2004).
RN   [41]
RP   3D-STRUCTURE MODELING OF 17-680.
RX   PubMed=14511651; DOI=10.1016/j.bbrc.2003.08.122;
RA   Spiga O., Bernini A., Ciutti A., Chiellini S., Menciassi N., Finetti F.,
RA   Causarono V., Anselmi F., Prischi F., Niccolai N.;
RT   "Molecular modelling of S1 and S2 subunits of SARS coronavirus spike
RT   glycoprotein.";
RL   Biochem. Biophys. Res. Commun. 310:78-83(2003).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 323-502 IN COMPLEX WITH HUMAN
RP   ACE2.
RX   PubMed=16166518; DOI=10.1126/science.1116480;
RA   Li F., Li W., Farzan M., Harrison S.C.;
RT   "Structure of SARS coronavirus spike receptor-binding domain complexed with
RT   receptor.";
RL   Science 309:1864-1868(2005).
RN   [43]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1150-1193.
RX   PubMed=16698550; DOI=10.1016/j.str.2006.03.007;
RA   Deng Y., Liu J., Zheng Q., Yong W., Lu M.;
RT   "Structures and polymorphic interactions of two heptad-repeat regions of
RT   the SARS virus S2 protein.";
RL   Structure 14:889-899(2006).
CC   -!- FUNCTION: [Spike protein S1]: attaches the virion to the cell membrane
CC       by interacting with host receptor, initiating the infection (By
CC       similarity). Binding to human ACE2 and CLEC4M/DC-SIGNR receptors and
CC       internalization of the virus into the endosomes of the host cell
CC       induces conformational changes in the S glycoprotein. Proteolysis by
CC       cathepsin CTSL may unmask the fusion peptide of S2 and activate
CC       membranes fusion within endosomes. {ECO:0000255|HAMAP-Rule:MF_04099,
CC       ECO:0000269|PubMed:14670965, ECO:0000269|PubMed:15496474}.
CC   -!- FUNCTION: [Spike protein S2]: mediates fusion of the virion and
CC       cellular membranes by acting as a class I viral fusion protein. Under
CC       the current model, the protein has at least three conformational
CC       states: pre-fusion native state, pre-hairpin intermediate state, and
CC       post-fusion hairpin state. During viral and target cell membrane
CC       fusion, the coiled coil regions (heptad repeats) assume a trimer-of-
CC       hairpins structure, positioning the fusion peptide in close proximity
CC       to the C-terminal region of the ectodomain. The formation of this
CC       structure appears to drive apposition and subsequent fusion of viral
CC       and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is
CC       unmasked following S2 cleavage occurring upon virus endocytosis.
CC       {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:19321428}.
CC   -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit.
CC       The resulting peplomers protrude from the virus surface as spikes (By
CC       similarity). Binds to human and palm civet ACE2 and human CLEC4M/DC-
CC       SIGNR. Interacts with the accessory proteins 3a and 7a.
CC       {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:14647384,
CC       ECO:0000269|PubMed:14670965, ECO:0000269|PubMed:15194747,
CC       ECO:0000269|PubMed:15496474, ECO:0000269|PubMed:16166518,
CC       ECO:0000269|PubMed:16840309}.
CC   -!- INTERACTION:
CC       P59594; P59594: S; NbExp=10; IntAct=EBI-15582614, EBI-15582614;
CC       P59594; Q9BYF1: ACE2; Xeno; NbExp=7; IntAct=EBI-15582614, EBI-7730807;
CC       P59594; Q9BYF1-1: ACE2; Xeno; NbExp=2; IntAct=EBI-15582614, EBI-15814450;
CC       PRO_0000037209; Q9BYF1: ACE2; Xeno; NbExp=2; IntAct=EBI-25475261, EBI-7730807;
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099,
CC       ECO:0000269|PubMed:15831954}; Single-pass type I membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:15831954}. Host
CC       endoplasmic reticulum-Golgi intermediate compartment membrane
CC       {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:20861307}; Single-
CC       pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099,
CC       ECO:0000269|PubMed:15831954}. Host cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04099, ECO:0000269|PubMed:15831954}; Single-pass type I
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_04099,
CC       ECO:0000269|PubMed:15831954}. Note=Accumulates in the endoplasmic
CC       reticulum-Golgi intermediate compartment, where it participates in
CC       virus particle assembly. Colocalizes with S in the host endoplasmic
CC       reticulum-Golgi intermediate compartment (PubMed:20861307). Some S
CC       oligomers are transported to the host plasma membrane, where they may
CC       mediate cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099,
CC       ECO:0000269|PubMed:20861307}.
CC   -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval and binds
CC       COPI in vitro.
CC   -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
CC       glycoprotein is digested by cathepsin CTSL within endosomes.
CC       {ECO:0000269|PubMed:17134730}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC       precursor is processed into S1 and S2 by host cell furin or another
CC       cellular protease to yield the mature S1 and S2 proteins. Additionally,
CC       a second cleavage leads to the release of a fusion peptide after viral
CC       attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
CC       glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-
CC       Rule:MF_04099}.
CC   -!- MISCELLANEOUS: Tor2 is the prototype of the virus isolated during the
CC       severe SARS outbreak in 2002-2003. GD03 has been isolated from the
CC       second mild SARS outbreak in winter 2003-2004. SZ3 has been isolated
CC       from palm civet, the presumed animal reservoir. The spike proteins from
CC       those three isolates display a strong affinity for palm civet ACE2
CC       receptor, whereas only the Tor2 spike protein efficiently binds human
CC       ACE2. This may explain the high pathogenicity of Tor2 virus, whose
CC       spike is highly adapted to the human host. Therefore, the lack of
CC       severity of disease during the 2003-2004 outbreak could be due to the
CC       incomplete adaptation of GD03 virus to bind human ACE2. Mutation Asn-
CC       479 and Thr-487 in palm civet coronavirus seems necessary and
CC       sufficient for the virus to acquire the ability to efficiently infect
CC       humans.
CC   -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
DR   EMBL; AY278741; AAP13441.1; -; Genomic_RNA.
DR   EMBL; AY274119; AAP41037.1; -; Genomic_RNA.
DR   EMBL; AY282752; AAP30713.1; -; Genomic_RNA.
DR   EMBL; AY278554; AAP13567.1; -; Genomic_RNA.
DR   EMBL; AY278491; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY304495; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY304492; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY278487; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY278488; AAP30030.1; -; Genomic_RNA.
DR   EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY278489; AAP51227.1; -; Genomic_RNA.
DR   EMBL; AY283794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY283795; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY283796; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY283797; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY283798; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY291451; AAP37017.1; -; Genomic_RNA.
DR   EMBL; AY310120; AAP50485.1; -; Genomic_RNA.
DR   EMBL; AY291315; AAP33697.1; -; Genomic_RNA.
DR   EMBL; AY304486; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY321118; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY323976; AAP73417.1; -; mRNA.
DR   EMBL; AY322207; AAP82968.1; -; Genomic_RNA.
DR   EMBL; AY338174; AAQ01597.1; -; Genomic_RNA.
DR   EMBL; AY338175; AAQ01609.1; -; Genomic_RNA.
DR   EMBL; AY348314; AAP97882.1; -; Genomic_RNA.
DR   EMBL; AP006557; BAC81348.1; -; Genomic_RNA.
DR   EMBL; AP006558; BAC81362.1; -; Genomic_RNA.
DR   EMBL; AP006559; BAC81376.1; -; Genomic_RNA.
DR   EMBL; AP006560; BAC81390.1; -; Genomic_RNA.
DR   EMBL; AP006561; BAC81404.1; -; Genomic_RNA.
DR   EMBL; AY323977; AAP72986.1; -; Genomic_RNA.
DR   EMBL; AY362698; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY362699; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AY427439; AAQ94060.1; -; Genomic_RNA.
DR   EMBL; AY463059; AAR86788.1; -; Genomic_RNA.
DR   EMBL; AY525636; AAS10463.1; -; Genomic_RNA.
DR   RefSeq; NP_828851.1; NC_004718.3.
DR   PDB; 1Q4Z; Model; -; A=17-680.
DR   PDB; 1T7G; Model; -; A/C/E=17-680, B/D/F=737-1026.
DR   PDB; 1U4K; Model; -; D=764-1089.
DR   PDB; 1WNC; X-ray; 2.80 A; A/B/C/D/E/F=900-948, A/B/C/D/E/F=1144-1185.
DR   PDB; 1WYY; X-ray; 2.20 A; A/B=885-981, A/B=1145-1189.
DR   PDB; 1XJP; Model; -; A=17-680.
DR   PDB; 1ZV7; X-ray; 1.70 A; A/B=1150-1193.
DR   PDB; 1ZV8; X-ray; 1.94 A; A/C/E/G/I/K=901-950, B/D/F/H/J/L=1150-1185.
DR   PDB; 1ZVB; X-ray; 1.70 A; A/B/C=940-973.
DR   PDB; 2AJF; X-ray; 2.90 A; E/F=323-502.
DR   PDB; 2BEQ; X-ray; 1.60 A; A/B/C=914-949, D/E/F=1148-1193.
DR   PDB; 2BEZ; X-ray; 1.60 A; C=896-972, F=1142-1183.
DR   PDB; 2DD8; X-ray; 2.30 A; S=317-518.
DR   PDB; 2FXP; NMR; -; A/B/C=1141-1193.
DR   PDB; 2GHV; X-ray; 2.20 A; C/E=317-510.
DR   PDB; 2GHW; X-ray; 2.30 A; A/C=317-510.
DR   PDB; 2RUM; NMR; -; A=770-788.
DR   PDB; 2RUN; NMR; -; A=1185-1202.
DR   PDB; 2RUO; NMR; -; A=873-888.
DR   PDB; 3BGF; X-ray; 3.00 A; A/S=318-510.
DR   PDB; 3D0G; X-ray; 2.80 A; E/F=324-502.
DR   PDB; 3D0H; X-ray; 3.10 A; E/F=324-502.
DR   PDB; 3D0I; X-ray; 2.90 A; E/F=324-502.
DR   PDB; 3SCI; X-ray; 2.90 A; E/F=306-527.
DR   PDB; 3SCJ; X-ray; 3.00 A; E/F=323-502.
DR   PDB; 3SCK; X-ray; 3.00 A; E/F=324-502.
DR   PDB; 3SCL; X-ray; 3.00 A; E/F=324-502.
DR   PDB; 5WRG; EM; 4.30 A; A/B/C=1-1196.
DR   PDB; 5X4S; X-ray; 2.20 A; A=14-292.
DR   PDB; 5X58; EM; 3.20 A; A/B/C=14-1193.
DR   PDB; 5X5B; EM; 3.70 A; A/B/C=14-1193.
DR   PDB; 5XJK; NMR; -; A=758-821.
DR   PDB; 5XLR; EM; 3.80 A; A/B/C=1-1196.
DR   PDB; 5ZVM; X-ray; 3.30 A; A/B/C=892-970.
DR   PDB; 6ACC; EM; 3.60 A; A/B/C=1-1196.
DR   PDB; 6ACD; EM; 3.90 A; A/B/C=1-1196.
DR   PDB; 6ACG; EM; 5.40 A; A/B/C=1-1196.
DR   PDB; 6ACJ; EM; 4.20 A; A/B/C=1-1196.
DR   PDB; 6ACK; EM; 4.50 A; A/B/C=1-1196.
DR   PDB; 6CRV; EM; 3.20 A; A/B/C=14-1190.
DR   PDB; 6CRW; EM; 3.90 A; A/B/C=14-1190.
DR   PDB; 6CRX; EM; 3.90 A; A/B/C=14-1190.
DR   PDB; 6CRZ; EM; 3.30 A; A/B/C=14-1190.
DR   PDB; 6CS0; EM; 3.80 A; A/B/C=14-1190.
DR   PDB; 6CS1; EM; 4.60 A; A/B/C=14-1190.
DR   PDB; 6CS2; EM; 4.40 A; A/B/C=14-1190.
DR   PDB; 6NB6; EM; 4.20 A; A/B/C=14-1193.
DR   PDB; 6NB7; EM; 4.50 A; A/B/C=14-1193.
DR   PDBsum; 1Q4Z; -.
DR   PDBsum; 1T7G; -.
DR   PDBsum; 1U4K; -.
DR   PDBsum; 1WNC; -.
DR   PDBsum; 1WYY; -.
DR   PDBsum; 1XJP; -.
DR   PDBsum; 1ZV7; -.
DR   PDBsum; 1ZV8; -.
DR   PDBsum; 1ZVB; -.
DR   PDBsum; 2AJF; -.
DR   PDBsum; 2BEQ; -.
DR   PDBsum; 2BEZ; -.
DR   PDBsum; 2DD8; -.
DR   PDBsum; 2FXP; -.
DR   PDBsum; 2GHV; -.
DR   PDBsum; 2GHW; -.
DR   PDBsum; 2RUM; -.
DR   PDBsum; 2RUN; -.
DR   PDBsum; 2RUO; -.
DR   PDBsum; 3BGF; -.
DR   PDBsum; 3D0G; -.
DR   PDBsum; 3D0H; -.
DR   PDBsum; 3D0I; -.
DR   PDBsum; 3SCI; -.
DR   PDBsum; 3SCJ; -.
DR   PDBsum; 3SCK; -.
DR   PDBsum; 3SCL; -.
DR   PDBsum; 5WRG; -.
DR   PDBsum; 5X4S; -.
DR   PDBsum; 5X58; -.
DR   PDBsum; 5X5B; -.
DR   PDBsum; 5XJK; -.
DR   PDBsum; 5XLR; -.
DR   PDBsum; 5ZVM; -.
DR   PDBsum; 6ACC; -.
DR   PDBsum; 6ACD; -.
DR   PDBsum; 6ACG; -.
DR   PDBsum; 6ACJ; -.
DR   PDBsum; 6ACK; -.
DR   PDBsum; 6CRV; -.
DR   PDBsum; 6CRW; -.
DR   PDBsum; 6CRX; -.
DR   PDBsum; 6CRZ; -.
DR   PDBsum; 6CS0; -.
DR   PDBsum; 6CS1; -.
DR   PDBsum; 6CS2; -.
DR   PDBsum; 6NB6; -.
DR   PDBsum; 6NB7; -.
DR   SMR; P59594; -.
DR   ComplexPortal; CPX-5694; SARS-CoV Spike protein complex.
DR   DIP; DIP-29105N; -.
DR   IntAct; P59594; 5.
DR   PRIDE; P59594; -.
DR   ABCD; P59594; 16 sequenced antibodies.
DR   GeneID; 1489668; -.
DR   KEGG; vg:1489668; -.
DR   KO; K19254; -.
DR   EvolutionaryTrace; P59594; -.
DR   Proteomes; UP000000354; Genome.
DR   Proteomes; UP000103670; Genome.
DR   Proteomes; UP000109640; Genome.
DR   Proteomes; UP000116947; Genome.
DR   Proteomes; UP000121636; Genome.
DR   Proteomes; UP000131569; Genome.
DR   Proteomes; UP000131955; Genome.
DR   Proteomes; UP000137377; Genome.
DR   Proteomes; UP000138690; Genome.
DR   Proteomes; UP000143093; Genome.
DR   Proteomes; UP000145651; Genome.
DR   Proteomes; UP000146108; Genome.
DR   Proteomes; UP000146181; Genome.
DR   Proteomes; UP000146296; Genome.
DR   Proteomes; UP000148194; Genome.
DR   Proteomes; UP000153467; Genome.
DR   Proteomes; UP000160648; Genome.
DR   Proteomes; UP000164441; Genome.
DR   Proteomes; UP000172416; Genome.
DR   GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046789; F:host cell surface receptor binding; IPI:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-UniRule.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:BHF-UCL.
DR   Gene3D; 1.20.5.790; -; 1.
DR   HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
DR   InterPro; IPR042578; BETA_CORONA_SPIKE.
DR   InterPro; IPR002552; Corona_S2.
DR   InterPro; IPR027400; S_HR2.
DR   InterPro; IPR032500; Spike_N.
DR   InterPro; IPR018548; Spike_rcpt-bd.
DR   InterPro; IPR036326; Spike_rcpt-bd_sf.
DR   Pfam; PF01601; Corona_S2; 1.
DR   Pfam; PF16451; Spike_NTD; 1.
DR   Pfam; PF09408; Spike_rec_bind; 1.
DR   SUPFAM; SSF143587; SSF143587; 1.
DR   PROSITE; PS51921; BCOV_S1_CTD; 1.
DR   PROSITE; PS51922; BCOV_S1_NTD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virulence;
KW   Virus entry into host cell.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CHAIN           14..1255
FT                   /note="Spike glycoprotein"
FT                   /id="PRO_0000037208"
FT   CHAIN           14..667
FT                   /note="Spike protein S1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT                   /id="PRO_0000037209"
FT   CHAIN           668..1255
FT                   /note="Spike protein S2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT                   /id="PRO_0000037210"
FT   CHAIN           798..1255
FT                   /note="Spike protein S2'"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT                   /id="PRO_0000444082"
FT   TOPO_DOM        14..1195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   TRANSMEM        1196..1216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   TOPO_DOM        1217..1255
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   DOMAIN          14..290
FT                   /note="BetaCoV S1-NTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DOMAIN          321..513
FT                   /note="BetaCoV S1-CTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   REGION          306..527
FT                   /note="Receptor-binding domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          424..494
FT                   /note="Receptor-binding motif; binding to human ACE2"
FT   REGION          770..788
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          902..952
FT                   /note="Heptad repeat 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          1145..1184
FT                   /note="Heptad repeat 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COILED          931..975
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COILED          1157..1185
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   MOTIF           1251..1255
FT                   /note="KxHxx"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COMPBIAS        1217..1236
FT                   /note="Cys-rich"
FT   SITE            667..668
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:19321428"
FT   SITE            797..798
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:19321428"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        589
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        602
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        691
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        699
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        783
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1056
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1080
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1116
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1140
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1155
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1176
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   DISULFID        19..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        128..159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        278..288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        323..348
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        366..419
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        378..511
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT   DISULFID        467..474
FT   VARIANT         49
FT                   /note="S -> L (in strain: Isolate GZ50)"
FT   VARIANT         77
FT                   /note="G -> D (in strain: Isolate BJ01, Isolate BJ02,
FT                   Isolate BJ03, Isolate GZ50, Isolate CUHK-W1, Isolate HKU-
FT                   36871, Isolate GD01, Isolate GD03 and Isolate SZ3)"
FT   VARIANT         78
FT                   /note="N -> D (in strain: Isolate GD03)"
FT   VARIANT         118
FT                   /note="N -> S (in strain: Isolate Shanghai LY)"
FT   VARIANT         139
FT                   /note="A -> V (in strain: Isolate GD03)"
FT   VARIANT         144
FT                   /note="M -> L (in strain: Isolate BJ03)"
FT   VARIANT         147
FT                   /note="Q -> R (in strain: Isolate GD03)"
FT   VARIANT         193
FT                   /note="F -> S (in strain: Isolate Shanghai LY)"
FT   VARIANT         227
FT                   /note="N -> K (in strain: Isolate SZ3)"
FT   VARIANT         239
FT                   /note="S -> L (in strain: Isolate GD01 and Isolate SZ3)"
FT   VARIANT         244
FT                   /note="I -> T (in strain: Isolate BJ01, Isolate BJ02,
FT                   Isolate BJ03, Isolate BJ04, Isolate GZ50, Isolate CUHK-W1,
FT                   Isolate HKU-36871, Isolate GD01, Isolate GD03 and Isolate
FT                   SZ3)"
FT   VARIANT         261
FT                   /note="T -> K (in strain: Isolate SZ3)"
FT   VARIANT         311
FT                   /note="G -> R (in strain: Isolate GD01 and Isolate BJ02)"
FT   VARIANT         344
FT                   /note="K -> R (in strain: Isolate GD01, Isolate GD03 and
FT                   Isolate SZ3; no effect on affinity with either human or
FT                   palm civet ACE2)"
FT                   /evidence="ECO:0000269|PubMed:15791205"
FT   VARIANT         360
FT                   /note="F -> S (in strain: Isolate GD03 and Isolate SZ3; no
FT                   effect on affinity with either human or palm civet ACE2)"
FT                   /evidence="ECO:0000269|PubMed:15791205"
FT   VARIANT         426
FT                   /note="R -> G (in strain: Isolate Shanghai LY)"
FT   VARIANT         437
FT                   /note="N -> D (in strain: Isolate Shanghai LY)"
FT   VARIANT         472
FT                   /note="L -> P (in strain: Isolate GD03)"
FT   VARIANT         479
FT                   /note="N -> K (in strain: Isolate SZ3; 20fold decrease of
FT                   affinity with human ACE2; no effect on affinity with palm
FT                   civet ACE2)"
FT                   /evidence="ECO:0000269|PubMed:15791205"
FT   VARIANT         480
FT                   /note="D -> G (in strain: Isolate GD03)"
FT   VARIANT         487
FT                   /note="T -> S (in strain: Isolate GD03 and Isolate SZ3;
FT                   20fold decrease of affinity with human ACE2; decrease of
FT                   affinity with palm civet ACE2)"
FT                   /evidence="ECO:0000269|PubMed:15791205"
FT   VARIANT         501
FT                   /note="F -> Y (in strain: Isolate GD01)"
FT   VARIANT         577
FT                   /note="S -> A (in strain: Isolate Tor2 and Isolate Shanghai
FT                   QXC1)"
FT   VARIANT         605
FT                   /note="D -> N (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         607
FT                   /note="S -> P (in strain: Isolate SZ3)"
FT   VARIANT         608
FT                   /note="T -> A (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         609
FT                   /note="A -> L (in strain: Isolate GD03)"
FT   VARIANT         613
FT                   /note="D -> E (in strain: Isolate GD03)"
FT   VARIANT         665
FT                   /note="L -> S (in strain: Isolate GD03 and Isolate SZ3)"
FT   VARIANT         701
FT                   /note="S -> L (in strain: Isolate SZ3)"
FT   VARIANT         743
FT                   /note="T -> A (in strain: Isolate SZ3)"
FT   VARIANT         743
FT                   /note="T -> R (in strain: Isolate GD03)"
FT   VARIANT         754
FT                   /note="A -> V (in strain: Isolate SZ3)"
FT   VARIANT         765
FT                   /note="A -> V (in strain: Isolate GD03)"
FT   VARIANT         778
FT                   /note="Y -> D (in strain: Isolate GD01, Isolate GZ50,
FT                   Isolate GD03 and Isolate SZ3)"
FT   VARIANT         794
FT                   /note="P -> S (in strain: Isolate GD01)"
FT   VARIANT         804
FT                   /note="L -> P (in strain: Isolate Shanghai LY)"
FT   VARIANT         860..861
FT                   /note="VS -> LR (in strain: Isolate BJ03)"
FT   VARIANT         894
FT                   /note="T -> A (in strain: Isolate SZ3)"
FT   VARIANT         999
FT                   /note="E -> G (in strain: Isolate Shanghai LY)"
FT   VARIANT         1001
FT                   /note="R -> M (in strain: Isolate BJ04)"
FT   VARIANT         1132
FT                   /note="E -> G (in strain: Isolate Shanghai QXC1)"
FT   VARIANT         1148
FT                   /note="L -> F (in strain: Isolate Frankfurt 1 and Isolate
FT                   FRA)"
FT   VARIANT         1163
FT                   /note="K -> E (in strain: Isolate GD03 and Isolate SZ3)"
FT   MUTAGEN         323
FT                   /note="C->A: No effect on human ACE2 binding in vitro."
FT                   /evidence="ECO:0000269|PubMed:14670965"
FT   MUTAGEN         348
FT                   /note="C->A: Complete loss of human ACE2 binding in vitro."
FT                   /evidence="ECO:0000269|PubMed:14670965"
FT   MUTAGEN         452
FT                   /note="E->A: 90% loss of human ACE2 binding in vitro."
FT                   /evidence="ECO:0000269|PubMed:14670965"
FT   MUTAGEN         454
FT                   /note="D->A: Complete loss of human ACE2 binding in vitro."
FT                   /evidence="ECO:0000269|PubMed:14670965"
FT   MUTAGEN         463
FT                   /note="D->A: Partial loss of human ACE2 binding in vitro."
FT                   /evidence="ECO:0000269|PubMed:14670965"
FT   MUTAGEN         467
FT                   /note="C->A: Complete loss of human ACE2 binding in vitro."
FT                   /evidence="ECO:0000269|PubMed:14670965"
FT   MUTAGEN         474
FT                   /note="C->A: Complete loss of human ACE2 binding in vitro."
FT                   /evidence="ECO:0000269|PubMed:14670965"
FT   MUTAGEN         480
FT                   /note="D->A: No effect on human ACE2 binding in vitro."
FT                   /evidence="ECO:0000269|PubMed:14670965"
FT   MUTAGEN         667
FT                   /note="R->S: 40% loss of cell-cell fusion."
FT                   /evidence="ECO:0000269|PubMed:16519916"
FT   MUTAGEN         672
FT                   /note="K->S: No effect on cell-cell fusion."
FT                   /evidence="ECO:0000269|PubMed:16519916"
FT   MUTAGEN         797
FT                   /note="R->N: Complete loss of trypsin-induced membrane
FT                   fusion."
FT                   /evidence="ECO:0000269|PubMed:19321428"
FT   MUTAGEN         1251
FT                   /note="K->A: Decrease in Golgi localization, and complete
FT                   loss of COPI binding; when associated with A-1253."
FT                   /evidence="ECO:0000269|PubMed:17166901"
FT   MUTAGEN         1253
FT                   /note="H->A: Decrease in Golgi localization, and complete
FT                   loss of COPI binding; when associated with A-1251."
FT                   /evidence="ECO:0000269|PubMed:17166901"
FT   STRAND          31..34
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          37..41
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          44..48
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          50..59
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          65..72
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          73..75
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          87..95
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          100..111
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          113..118
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          123..141
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   TURN            142..144
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          146..164
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          177..190
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          193..208
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          216..222
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          229..239
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          250..256
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          258..266
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          268..270
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          272..277
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   TURN            282..288
FT                   /evidence="ECO:0000244|PDB:5X4S"
FT   STRAND          297..299
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          310..312
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           326..329
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   HELIX           337..339
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          341..345
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          347..349
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   HELIX           352..354
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          362..368
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   HELIX           371..378
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          380..390
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   HELIX           391..396
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          397..400
FT                   /evidence="ECO:0000244|PDB:3D0G"
FT   HELIX           404..408
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          414..416
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          418..424
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   HELIX           426..429
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          431..433
FT                   /evidence="ECO:0000244|PDB:2DD8"
FT   STRAND          439..441
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          462..464
FT                   /evidence="ECO:0000244|PDB:3D0I"
FT   STRAND          469..471
FT                   /evidence="ECO:0000244|PDB:2GHW"
FT   STRAND          478..480
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          483..487
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   HELIX           489..491
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          492..501
FT                   /evidence="ECO:0000244|PDB:2GHV"
FT   STRAND          509..511
FT                   /evidence="ECO:0000244|PDB:2DD8"
FT   STRAND          523..527
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          536..540
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          551..563
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   TURN            565..567
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          570..574
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          583..585
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   TURN            588..590
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          596..599
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           604..610
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   TURN            611..613
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          615..617
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   STRAND          628..631
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   STRAND          635..638
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          640..646
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   STRAND          649..653
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          656..659
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          675..678
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          682..685
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          691..698
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          704..710
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          716..718
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   HELIX           720..725
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           730..735
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           736..738
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          740..744
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           745..764
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          768..771
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           773..777
FT                   /evidence="ECO:0000244|PDB:2RUM"
FT   STRAND          778..781
FT                   /evidence="ECO:0000244|PDB:6CRZ"
FT   TURN            785..787
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   STRAND          790..792
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          794..797
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           799..806
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           813..817
FT                   /evidence="ECO:0000244|PDB:5XJK"
FT   STRAND          820..823
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   STRAND          832..834
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   STRAND          837..842
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   HELIX           849..865
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           869..872
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           880..891
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          898..900
FT                   /evidence="ECO:0000244|PDB:2BEZ"
FT   HELIX           915..948
FT                   /evidence="ECO:0000244|PDB:2BEQ"
FT   HELIX           959..963
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   TURN            964..969
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   HELIX           971..1013
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   TURN            1014..1016
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          1027..1032
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          1035..1038
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          1041..1048
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          1054..1059
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          1061..1063
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          1066..1068
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          1070..1074
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          1078..1080
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          1083..1086
FT                   /evidence="ECO:0000244|PDB:5X58"
FT   STRAND          1089..1091
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   STRAND          1101..1111
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   STRAND          1114..1116
FT                   /evidence="ECO:0000244|PDB:6CRV"
FT   HELIX           1148..1151
FT                   /evidence="ECO:0000244|PDB:2FXP"
FT   HELIX           1162..1172
FT                   /evidence="ECO:0000244|PDB:2BEQ"
FT   HELIX           1173..1178
FT                   /evidence="ECO:0000244|PDB:2BEQ"
FT   HELIX           1182..1192
FT                   /evidence="ECO:0000244|PDB:2BEQ"
SQ   SEQUENCE   1255 AA;  139125 MW;  1C49ACA2CFD38FC0 CRC64;
     MFIFLLFLTL TSGSDLDRCT TFDDVQAPNY TQHTSSMRGV YYPDEIFRSD TLYLTQDLFL
     PFYSNVTGFH TINHTFGNPV IPFKDGIYFA ATEKSNVVRG WVFGSTMNNK SQSVIIINNS
     TNVVIRACNF ELCDNPFFAV SKPMGTQTHT MIFDNAFNCT FEYISDAFSL DVSEKSGNFK
     HLREFVFKNK DGFLYVYKGY QPIDVVRDLP SGFNTLKPIF KLPLGINITN FRAILTAFSP
     AQDIWGTSAA AYFVGYLKPT TFMLKYDENG TITDAVDCSQ NPLAELKCSV KSFEIDKGIY
     QTSNFRVVPS GDVVRFPNIT NLCPFGEVFN ATKFPSVYAW ERKKISNCVA DYSVLYNSTF
     FSTFKCYGVS ATKLNDLCFS NVYADSFVVK GDDVRQIAPG QTGVIADYNY KLPDDFMGCV
     LAWNTRNIDA TSTGNYNYKY RYLRHGKLRP FERDISNVPF SPDGKPCTPP ALNCYWPLND
     YGFYTTTGIG YQPYRVVVLS FELLNAPATV CGPKLSTDLI KNQCVNFNFN GLTGTGVLTP
     SSKRFQPFQQ FGRDVSDFTD SVRDPKTSEI LDISPCSFGG VSVITPGTNA SSEVAVLYQD
     VNCTDVSTAI HADQLTPAWR IYSTGNNVFQ TQAGCLIGAE HVDTSYECDI PIGAGICASY
     HTVSLLRSTS QKSIVAYTMS LGADSSIAYS NNTIAIPTNF SISITTEVMP VSMAKTSVDC
     NMYICGDSTE CANLLLQYGS FCTQLNRALS GIAAEQDRNT REVFAQVKQM YKTPTLKYFG
     GFNFSQILPD PLKPTKRSFI EDLLFNKVTL ADAGFMKQYG ECLGDINARD LICAQKFNGL
     TVLPPLLTDD MIAAYTAALV SGTATAGWTF GAGAALQIPF AMQMAYRFNG IGVTQNVLYE
     NQKQIANQFN KAISQIQESL TTTSTALGKL QDVVNQNAQA LNTLVKQLSS NFGAISSVLN
     DILSRLDKVE AEVQIDRLIT GRLQSLQTYV TQQLIRAAEI RASANLAATK MSECVLGQSK
     RVDFCGKGYH LMSFPQAAPH GVVFLHVTYV PSQERNFTTA PAICHEGKAY FPREGVFVFN
     GTSWFITQRN FFSPQIITTD NTFVSGNCDV VIGIINNTVY DPLQPELDSF KEELDKYFKN
     HTSPDVDLGD ISGINASVVN IQKEIDRLNE VAKNLNESLI DLQELGKYEQ YIKWPWYVWL
     GFIAGLIAIV MVTILLCCMT SCCSCLKGAC SCGSCCKFDE DDSEPVLKGV KLHYT
//