ID   SPIKE_SARS2             Reviewed;        1273 AA.
AC   P0DTC2;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   17-JUN-2020, entry version 2.
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   Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2).
OC   Viruses; Riboviria; Nidovirales; Cornidovirineae; Coronaviridae;
OC   Orthocoronavirinae; Betacoronavirus; Sarbecovirus.
OX   NCBI_TaxID=2697049;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=32015508; DOI=10.1038/s41586-020-2008-3;
RA   Wu F., Zhao S., Yu B., Chen Y.-M., Wang W., Song Z.-G., Hu Y., Tao Z.-W.,
RA   Tian J.-H., Pei Y.-Y., Yuan M.-L., Zhang Y.-L., Dai F.-H., Liu Y.,
RA   Wang Q.-M., Zheng J.-J., Xu L., Holmes E.C., Zhang Y.-Z.;
RT   "A new coronavirus associated with human respiratory disease in China.";
RL   Nature 579:265-269(2020).
RN   [2]
RP   FUNCTION (SPIKE PROTEIN S1).
RX   PubMed=32142651; DOI=10.1016/j.cell.2020.02.052;
RA   Hoffmann M., Kleine-Weber H., Schroeder S., Krueger N., Herrler T.,
RA   Erichsen S., Schiergens T.S., Herrler G., Wu N.H., Nitsche A.,
RA   Mueller M.A., Drosten C., Poehlmann S.;
RT   "SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a
RT   clinically proven protease inhibitor.";
RL   Cell 181:1-10(2020).
RN   [3] {ECO:0000244|PDB:6M17}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS), FUNCTION (SPIKE PROTEIN
RP   S1), DOMAIN, AND INTERACTION WITH HUMAN ACE2 (SPIKE PROTEIN S1).
RX   PubMed=32132184; DOI=10.1126/science.abb2762;
RA   Yan R., Zhang Y., Li Y., Xia L., Guo Y., Zhou Q.;
RT   "Structural basis for the recognition of the SARS-CoV-2 by full-length
RT   human ACE2.";
RL   Science 0:0-0(2020).
RN   [4] {ECO:0000244|PDB:6VSB}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.46 ANGSTROMS), FUNCTION (SPIKE PROTEIN
RP   S1), INTERACTION WITH HUMAN ACE2 (SPIKE PROTEIN S1), SUBUNIT, AND
RP   GLYCOSYLATION.
RX   PubMed=32075877; DOI=10.1126/science.abb2507;
RA   Wrapp D., Wang N., Corbett K.S., Goldsmith J.A., Hsieh C.L., Abiona O.,
RA   Graham B.S., McLellan J.S.;
RT   "Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.";
RL   Science 367:1260-1263(2020).
RN   [5] {ECO:0000244|PDB:6VXX, ECO:0000244|PDB:6VYB}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS), FUNCTION (SPIKE PROTEIN
RP   S1), SUBUNIT (SPIKE PROTEIN S1), INTERACTION WITH HUMAN ACE2 (SPIKE PROTEIN
RP   S1), MUTAGENESIS OF 679-GLN--ALA-684, GLYCOSYLATION AT ASN-61; ASN-122;
RP   ASN-61; ASN-165; ASN-234; ASN-282; ASN-331; ASN-343; ASN-603; ASN-616;
RP   ASN-657; ASN-709; ASN-717; ASN-801; ASN-1074; ASN-1098 AND ASN-1134, AND
RP   DISULFIDE BOND.
RX   PubMed=32155444; DOI=10.1016/j.cell.2020.02.058;
RA   Walls A.C., Park Y.J., Tortorici M.A., Wall A., McGuire A.T., Veesler D.;
RT   "Structure, function, and antigenicity of the SARS-CoV-2 spike
RT   glycoprotein.";
RL   Cell 180:1-12(2020).
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 receptor and internalization of the
CC       virus into the endosomes of the host cell induces conformational
CC       changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877,
CC       PubMed:32155444). Uses also human TMPRSS2 for priming in human lung
CC       cells which is an essential step for viral entry (PubMed:32142651).
CC       Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and
CC       activate membranes fusion within endosomes. {ECO:0000255|HAMAP-
CC       Rule:MF_04099, ECO:0000269|PubMed:32075877,
CC       ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32155444}.
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}.
CC   -!- SUBUNIT: [Spike glycoprotein]: Homotrimer; each monomer consists of a
CC       S1 and a S2 subunit (PubMed:32155444, PubMed:32075877). The resulting
CC       peplomers protrude from the virus surface as spikes (By similarity).
CC       Interacts with the accessory proteins 3a and 7a. {ECO:0000255|HAMAP-
CC       Rule:MF_04099, ECO:0000269|PubMed:32075877,
CC       ECO:0000269|PubMed:32155444}.
CC   -!- SUBUNIT: [Spike protein S1]: Binds to human ACE2.
CC       {ECO:0000269|PubMed:32075877, ECO:0000269|PubMed:32132184,
CC       ECO:0000269|PubMed:32155444, ECO:0000305}.
CC   -!- INTERACTION:
CC       P0DTC2; Q9BYF1: ACE2; Xeno; NbExp=11; IntAct=EBI-25474821, EBI-7730807;
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate
CC       compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass
CC       type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell
CC       membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the
CC       endoplasmic reticulum-Golgi intermediate compartment, where it
CC       participates in virus particle assembly. Colocalizes with S in the host
CC       endoplasmic reticulum-Golgi intermediate compartment. Some S oligomers
CC       are transported to the host plasma membrane, where they may mediate
CC       cell-cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC   -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval and binds
CC       COPI in vitro. {ECO:0000250|UniProtKB:P59594}.
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   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC       precurssor is processed into S1 and S2 by host cell furin or another
CC       cellular protease to yield the mature S1 and S2 proteins
CC       (PubMed:32155444). Additionally, a second cleavage leads to the release
CC       of a fusion peptide after viral attachment to host cell receptor (By
CC       similarity). The presence of a furin polybasic cleavage site sets SARS-
CC       CoV-2 S apart from SARS-CoV S that possesses a monobasic S1/S2 cleavage
CC       site processed upon entry of target cells (PubMed:32155444).
CC       {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444}.
CC   -!- PTM: Highly decorated by heterogeneous N-linked glycans protruding from
CC       the trimer surface. {ECO:0000269|PubMed:32075877,
CC       ECO:0000269|PubMed:32155444}.
CC   -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04099}.
DR   EMBL; MN908947; QHD43416.1; -; Genomic_RNA.
DR   PDB; 6LVN; X-ray; 2.47 A; A/B/C/D=1168-1203.
DR   PDB; 6LXT; X-ray; 2.90 A; A/B/C/D/E/F=910-988, A/B/C/D/E/F=1162-1206.
DR   PDB; 6M0J; X-ray; 2.45 A; E=319-541.
DR   PDB; 6M17; EM; 2.90 A; E/F=319-541.
DR   PDB; 6VSB; EM; 3.46 A; A/B/C=1-1208.
DR   PDB; 6VXX; EM; 2.80 A; A/B/C=14-1211.
DR   PDB; 6VYB; EM; 3.20 A; A/B/C=14-1211.
DR   PDB; 6W41; X-ray; 3.08 A; C=319-541.
DR   PDBsum; 6LVN; -.
DR   PDBsum; 6LXT; -.
DR   PDBsum; 6M0J; -.
DR   PDBsum; 6M17; -.
DR   PDBsum; 6VSB; -.
DR   PDBsum; 6VXX; -.
DR   PDBsum; 6VYB; -.
DR   PDBsum; 6W41; -.
DR   ComplexPortal; CPX-5682; SARS-CoV-2 Spike protein complex.
DR   IntAct; P0DTC2; 3.
DR   Proteomes; UP000464024; 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-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046789; F:host cell surface receptor binding; IDA:UniProtKB.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IDA:UniProtKB.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.790; -; 1.
DR   HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
DR   InterPro; IPR002552; Corona_S2.
DR   InterPro; IPR027400; S_HR2.
DR   InterPro; IPR018548; Spike_rcpt-bd.
DR   InterPro; IPR036326; Spike_rcpt-bd_sf.
DR   Pfam; PF16451; bCoV_S1_N; 1.
DR   Pfam; PF09408; bCoV_S1_RBD; 1.
DR   Pfam; PF19209; CoV_S1_C; 1.
DR   Pfam; PF01601; CoV_S2; 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..12
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CHAIN           13..1273
FT                   /note="Spike glycoprotein"
FT                   /id="PRO_0000449646"
FT   CHAIN           13..685
FT                   /note="Spike protein S1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT                   /id="PRO_0000449647"
FT   CHAIN           686..1273
FT                   /note="Spike protein S2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT                   /id="PRO_0000449648"
FT   CHAIN           816..1273
FT                   /note="Spike protein S2'"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT                   /id="PRO_0000449649"
FT   TOPO_DOM        13..1213
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   TRANSMEM        1214..1234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   TOPO_DOM        1235..1273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   DOMAIN          13..303
FT                   /note="BetaCoV S1-NTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DOMAIN          334..527
FT                   /note="BetaCoV S1-CTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269,
FT                   ECO:0000269|PubMed:32132184"
FT   REGION          319..541
FT                   /note="Receptor-binding domain (RBD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32132184"
FT   REGION          437..508
FT                   /note="Receptor-binding motif; binding to human ACE2"
FT                   /evidence="ECO:0000250|UniProtKB:P59594"
FT   REGION          788..806
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          920..970
FT                   /note="Heptad repeat 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   REGION          1163..1202
FT                   /note="Heptad repeat 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COILED          949..993
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   COILED          1176..1203
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   MOTIF           1269..1273
FT                   /note="KxHxx"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   SITE            685..686
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   SITE            815..816
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        603
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        616
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        657
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        709
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        717
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        801
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        1074
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        1098
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        1134
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099,
FT                   ECO:0000269|PubMed:32155444"
FT   CARBOHYD        1158
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1173
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   CARBOHYD        1194
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT   DISULFID        15..136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT   DISULFID        131..166
FT                   /evidence="ECO:0000244|PDB:6VXX, ECO:0000255|PROSITE-
FT                   ProRule:PRU01270, ECO:0000269|PubMed:32155444"
FT   DISULFID        291..301
FT                   /evidence="ECO:0000244|PDB:6VXX, ECO:0000255|PROSITE-
FT                   ProRule:PRU01270, ECO:0000269|PubMed:32155444"
FT   DISULFID        336..361
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269,
FT                   ECO:0000269|PubMed:32155444"
FT   DISULFID        379..432
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01269,
FT                   ECO:0000269|PubMed:32155444"
FT   DISULFID        391..525
FT                   /evidence="ECO:0000244|PDB:6VXX, ECO:0000255|PROSITE-
FT                   ProRule:PRU01269, ECO:0000269|PubMed:32155444"
FT   DISULFID        538..590
FT                   /evidence="ECO:0000244|PDB:6VXX,
FT                   ECO:0000269|PubMed:32155444"
FT   DISULFID        617..649
FT                   /evidence="ECO:0000244|PDB:6VXX,
FT                   ECO:0000269|PubMed:32155444"
FT   DISULFID        662..671
FT                   /evidence="ECO:0000244|PDB:6VXX,
FT                   ECO:0000269|PubMed:32155444"
FT   DISULFID        738..760
FT                   /evidence="ECO:0000244|PDB:6VXX,
FT                   ECO:0000269|PubMed:32155444"
FT   DISULFID        743..749
FT                   /evidence="ECO:0000244|PDB:6VXX,
FT                   ECO:0000269|PubMed:32155444"
FT   DISULFID        1032..1043
FT                   /evidence="ECO:0000244|PDB:6VXX,
FT                   ECO:0000269|PubMed:32155444"
FT   DISULFID        1082..1126
FT                   /evidence="ECO:0000244|PDB:6VXX,
FT                   ECO:0000269|PubMed:32155444"
FT   MUTAGEN         679..684
FT                   /note="NSPRRA->IL: About 50% stronger entry efficiency in
FT                   Vero E6 cells while 30% weaker entry efficiency in hACE2-
FT                   expressing BHK cells."
FT                   /evidence="ECO:0000269|PubMed:32155444"
SQ   SEQUENCE   1273 AA;  141178 MW;  B17BE6D9F1C4EA34 CRC64;
     MFVFLVLLPL VSSQCVNLTT RTQLPPAYTN SFTRGVYYPD KVFRSSVLHS TQDLFLPFFS
     NVTWFHAIHV SGTNGTKRFD NPVLPFNDGV YFASTEKSNI IRGWIFGTTL DSKTQSLLIV
     NNATNVVIKV CEFQFCNDPF LGVYYHKNNK SWMESEFRVY SSANNCTFEY VSQPFLMDLE
     GKQGNFKNLR EFVFKNIDGY FKIYSKHTPI NLVRDLPQGF SALEPLVDLP IGINITRFQT
     LLALHRSYLT PGDSSSGWTA GAAAYYVGYL QPRTFLLKYN ENGTITDAVD CALDPLSETK
     CTLKSFTVEK GIYQTSNFRV QPTESIVRFP NITNLCPFGE VFNATRFASV YAWNRKRISN
     CVADYSVLYN SASFSTFKCY GVSPTKLNDL CFTNVYADSF VIRGDEVRQI APGQTGKIAD
     YNYKLPDDFT GCVIAWNSNN LDSKVGGNYN YLYRLFRKSN LKPFERDIST EIYQAGSTPC
     NGVEGFNCYF PLQSYGFQPT NGVGYQPYRV VVLSFELLHA PATVCGPKKS TNLVKNKCVN
     FNFNGLTGTG VLTESNKKFL PFQQFGRDIA DTTDAVRDPQ TLEILDITPC SFGGVSVITP
     GTNTSNQVAV LYQDVNCTEV PVAIHADQLT PTWRVYSTGS NVFQTRAGCL IGAEHVNNSY
     ECDIPIGAGI CASYQTQTNS PRRARSVASQ SIIAYTMSLG AENSVAYSNN SIAIPTNFTI
     SVTTEILPVS MTKTSVDCTM YICGDSTECS NLLLQYGSFC TQLNRALTGI AVEQDKNTQE
     VFAQVKQIYK TPPIKDFGGF NFSQILPDPS KPSKRSFIED LLFNKVTLAD AGFIKQYGDC
     LGDIAARDLI CAQKFNGLTV LPPLLTDEMI AQYTSALLAG TITSGWTFGA GAALQIPFAM
     QMAYRFNGIG VTQNVLYENQ KLIANQFNSA IGKIQDSLSS TASALGKLQD VVNQNAQALN
     TLVKQLSSNF GAISSVLNDI LSRLDKVEAE VQIDRLITGR LQSLQTYVTQ QLIRAAEIRA
     SANLAATKMS ECVLGQSKRV DFCGKGYHLM SFPQSAPHGV VFLHVTYVPA QEKNFTTAPA
     ICHDGKAHFP REGVFVSNGT HWFVTQRNFY EPQIITTDNT FVSGNCDVVI GIVNNTVYDP
     LQPELDSFKE ELDKYFKNHT SPDVDLGDIS GINASVVNIQ KEIDRLNEVA KNLNESLIDL
     QELGKYEQYI KWPWYIWLGF IAGLIAIVMV TIMLCCMTSC CSCLKGCCSC GSCCKFDEDD
     SEPVLKGVKL HYT
//