ID   ITAL_HUMAN              Reviewed;        1170 AA.
AC   P20701; O43746; Q45H73; Q96HB1; Q9UBC8;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 3.
DT   12-AUG-2020, entry version 217.
DE   RecName: Full=Integrin alpha-L;
DE   AltName: Full=CD11 antigen-like family member A;
DE   AltName: Full=Leukocyte adhesion glycoprotein LFA-1 alpha chain;
DE            Short=LFA-1A;
DE   AltName: Full=Leukocyte function-associated molecule 1 alpha chain;
DE   AltName: CD_antigen=CD11a;
DE   Flags: Precursor;
GN   Name=ITGAL; Synonyms=CD11A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 120-132;
RP   226-237; 282-288; 433-441; 522-531; 569-582; 591-604; 831-844 AND 957-974,
RP   DOMAIN, AND VARIANT TRP-214.
RX   PubMed=2537322; DOI=10.1083/jcb.108.2.703;
RA   Larson R.S., Corbi A.L., Berman L., Springer T.;
RT   "Primary structure of the leukocyte function-associated molecule-1 alpha
RT   subunit: an integrin with an embedded domain defining a protein
RT   superfamily.";
RL   J. Cell Biol. 108:703-712(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-144; TRP-214; LYS-746
RP   AND THR-791.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2), AND VARIANT
RP   TRP-214.
RX   PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA   Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA   Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA   Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA   Adams M.D.;
RT   "Genome duplications and other features in 12 Mb of DNA sequence from human
RT   chromosome 16p and 16q.";
RL   Genomics 60:295-308(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX   PubMed=8099450; DOI=10.1073/pnas.90.11.5364;
RA   Shelley C.S., Farokhzad O.C., Arnaout M.A.;
RT   "Identification of cell-specific and developmentally regulated nuclear
RT   factors that direct myeloid and lymphoid expression of the CD11a gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5364-5368(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX   PubMed=8103515;
RA   Nueda A., Lopez-Cabrera M., Vara A., Corbi A.L.;
RT   "Characterization of the CD11a (alpha L, LFA-1 alpha) integrin gene
RT   promoter.";
RL   J. Biol. Chem. 268:19305-19311(1993).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX   PubMed=8097887; DOI=10.1073/pnas.90.9.4221;
RA   Cornwell R.D., Gollahon K.A., Hickstein D.D.;
RT   "Description of the leukocyte function-associated antigen 1 (LFA-1 or
RT   CD11a) promoter.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:4221-4225(1993).
RN   [10]
RP   FUNCTION.
RX   PubMed=11812992; DOI=10.1038/ni755;
RA   Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.;
RT   "JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in
RT   transendothelial migration of leukocytes.";
RL   Nat. Immunol. 3:151-158(2002).
RN   [11]
RP   FUNCTION.
RX   PubMed=15356110; DOI=10.4049/jimmunol.173.6.3653;
RA   Barber D.F., Faure M., Long E.O.;
RT   "LFA-1 contributes an early signal for NK cell cytotoxicity.";
RL   J. Immunol. 173:3653-3659(2004).
RN   [12]
RP   DOMAIN, AND FUNCTION.
RX   PubMed=15528364; DOI=10.4049/jimmunol.173.10.6259;
RA   Fraemohs L., Koenen R.R., Ostermann G., Heinemann B., Weber C.;
RT   "The functional interaction of the beta 2 integrin lymphocyte function-
RT   associated antigen-1 with junctional adhesion molecule-A is mediated by the
RT   I domain.";
RL   J. Immunol. 173:6259-6264(2004).
RN   [13]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1165, AND
RP   MUTAGENESIS OF SER-1165.
RX   PubMed=16301335; DOI=10.1083/jcb.200504016;
RA   Fagerholm S.C., Hilden T.J., Nurmi S.M., Gahmberg C.G.;
RT   "Specific integrin alpha and beta chain phosphorylations regulate LFA-1
RT   activation through affinity-dependent and -independent mechanisms.";
RL   J. Cell Biol. 171:705-715(2005).
RN   [14]
RP   INTERACTION WITH SARS-COV ORF7A PROTEIN (MICROBIAL INFECTION).
RX   PubMed=18020948; DOI=10.1515/bc.2007.157;
RA   Haenel K., Willbold D.;
RT   "SARS-CoV accessory protein 7a directly interacts with human LFA-1.";
RL   Biol. Chem. 388:1325-1332(2007).
RN   [15]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-188.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [16]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=23775590; DOI=10.1007/s10495-013-0873-z;
RA   Kristof E., Zahuczky G., Katona K., Doro Z., Nagy E., Fesues L.;
RT   "Novel role of ICAM3 and LFA-1 in the clearance of apoptotic neutrophils by
RT   human macrophages.";
RL   Apoptosis 18:1235-1251(2013).
RN   [17]
RP   INTERACTION WITH THBD.
RX   PubMed=27055590; DOI=10.1016/j.bbrc.2016.04.007;
RA   Kawamoto E., Okamoto T., Takagi Y., Honda G., Suzuki K., Imai H.,
RA   Shimaoka M.;
RT   "LFA-1 and Mac-1 integrins bind to the serine/threonine-rich domain of
RT   thrombomodulin.";
RL   Biochem. Biophys. Res. Commun. 473:1005-1012(2016).
RN   [18]
RP   FUNCTION.
RX   PubMed=29100055; DOI=10.1016/j.molcel.2017.10.003;
RA   Swaim C.D., Scott A.F., Canadeo L.A., Huibregtse J.M.;
RT   "Extracellular ISG15 signals cytokine secretion through the LFA-1 integrin
RT   receptor.";
RL   Mol. Cell 68:581-590(2017).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 153-335, AND SEQUENCE REVISION TO
RP   214.
RX   PubMed=7479767; DOI=10.1073/pnas.92.22.10277;
RA   Qu A., Leahy D.J.;
RT   "Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta
RT   2) integrin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:10277-10281(1995).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-335.
RX   PubMed=8805579; DOI=10.1016/s0969-2126(96)00100-1;
RA   Qu A., Leahy D.J.;
RT   "The role of the divalent cation in the structure of the I domain from the
RT   CD11a/CD18 integrin.";
RL   Structure 4:931-942(1996).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 153-334.
RX   PubMed=10493852; DOI=10.1006/jmbi.1999.3047;
RA   Kallen J., Welzenbach K., Ramage P., Geyl D., Kriwacki R., Legge G.,
RA   Cottens S., Weitz-Schmidt G., Hommel U.;
RT   "Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a
RT   I-domain.";
RL   J. Mol. Biol. 292:1-9(1999).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 155-331 IN COMPLEX WITH ICAM1.
RX   PubMed=12526797; DOI=10.1016/s0092-8674(02)01257-6;
RA   Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D., McCormack A.,
RA   Zhang R., Joachimiak A., Takagi J., Wang J.H., Springer T.A.;
RT   "Structures of the alpha L I domain and its complex with ICAM-1 reveal a
RT   shape-shifting pathway for integrin regulation.";
RL   Cell 112:99-111(2003).
CC   -!- FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3
CC       and ICAM4. Integrin ITGAL/ITGB2 is a receptor for F11R
CC       (PubMed:11812992, PubMed:15528364). Integin ITGAL/ITGB2 is a receptor
CC       for the secreted form of ubiquitin-like protein ISG15; the interaction
CC       is mediated by ITGAL (PubMed:29100055). Involved in a variety of immune
CC       phenomena including leukocyte-endothelial cell interaction, cytotoxic
CC       T-cell mediated killing, and antibody dependent killing by granulocytes
CC       and monocytes. Contributes to natural killer cell cytotoxicity
CC       (PubMed:15356110). Involved in leukocyte adhesion and transmigration of
CC       leukocytes including T-cells and neutrophils (PubMed:11812992).
CC       Required for generation of common lymphoid progenitor cells in bone
CC       marrow, indicating a role in lymphopoiesis (By similarity). Integrin
CC       ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic
CC       neutrophil phagocytosis by macrophages (PubMed:23775590).
CC       {ECO:0000250|UniProtKB:P24063, ECO:0000269|PubMed:11812992,
CC       ECO:0000269|PubMed:15356110, ECO:0000269|PubMed:15528364,
CC       ECO:0000269|PubMed:23775590, ECO:0000269|PubMed:29100055}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:12526797).
CC       The ITGAL alpha subunit associates with the ITGB2 beta subunit
CC       (PubMed:12526797). Interacts with THBD (PubMed:27055590).
CC       {ECO:0000269|PubMed:12526797, ECO:0000269|PubMed:27055590}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV Orf7a protein.
CC       {ECO:0000269|PubMed:18020948}.
CC   -!- INTERACTION:
CC       P20701; P05362: ICAM1; NbExp=2; IntAct=EBI-961214, EBI-1035358;
CC       P20701; P08575: PTPRC; NbExp=2; IntAct=EBI-961214, EBI-1341;
CC       P20701; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-961214, EBI-6863748;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16301335};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P20701-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P20701-2; Sequence=VSP_002738;
CC       Name=3;
CC         IsoId=P20701-3; Sequence=VSP_042842, VSP_042843;
CC   -!- TISSUE SPECIFICITY: Leukocytes. {ECO:0000269|PubMed:16301335,
CC       ECO:0000269|PubMed:23775590}.
CC   -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain
CC       (PubMed:2537322). Integrins with I-domains do not undergo protease
CC       cleavage. The I-domain is necessary and sufficient for interaction with
CC       ICAM1 and F11R (PubMed:15528364). {ECO:0000269|PubMed:15528364,
CC       ECO:0000269|PubMed:2537322}.
CC   -!- PTM: In resting T-cells, up to 40% of surface ITGAL is constitutively
CC       phosphorylated. Phosphorylation causes conformational changes needed
CC       for ligand binding and is necessary for activation by some
CC       physiological agents. {ECO:0000269|PubMed:16301335}.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/itgal/";
DR   EMBL; Y00796; CAA68747.1; -; mRNA.
DR   EMBL; DQ131904; AAZ38713.1; -; Genomic_DNA.
DR   EMBL; AC002310; AAC31672.1; -; Genomic_DNA.
DR   EMBL; AC116348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471192; EAW52243.1; -; Genomic_DNA.
DR   EMBL; BC008777; AAH08777.1; -; mRNA.
DR   EMBL; M95609; AAA16474.2; -; Genomic_DNA.
DR   EMBL; Z22804; CAA80461.1; -; Genomic_DNA.
DR   EMBL; M87662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS32433.1; -. [P20701-1]
DR   CCDS; CCDS45461.1; -. [P20701-3]
DR   PIR; S03308; S03308.
DR   RefSeq; NP_001107852.1; NM_001114380.1. [P20701-3]
DR   RefSeq; NP_002200.2; NM_002209.2. [P20701-1]
DR   PDB; 1CQP; X-ray; 2.60 A; A/B=153-334.
DR   PDB; 1DGQ; NMR; -; A=152-336.
DR   PDB; 1IJ4; Model; -; L=153-333.
DR   PDB; 1LFA; X-ray; 1.80 A; A/B=150-336.
DR   PDB; 1MJN; X-ray; 1.30 A; A=153-331.
DR   PDB; 1MQ8; X-ray; 3.30 A; B/D=155-331.
DR   PDB; 1MQ9; X-ray; 2.00 A; A=153-331.
DR   PDB; 1MQA; X-ray; 2.50 A; A=153-331.
DR   PDB; 1RD4; X-ray; 2.40 A; A/B/C/D=150-336.
DR   PDB; 1T0P; X-ray; 1.66 A; A=153-326.
DR   PDB; 1XDD; X-ray; 2.20 A; A/B=152-336.
DR   PDB; 1XDG; X-ray; 2.10 A; A/B=152-336.
DR   PDB; 1XUO; X-ray; 1.80 A; A/B=152-336.
DR   PDB; 1ZON; X-ray; 2.00 A; A=150-336.
DR   PDB; 1ZOO; X-ray; 3.00 A; A/B=150-336.
DR   PDB; 1ZOP; X-ray; 2.00 A; A/B=150-336.
DR   PDB; 2ICA; X-ray; 1.56 A; A=154-332.
DR   PDB; 2K8O; NMR; -; A=1113-1170.
DR   PDB; 2M3E; NMR; -; A=1082-1128.
DR   PDB; 2O7N; X-ray; 1.75 A; A=154-332.
DR   PDB; 3BN3; X-ray; 2.10 A; A=154-332.
DR   PDB; 3BQM; X-ray; 1.95 A; B/C=153-334.
DR   PDB; 3BQN; X-ray; 1.80 A; B/C=153-334.
DR   PDB; 3E2M; X-ray; 2.00 A; A/B=152-334.
DR   PDB; 3EOA; X-ray; 2.80 A; I/J=153-333.
DR   PDB; 3EOB; X-ray; 3.60 A; I/J=153-333.
DR   PDB; 3F74; X-ray; 1.70 A; A/B/C=153-332.
DR   PDB; 3F78; X-ray; 1.60 A; A/B/C=153-332.
DR   PDB; 3HI6; X-ray; 2.30 A; A/B=153-332.
DR   PDB; 3M6F; X-ray; 1.85 A; A=154-332.
DR   PDB; 3TCX; X-ray; 3.60 A; B/D/F/H/J/L/N/P/R/T/V/X/Z/b=154-332.
DR   PDB; 4IXD; X-ray; 1.80 A; A=152-336.
DR   PDB; 5E6R; X-ray; 2.90 A; A=26-770.
DR   PDB; 5E6S; X-ray; 2.15 A; A/C/E=26-770.
DR   PDB; 5E6U; X-ray; 2.50 A; A=26-770.
DR   PDB; 6BXB; X-ray; 2.39 A; A/B=153-331.
DR   PDB; 6BXF; X-ray; 3.20 A; A/B=153-331.
DR   PDB; 6BXJ; X-ray; 2.09 A; A=153-331.
DR   PDB; 6CKB; X-ray; 2.80 A; A/B=153-331.
DR   PDBsum; 1CQP; -.
DR   PDBsum; 1DGQ; -.
DR   PDBsum; 1IJ4; -.
DR   PDBsum; 1LFA; -.
DR   PDBsum; 1MJN; -.
DR   PDBsum; 1MQ8; -.
DR   PDBsum; 1MQ9; -.
DR   PDBsum; 1MQA; -.
DR   PDBsum; 1RD4; -.
DR   PDBsum; 1T0P; -.
DR   PDBsum; 1XDD; -.
DR   PDBsum; 1XDG; -.
DR   PDBsum; 1XUO; -.
DR   PDBsum; 1ZON; -.
DR   PDBsum; 1ZOO; -.
DR   PDBsum; 1ZOP; -.
DR   PDBsum; 2ICA; -.
DR   PDBsum; 2K8O; -.
DR   PDBsum; 2M3E; -.
DR   PDBsum; 2O7N; -.
DR   PDBsum; 3BN3; -.
DR   PDBsum; 3BQM; -.
DR   PDBsum; 3BQN; -.
DR   PDBsum; 3E2M; -.
DR   PDBsum; 3EOA; -.
DR   PDBsum; 3EOB; -.
DR   PDBsum; 3F74; -.
DR   PDBsum; 3F78; -.
DR   PDBsum; 3HI6; -.
DR   PDBsum; 3M6F; -.
DR   PDBsum; 3TCX; -.
DR   PDBsum; 4IXD; -.
DR   PDBsum; 5E6R; -.
DR   PDBsum; 5E6S; -.
DR   PDBsum; 5E6U; -.
DR   PDBsum; 6BXB; -.
DR   PDBsum; 6BXF; -.
DR   PDBsum; 6BXJ; -.
DR   PDBsum; 6CKB; -.
DR   SMR; P20701; -.
DR   BioGRID; 109889; 7.
DR   ComplexPortal; CPX-1825; Integrin alphaL-beta2 complex.
DR   DIP; DIP-623N; -.
DR   IntAct; P20701; 9.
DR   MINT; P20701; -.
DR   STRING; 9606.ENSP00000349252; -.
DR   BindingDB; P20701; -.
DR   ChEMBL; CHEMBL1803; -.
DR   DrugBank; DB04724; (S)-2-((S)-3-isobutyl-2,5-dioxo-4-quinolin-3-ylmethyl-[1,4]diazepan-1yl)-N-methyl-3-naphtalen-2-yl-propionamide.
DR   DrugBank; DB02177; 1-Acetyl-4-(4-{4-[(2-Ethoxyphenyl)Thio]-3-Nitrophenyl}Pyridin-2-Yl)Piperazine.
DR   DrugBank; DB07486; 3-({4-[(1E)-3-morpholin-4-yl-3-oxoprop-1-en-1-yl]-2,3-bis(trifluoromethyl)phenyl}sulfanyl)aniline.
DR   DrugBank; DB06972; 7A-[(4-cyanophenyl)methyl]-6-(3,5-dichlorophenyl)-5-oxo-2,3,5,7A-tetrahydro-1H-pyrrolo[1,2-A]pyrrole-7-carbonitrile.
DR   DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit).
DR   DrugBank; DB00095; Efalizumab.
DR   DrugBank; DB03932; LFA703.
DR   DrugBank; DB11611; Lifitegrast.
DR   DrugBank; DB00227; Lovastatin.
DR   DrugBank; DB08860; Pitavastatin.
DR   DrugBank; DB01098; Rosuvastatin.
DR   DrugBank; DB00641; Simvastatin.
DR   DrugCentral; P20701; -.
DR   GuidetoPHARMACOLOGY; 2451; -.
DR   GlyConnect; 1410; 9 N-Linked glycans (1 site).
DR   GlyGen; P20701; 12 sites.
DR   iPTMnet; P20701; -.
DR   PhosphoSitePlus; P20701; -.
DR   BioMuta; ITGAL; -.
DR   DMDM; 88911345; -.
DR   jPOST; P20701; -.
DR   MassIVE; P20701; -.
DR   MaxQB; P20701; -.
DR   PaxDb; P20701; -.
DR   PeptideAtlas; P20701; -.
DR   PRIDE; P20701; -.
DR   ProteomicsDB; 53774; -. [P20701-1]
DR   ProteomicsDB; 53775; -. [P20701-2]
DR   ProteomicsDB; 53776; -. [P20701-3]
DR   ABCD; P20701; 36 sequenced antibodies.
DR   Antibodypedia; 13698; 2051 antibodies.
DR   DNASU; 3683; -.
DR   Ensembl; ENST00000356798; ENSP00000349252; ENSG00000005844. [P20701-1]
DR   Ensembl; ENST00000358164; ENSP00000350886; ENSG00000005844. [P20701-3]
DR   GeneID; 3683; -.
DR   KEGG; hsa:3683; -.
DR   UCSC; uc002dyi.5; human. [P20701-1]
DR   CTD; 3683; -.
DR   DisGeNET; 3683; -.
DR   EuPathDB; HostDB:ENSG00000005844.17; -.
DR   GeneCards; ITGAL; -.
DR   HGNC; HGNC:6148; ITGAL.
DR   HPA; ENSG00000005844; Tissue enhanced (blood, lymphoid tissue).
DR   MIM; 153370; gene.
DR   neXtProt; NX_P20701; -.
DR   OpenTargets; ENSG00000005844; -.
DR   PharmGKB; PA29948; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   GeneTree; ENSGT00940000161495; -.
DR   HOGENOM; CLU_004111_3_0_1; -.
DR   InParanoid; P20701; -.
DR   KO; K05718; -.
DR   OMA; TVCFQLK; -.
DR   PhylomeDB; P20701; -.
DR   TreeFam; TF105391; -.
DR   PathwayCommons; P20701; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-8949275; RUNX3 Regulates Immune Response and Cell Migration.
DR   SignaLink; P20701; -.
DR   SIGNOR; P20701; -.
DR   BioGRID-ORCS; 3683; 9 hits in 871 CRISPR screens.
DR   ChiTaRS; ITGAL; human.
DR   EvolutionaryTrace; P20701; -.
DR   GeneWiki; CD11a; -.
DR   GenomeRNAi; 3683; -.
DR   Pharos; P20701; Tclin.
DR   PRO; PR:P20701; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P20701; protein.
DR   Bgee; ENSG00000005844; Expressed in granulocyte and 223 other tissues.
DR   ExpressionAtlas; P20701; baseline and differential.
DR   Genevisible; P20701; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0034687; C:integrin alphaL-beta2 complex; IDA:UniProtKB.
DR   GO; GO:0008305; C:integrin complex; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IMP:UniProtKB.
DR   GO; GO:0030369; F:ICAM-3 receptor activity; IMP:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; ISS:BHF-UCL.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:BHF-UCL.
DR   GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:ARUK-UCL.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0035683; P:memory T cell extravasation; IDA:ARUK-UCL.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0043113; P:receptor clustering; IMP:UniProtKB.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR   GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR   GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IMP:BHF-UCL.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.130; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR013649; Integrin_alpha-2.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF01839; FG-GAP; 1.
DR   Pfam; PF00357; Integrin_alpha; 1.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69179; SSF69179; 2.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Host-virus interaction; Integrin; Magnesium; Membrane; Metal-binding;
KW   Phagocytosis; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..1170
FT                   /note="Integrin alpha-L"
FT                   /id="PRO_0000016292"
FT   TOPO_DOM        26..1090
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1091..1111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1112..1170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          31..82
FT                   /note="FG-GAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          83..141
FT                   /note="FG-GAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   DOMAIN          156..327
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REPEAT          338..389
FT                   /note="FG-GAP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          390..445
FT                   /note="FG-GAP 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          446..506
FT                   /note="FG-GAP 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          507..563
FT                   /note="FG-GAP 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          567..627
FT                   /note="FG-GAP 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   CA_BIND         468..476
FT                   /evidence="ECO:0000255"
FT   CA_BIND         530..538
FT                   /evidence="ECO:0000255"
FT   CA_BIND         590..598
FT                   /evidence="ECO:0000255"
FT   MOTIF           1115..1119
FT                   /note="GFFKR motif"
FT   MOD_RES         1165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16301335"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        649
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        670
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        726
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        730
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        862
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        885
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        897
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1060
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1071
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        73..80
FT                   /evidence="ECO:0000250"
FT   DISULFID        111..129
FT                   /evidence="ECO:0000250"
FT   DISULFID        653..707
FT                   /evidence="ECO:0000250"
FT   DISULFID        771..777
FT                   /evidence="ECO:0000250"
FT   DISULFID        845..861
FT                   /evidence="ECO:0000250"
FT   DISULFID        998..1013
FT                   /evidence="ECO:0000250"
FT   DISULFID        1021..1052
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         110..192
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042842"
FT   VAR_SEQ         746
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042843"
FT   VAR_SEQ         954
FT                   /note="Q -> QGVHGLVEMQTSKQILCRPAGDAEHTVGAQEGELPCPWGVSEAFRDN
FT                   IRAGPCR (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002738"
FT   VARIANT         144
FT                   /note="R -> H (in dbSNP:rs34166708)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025235"
FT   VARIANT         214
FT                   /note="R -> W (in dbSNP:rs1064524)"
FT                   /evidence="ECO:0000269|PubMed:10493829,
FT                   ECO:0000269|PubMed:2537322, ECO:0000269|Ref.2"
FT                   /id="VAR_025236"
FT   VARIANT         746
FT                   /note="Q -> K (in dbSNP:rs34838942)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025237"
FT   VARIANT         791
FT                   /note="R -> T (in dbSNP:rs2230433)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_025238"
FT   MUTAGEN         1165
FT                   /note="S->A: Abolishes phosphorylation and MEM-83-activated
FT                   T-cell adhesion to ICAM1. Abolishes integrin alpha-L/beta-2
FT                   activation by CXCL12 and TERF2IP/RAP1. Does not affect
FT                   heterodimerization of cell surface expression. Does not
FT                   affect TCR- or phorbol ester-activated T-cell adhesion to
FT                   ICAM1."
FT                   /evidence="ECO:0000269|PubMed:16301335"
FT   CONFLICT        660
FT                   /note="I -> Y (in Ref. 1; CAA68747)"
FT                   /evidence="ECO:0000305"
FT   HELIX           30..32
FT                   /evidence="ECO:0000244|PDB:5E6U"
FT   STRAND          34..36
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   TURN            43..46
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          47..52
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          55..60
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          69..73
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   TURN            75..77
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          80..82
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   TURN            93..96
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          97..101
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   TURN            103..105
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          108..119
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          122..134
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          140..143
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          155..162
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           169..185
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   TURN            186..188
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   STRAND          189..206
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           208..214
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           217..221
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           233..243
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           247..249
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   STRAND          255..265
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           274..276
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   STRAND          279..287
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           288..290
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           293..297
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           298..302
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           307..310
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   STRAND          311..316
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           317..319
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   HELIX           323..330
FT                   /evidence="ECO:0000244|PDB:1MJN"
FT   STRAND          331..333
FT                   /evidence="ECO:0000244|PDB:3BQN"
FT   STRAND          352..359
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          362..367
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   HELIX           370..373
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          375..380
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          387..391
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   TURN            398..401
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          406..411
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          413..416
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          419..424
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   HELIX           427..429
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          432..437
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          446..452
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          462..467
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          472..474
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          477..482
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          493..499
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          501..510
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          514..516
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          523..527
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          531..535
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          539..543
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          549..554
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          558..561
FT                   /evidence="ECO:0000244|PDB:5E6R"
FT   STRAND          566..570
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   HELIX           571..574
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          583..589
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          593..595
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          598..603
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   STRAND          606..612
FT                   /evidence="ECO:0000244|PDB:5E6S"
FT   TURN            1082..1086
FT                   /evidence="ECO:0000244|PDB:2M3E"
FT   HELIX           1090..1114
FT                   /evidence="ECO:0000244|PDB:2M3E"
FT   HELIX           1118..1123
FT                   /evidence="ECO:0000244|PDB:2K8O"
FT   TURN            1124..1127
FT                   /evidence="ECO:0000244|PDB:2K8O"
FT   HELIX           1137..1147
FT                   /evidence="ECO:0000244|PDB:2K8O"
FT   HELIX           1153..1155
FT                   /evidence="ECO:0000244|PDB:2K8O"
FT   HELIX           1156..1165
FT                   /evidence="ECO:0000244|PDB:2K8O"
FT   HELIX           1167..1170
FT                   /evidence="ECO:0000244|PDB:2K8O"
SQ   SEQUENCE   1170 AA;  128770 MW;  22A7AF92EF286876 CRC64;
     MKDSCITVMA MALLSGFFFF APASSYNLDV RGARSFSPPR AGRHFGYRVL QVGNGVIVGA
     PGEGNSTGSL YQCQSGTGHC LPVTLRGSNY TSKYLGMTLA TDPTDGSILA CDPGLSRTCD
     QNTYLSGLCY LFRQNLQGPM LQGRPGFQEC IKGNVDLVFL FDGSMSLQPD EFQKILDFMK
     DVMKKLSNTS YQFAAVQFST SYKTEFDFSD YVKRKDPDAL LKHVKHMLLL TNTFGAINYV
     ATEVFREELG ARPDATKVLI IITDGEATDS GNIDAAKDII RYIIGIGKHF QTKESQETLH
     KFASKPASEF VKILDTFEKL KDLFTELQKK IYVIEGTSKQ DLTSFNMELS SSGISADLSR
     GHAVVGAVGA KDWAGGFLDL KADLQDDTFI GNEPLTPEVR AGYLGYTVTW LPSRQKTSLL
     ASGAPRYQHM GRVLLFQEPQ GGGHWSQVQT IHGTQIGSYF GGELCGVDVD QDGETELLLI
     GAPLFYGEQR GGRVFIYQRR QLGFEEVSEL QGDPGYPLGR FGEAITALTD INGDGLVDVA
     VGAPLEEQGA VYIFNGRHGG LSPQPSQRIE GTQVLSGIQW FGRSIHGVKD LEGDGLADVA
     VGAESQMIVL SSRPVVDMVT LMSFSPAEIP VHEVECSYST SNKMKEGVNI TICFQIKSLI
     PQFQGRLVAN LTYTLQLDGH RTRRRGLFPG GRHELRRNIA VTTSMSCTDF SFHFPVCVQD
     LISPINVSLN FSLWEEEGTP RDQRAQGKDI PPILRPSLHS ETWEIPFEKN CGEDKKCEAN
     LRVSFSPARS RALRLTAFAS LSVELSLSNL EEDAYWVQLD LHFPPGLSFR KVEMLKPHSQ
     IPVSCEELPE ESRLLSRALS CNVSSPIFKA GHSVALQMMF NTLVNSSWGD SVELHANVTC
     NNEDSDLLED NSATTIIPIL YPINILIQDQ EDSTLYVSFT PKGPKIHQVK HMYQVRIQPS
     IHDHNIPTLE AVVGVPQPPS EGPITHQWSV QMEPPVPCHY EDLERLPDAA EPCLPGALFR
     CPVVFRQEIL VQVIGTLELV GEIEASSMFS LCSSLSISFN SSKHFHLYGS NASLAQVVMK
     VDVVYEKQML YLYVLSGIGG LLLLLLIFIV LYKVGFFKRN LKEKMEAGRG VPNGIPAEDS
     EQLASGQEAG DPGCLKPLHE KDSESGGGKD
//