ID   ITAE_HUMAN              Reviewed;        1179 AA.
AC   P38570; Q17RS6; Q9NZU9;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 3.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Integrin alpha-E;
DE   AltName: Full=HML-1 antigen;
DE   AltName: Full=Integrin alpha-IEL;
DE   AltName: Full=Mucosal lymphocyte 1 antigen;
DE   AltName: CD_antigen=CD103;
DE   Contains:
DE     RecName: Full=Integrin alpha-E light chain;
DE   Contains:
DE     RecName: Full=Integrin alpha-E heavy chain;
DE   Flags: Precursor;
GN   Name=ITGAE;
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], PROTEIN SEQUENCE OF 19-38 AND 179-188, AND
RP   VARIANTS VAL-477; GLN-482 AND ALA-1019.
RC   TISSUE=Leukemia, and Lymphocyte;
RX   PubMed=8119947; DOI=10.1016/s0021-9258(17)37563-4;
RA   Shaw S.K., Cepek K.L., Murphy E.A., Russell G.J., Brenner M.B.,
RA   Parker C.M.;
RT   "Molecular cloning of the human mucosal lymphocyte integrin alpha E
RT   subunit. Unusual structure and restricted RNA distribution.";
RL   J. Biol. Chem. 269:6016-6025(1994).
RN   [2]
RP   SEQUENCE REVISION TO 88-114.
RA   Parker C.M.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-477; GLN-482 AND
RP   ALA-1019.
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-1179, AND VARIANT TRP-950.
RC   TISSUE=Fetal kidney;
RX   PubMed=10673275; DOI=10.1101/gr.10.2.165;
RA   Touchman J.W., Anikster Y., Dietrich N.L., Maduro V.V.B., McDowell G.,
RA   Shotelersuk V., Bouffard G.G., Beckstrom-Sternberg S.M., Gahl W.A.,
RA   Green E.D.;
RT   "The genomic region encompassing the nephropathic cystinosis gene (CTNS):
RT   complete sequencing of a 200-kb segment and discovery of a novel gene
RT   within the common cystinosis-causing deletion.";
RL   Genome Res. 10:165-173(2000).
RN   [6]
RP   INTERACTION WITH INTEGRIN BETA-7, AND INDUCTION.
RX   PubMed=1542691; DOI=10.1073/pnas.89.5.1924;
RA   Parker C.M., Cepek K.L., Russell G.J., Shaw S.K., Posnett D.N.,
RA   Schwarting R., Brenner M.B.;
RT   "A family of beta 7 integrins on human mucosal lymphocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:1924-1928(1992).
RN   [7]
RP   MUTAGENESIS OF ASP-208 AND PHE-316.
RX   PubMed=10837471; DOI=10.1074/jbc.m001228200;
RA   Higgins J.M.G., Cernadas M., Tan K., Irie A., Wang J.-H., Takada Y.,
RA   Brenner M.B.;
RT   "The role of alpha and beta chains in ligand recognition by beta 7
RT   integrins.";
RL   J. Biol. Chem. 275:25652-25664(2000).
CC   -!- FUNCTION: Integrin alpha-E/beta-7 is a receptor for E-cadherin. It
CC       mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell
CC       monolayers.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC       is composed of a heavy and a light chains linked by a disulfide bond.
CC       Alpha-E associates with beta-7.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed on a subclass of T-lymphocytes known as
CC       intra-epithelial lymphocytes which are located between mucosal
CC       epithelial cells.
CC   -!- INDUCTION: Integrin alpha-E/beta-7 is induced by TGFB1.
CC       {ECO:0000269|PubMed:1542691}.
CC   -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC       I-domains do not undergo protease cleavage.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR   EMBL; L25851; AAB59359.2; -; mRNA.
DR   EMBL; AC116914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC113436; AAI13437.1; -; mRNA.
DR   EMBL; BC117207; AAI17208.1; -; mRNA.
DR   EMBL; AF168787; AAF43107.1; -; Genomic_DNA.
DR   CCDS; CCDS32531.1; -.
DR   PIR; A53213; A53213.
DR   RefSeq; NP_002199.3; NM_002208.4.
DR   AlphaFoldDB; P38570; -.
DR   SMR; P38570; -.
DR   BioGRID; 109888; 6.
DR   ComplexPortal; CPX-1824; Integrin alphaE-beta7 complex.
DR   CORUM; P38570; -.
DR   IntAct; P38570; 2.
DR   STRING; 9606.ENSP00000263087; -.
DR   GlyCosmos; P38570; 11 sites, No reported glycans.
DR   GlyGen; P38570; 11 sites.
DR   iPTMnet; P38570; -.
DR   PhosphoSitePlus; P38570; -.
DR   BioMuta; ITGAE; -.
DR   DMDM; 226694184; -.
DR   CPTAC; CPTAC-5961; -.
DR   EPD; P38570; -.
DR   jPOST; P38570; -.
DR   MassIVE; P38570; -.
DR   PaxDb; 9606-ENSP00000263087; -.
DR   PeptideAtlas; P38570; -.
DR   ProteomicsDB; 55300; -.
DR   Antibodypedia; 10997; 1270 antibodies from 44 providers.
DR   CPTC; P38570; 1 antibody.
DR   DNASU; 3682; -.
DR   Ensembl; ENST00000263087.9; ENSP00000263087.4; ENSG00000083457.12.
DR   GeneID; 3682; -.
DR   KEGG; hsa:3682; -.
DR   MANE-Select; ENST00000263087.9; ENSP00000263087.4; NM_002208.5; NP_002199.3.
DR   UCSC; uc002fwo.5; human.
DR   AGR; HGNC:6147; -.
DR   CTD; 3682; -.
DR   DisGeNET; 3682; -.
DR   GeneCards; ITGAE; -.
DR   HGNC; HGNC:6147; ITGAE.
DR   HPA; ENSG00000083457; Tissue enhanced (bone marrow, intestine, lung).
DR   MIM; 604682; gene.
DR   neXtProt; NX_P38570; -.
DR   OpenTargets; ENSG00000083457; -.
DR   PharmGKB; PA29947; -.
DR   VEuPathDB; HostDB:ENSG00000083457; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   GeneTree; ENSGT00940000161532; -.
DR   HOGENOM; CLU_004111_0_0_1; -.
DR   InParanoid; P38570; -.
DR   OMA; FKRMQKP; -.
DR   OrthoDB; 3816176at2759; -.
DR   PhylomeDB; P38570; -.
DR   TreeFam; TF105391; -.
DR   PathwayCommons; P38570; -.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   SignaLink; P38570; -.
DR   SIGNOR; P38570; -.
DR   BioGRID-ORCS; 3682; 9 hits in 1163 CRISPR screens.
DR   ChiTaRS; ITGAE; human.
DR   GeneWiki; ITGAE; -.
DR   GenomeRNAi; 3682; -.
DR   Pharos; P38570; Tbio.
DR   PRO; PR:P38570; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P38570; Protein.
DR   Bgee; ENSG00000083457; Expressed in oocyte and 208 other cell types or tissues.
DR   ExpressionAtlas; P38570; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   CDD; cd01469; vWA_integrins_alpha_subunit; 1.
DR   Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 2.
DR   Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR   Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF79; INTEGRIN ALPHA-E; 1.
DR   Pfam; PF01839; FG-GAP; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF00357; Integrin_alpha; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00191; Int_alpha; 4.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 2.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS51470; FG_GAP; 5.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   PROSITE; PS50234; VWFA; 1.
DR   Genevisible; P38570; HS.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Integrin;
KW   Magnesium; Membrane; Metal-binding; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:8119947"
FT   CHAIN           19..1179
FT                   /note="Integrin alpha-E"
FT                   /id="PRO_0000016283"
FT   CHAIN           19..177
FT                   /note="Integrin alpha-E light chain"
FT                   /id="PRO_0000016284"
FT   CHAIN           179..1177
FT                   /note="Integrin alpha-E heavy chain"
FT                   /id="PRO_0000016285"
FT   TOPO_DOM        19..1124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1125..1147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1148..1179
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          22..79
FT                   /note="FG-GAP 1"
FT   REPEAT          80..138
FT                   /note="FG-GAP 2"
FT   DOMAIN          200..389
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REPEAT          390..442
FT                   /note="FG-GAP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          447..499
FT                   /note="FG-GAP 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          500..560
FT                   /note="FG-GAP 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          563..627
FT                   /note="FG-GAP 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          631..691
FT                   /note="FG-GAP 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REGION          145..199
FT                   /note="X-domain (extra domain)"
FT   REGION          158..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1150..1154
FT                   /note="GFFKR motif"
FT   COMPBIAS        158..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..200
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         522
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         524
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         526
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         530
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         586
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         588
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         590
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         594
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         654
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         656
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         658
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   BINDING         662
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P08648"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        444
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        782
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        857
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        934
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        954
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1065
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1096
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        70..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        126..159
FT                   /evidence="ECO:0000250"
FT   DISULFID        706..762
FT                   /evidence="ECO:0000250"
FT   DISULFID        823..829
FT                   /evidence="ECO:0000250"
FT   DISULFID        893..907
FT                   /evidence="ECO:0000250"
FT   DISULFID        1008..1033
FT                   /evidence="ECO:0000250"
FT   DISULFID        1041..1057
FT                   /evidence="ECO:0000250"
FT   VARIANT         360
FT                   /note="D -> E"
FT                   /id="VAR_008884"
FT   VARIANT         477
FT                   /note="I -> V (in dbSNP:rs220479)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:8119947"
FT                   /id="VAR_054889"
FT   VARIANT         482
FT                   /note="R -> Q (in dbSNP:rs2272606)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:8119947"
FT                   /id="VAR_054890"
FT   VARIANT         892
FT                   /note="Q -> H (in dbSNP:rs3744679)"
FT                   /id="VAR_020037"
FT   VARIANT         950
FT                   /note="R -> W (in dbSNP:rs1716)"
FT                   /evidence="ECO:0000269|PubMed:10673275"
FT                   /id="VAR_034025"
FT   VARIANT         1019
FT                   /note="V -> A (in dbSNP:rs2976230)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:8119947"
FT                   /id="VAR_054891"
FT   VARIANT         1041
FT                   /note="C -> S"
FT                   /id="VAR_008885"
FT   MUTAGEN         208
FT                   /note="D->A: Loss of E-cadherin binding."
FT                   /evidence="ECO:0000269|PubMed:10837471"
FT   MUTAGEN         316
FT                   /note="F->A: Loss of E-cadherin binding."
FT                   /evidence="ECO:0000269|PubMed:10837471"
SQ   SEQUENCE   1179 AA;  130159 MW;  6645F8FFF9A0F045 CRC64;
     MWLFHTLLCI ASLALLAAFN VDVARPWLTP KGGAPFVLSS LLHQDPSTNQ TWLLVTSPRT
     KRTPGPLHRC SLVQDEILCH PVEHVPIPKG RHRGVTVVRS HHGVLICIQV LVRRPHSLSS
     ELTGTCSLLG PDLRPQAQAN FFDLENLLDP DARVDTGDCY SNKEGGGEDD VNTARQRRAL
     EKEEEEDKEE EEDEEEEEAG TEIAIILDGS GSIDPPDFQR AKDFISNMMR NFYEKCFECN
     FALVQYGGVI QTEFDLRDSQ DVMASLARVQ NITQVGSVTK TASAMQHVLD SIFTSSHGSR
     RKASKVMVVL TDGGIFEDPL NLTTVINSPK MQGVERFAIG VGEEFKSART ARELNLIASD
     PDETHAFKVT NYMALDGLLS KLRYNIISME GTVGDALHYQ LAQIGFSAQI LDERQVLLGA
     VGAFDWSGGA LLYDTRSRRG RFLNQTAAAA ADAEAAQYSY LGYAVAVLHK TCSLSYIAGA
     PRYKHHGAVF ELQKEGREAS FLPVLEGEQM GSYFGSELCP VDIDMDGSTD FLLVAAPFYH
     VHGEEGRVYV YRLSEQDGSF SLARILSGHP GFTNARFGFA MAAMGDLSQD KLTDVAIGAP
     LEGFGADDGA SFGSVYIYNG HWDGLSASPS QRIRASTVAP GLQYFGMSMA GGFDISGDGL
     ADITVGTLGQ AVVFRSRPVV RLKVSMAFTP SALPIGFNGV VNVRLCFEIS SVTTASESGL
     REALLNFTLD VDVGKQRRRL QCSDVRSCLG CLREWSSGSQ LCEDLLLMPT EGELCEEDCF
     SNASVKVSYQ LQTPEGQTDH PQPILDRYTE PFAIFQLPYE KACKNKLFCV AELQLATTVS
     QQELVVGLTK ELTLNINLTN SGEDSYMTSM ALNYPRNLQL KRMQKPPSPN IQCDDPQPVA
     SVLIMNCRIG HPVLKRSSAH VSVVWQLEEN AFPNRTADIT VTVTNSNERR SLANETHTLQ
     FRHGFVAVLS KPSIMYVNTG QGLSHHKEFL FHVHGENLFG AEYQLQICVP TKLRGLQVVA
     VKKLTRTQAS TVCTWSQERA CAYSSVQHVE EWHSVSCVIA SDKENVTVAA EISWDHSEEL
     LKDVTELQIL GEISFNKSLY EGLNAENHRT KITVVFLKDE KYHSLPIIIK GSVGGLLVLI
     VILVILFKCG FFKRKYQQLN LESIRKAQLK SENLLEEEN
//