ID ITA9_HUMAN Reviewed; 1035 AA. AC Q13797; Q14638; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 24-JAN-2024, entry version 183. DE RecName: Full=Integrin alpha-9; DE AltName: Full=Integrin alpha-RLC; DE Flags: Precursor; GN Name=ITGA9; 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], VARIANT GLU-507, AND DEVELOPMENTAL STAGE. RC TISSUE=Lung; RX PubMed=8290272; RA Hibi K., Yamakawa K., Ueda R., Horio Y., Murata Y., Tamari M., Uchida K., RA Takahashi T., Nakamura Y., Takahashi T.; RT "Aberrant upregulation of a novel integrin alpha subunit gene at 3p21.3 in RT small cell lung cancer."; RL Oncogene 9:611-619(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-1035, PROTEIN SEQUENCE OF 30-35, VARIANT RP GLU-507, AND TISSUE SPECIFICITY. RC TISSUE=Intestine, and Lung; RX PubMed=8245132; DOI=10.1083/jcb.123.5.1289; RA Palmer E.L., Rueegg C., Ferrando R., Pytela R., Sheppard D.; RT "Sequence and tissue distribution of the integrin alpha 9 subunit, a novel RT partner of beta 1 that is widely distributed in epithelia and muscle."; RL J. Cell Biol. 123:1289-1297(1993). RN [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [5] RP VARIANT [LARGE SCALE ANALYSIS] CYS-750. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [6] RP INTERACTION WITH TNC. RX PubMed=22654117; DOI=10.1074/jbc.m112.355016; RA Sato-Nishiuchi R., Nakano I., Ozawa A., Sato Y., Takeichi M., Kiyozumi D., RA Yamazaki K., Yasunaga T., Futaki S., Sekiguchi K.; RT "Polydom/SVEP1 is a ligand for integrin alpha9beta1."; RL J. Biol. Chem. 287:25615-25630(2012). RN [7] RP FUNCTION, INTERACTION WITH SVEP1, AND TISSUE SPECIFICITY. RX PubMed=35802072; DOI=10.1111/bph.15921; RA Morris G.E., Denniff M.J., Karamanavi E., Andrews S.A., Kostogrys R.B., RA Bountziouka V., Ghaderi-Najafabadi M., Shamkhi N., McConnell G., RA Kaiser M.A., Carleton L., Schofield C., Kessler T., Rainbow R.D., RA Samani N.J., Webb T.R.; RT "The integrin ligand SVEP1 regulates GPCR-mediated vasoconstriction via RT integrins alpha9beta1 and alpha4beta1."; RL Br. J. Pharmacol. 179:4958-4973(2022). CC -!- FUNCTION: Integrin alpha-9/beta-1 (ITGA9:ITGB1) is a receptor for CC VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D- CC G-I-E-L in cytotactin. ITGA9:ITGB1 may play a crucial role in CC SVEP1/polydom-mediated myoblast cell adhesion (By similarity). Integrin CC ITGA9:ITGB1 represses PRKCA-mediated L-type voltage-gated channel CC Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth CC muscle cells via its interaction with SVEP1, thereby inhibiting CC vasocontraction (PubMed:35802072). {ECO:0000250, CC ECO:0000250|UniProtKB:B8JK39, ECO:0000269|PubMed:35802072}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-9 (ITGA9) CC associates with beta-1 (ITGB1). Integrin ITGA9:ITGB1 interacts with CC FBLN5 (via N-terminus). Integrin ITGA9:ITGB1 interacts with SPP1/OPN CC (via N-terminus) (By similarity). Integrin ITGA9:ITGB1 interacts with CC TNC/TNFN3 (via the 3rd Fibronectin type-III domain) (PubMed:22654117). CC Integrin ITGA9:ITGB1 interacts with SVEP1/polydom (via Sushi domain CC 21); thereby inhibits Ca(2+) intracellular signaling and as a result CC represses vasocontraction (PubMed:35802072). {ECO:0000250, CC ECO:0000250|UniProtKB:B8JK39, ECO:0000269|PubMed:22654117, CC ECO:0000269|PubMed:35802072}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I CC membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Expressed in vascular smooth muscle cells (at CC protein level) (PubMed:35802072). Expressed in the airway epithelium CC (at protein level) (PubMed:8245132). {ECO:0000269|PubMed:35802072, CC ECO:0000269|PubMed:8245132}. CC -!- DEVELOPMENTAL STAGE: Abundantly expressed in the fetal lung. CC {ECO:0000269|PubMed:8290272}. CC -!- MISCELLANEOUS: Expression is increased in small cell lung cancers CC (SCLC). {ECO:0000269|PubMed:8290272}. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D25303; BAA04984.1; -; mRNA. DR EMBL; AC092055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093415; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP006240; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L24158; AAA16099.1; -; mRNA. DR CCDS; CCDS2669.1; -. DR PIR; I58409; I58409. DR RefSeq; NP_002198.2; NM_002207.2. DR AlphaFoldDB; Q13797; -. DR SMR; Q13797; -. DR BioGRID; 109886; 32. DR ComplexPortal; CPX-1816; Integrin alpha9-beta1 complex. DR CORUM; Q13797; -. DR IntAct; Q13797; 1. DR STRING; 9606.ENSP00000264741; -. DR ChEMBL; CHEMBL3170; -. DR GuidetoPHARMACOLOGY; 2448; -. DR GlyCosmos; Q13797; 11 sites, No reported glycans. DR GlyGen; Q13797; 11 sites. DR iPTMnet; Q13797; -. DR PhosphoSitePlus; Q13797; -. DR BioMuta; ITGA9; -. DR DMDM; 229462922; -. DR CPTAC; CPTAC-1492; -. DR EPD; Q13797; -. DR jPOST; Q13797; -. DR MassIVE; Q13797; -. DR PaxDb; 9606-ENSP00000264741; -. DR PeptideAtlas; Q13797; -. DR ProteomicsDB; 59688; -. DR ABCD; Q13797; 3 sequenced antibodies. DR Antibodypedia; 11893; 249 antibodies from 32 providers. DR DNASU; 3680; -. DR Ensembl; ENST00000264741.10; ENSP00000264741.5; ENSG00000144668.12. DR Ensembl; ENST00000707666.1; ENSP00000516955.1; ENSG00000291488.1. DR GeneID; 3680; -. DR KEGG; hsa:3680; -. DR MANE-Select; ENST00000264741.10; ENSP00000264741.5; NM_002207.3; NP_002198.2. DR UCSC; uc003chd.4; human. DR AGR; HGNC:6145; -. DR CTD; 3680; -. DR DisGeNET; 3680; -. DR GeneCards; ITGA9; -. DR HGNC; HGNC:6145; ITGA9. DR HPA; ENSG00000144668; Low tissue specificity. DR MIM; 603963; gene. DR neXtProt; NX_Q13797; -. DR OpenTargets; ENSG00000144668; -. DR PharmGKB; PA29945; -. DR VEuPathDB; HostDB:ENSG00000144668; -. DR eggNOG; KOG3637; Eukaryota. DR GeneTree; ENSGT00940000156503; -. DR HOGENOM; CLU_004111_5_0_1; -. DR InParanoid; Q13797; -. DR OMA; MMRKGMA; -. DR OrthoDB; 3816176at2759; -. DR PhylomeDB; Q13797; -. DR TreeFam; TF105391; -. DR PathwayCommons; Q13797; -. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-445144; Signal transduction by L1. DR SignaLink; Q13797; -. DR SIGNOR; Q13797; -. DR BioGRID-ORCS; 3680; 13 hits in 1141 CRISPR screens. DR ChiTaRS; ITGA9; human. DR GeneWiki; ITGA9; -. DR GenomeRNAi; 3680; -. DR Pharos; Q13797; Tbio. DR PRO; PR:Q13797; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q13797; Protein. DR Bgee; ENSG00000144668; Expressed in urethra and 174 other cell types or tissues. DR ExpressionAtlas; Q13797; baseline and differential. DR GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0034679; C:integrin alpha9-beta1 complex; ISS:UniProtKB. 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:0098640; F:integrin binding involved in cell-matrix adhesion; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IGI:MGI. 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 GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:UniProtKB. DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl. DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1. DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1. 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; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 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; IPR013649; Integrin_alpha_Ig-like_1. DR InterPro; IPR048285; Integrin_alpha_Ig-like_2. DR InterPro; IPR048286; Integrin_alpha_Ig-like_3. DR InterPro; IPR028994; Integrin_alpha_N. DR InterPro; IPR032695; Integrin_dom_sf. DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1. DR PANTHER; PTHR23220:SF69; INTEGRIN ALPHA-9; 1. DR Pfam; PF01839; FG-GAP; 2. DR Pfam; PF08441; Integrin_A_Ig_1; 1. DR Pfam; PF20805; Integrin_A_Ig_2; 1. DR Pfam; PF20806; Integrin_A_Ig_3; 1. DR PRINTS; PR01185; INTEGRINA. DR SMART; SM00191; Int_alpha; 5. DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1. DR SUPFAM; SSF69179; Integrin domains; 3. DR PROSITE; PS51470; FG_GAP; 7. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. DR Genevisible; Q13797; HS. PE 1: Evidence at protein level; KW Calcium; Cell adhesion; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Integrin; Membrane; Metal-binding; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..1035 FT /note="Integrin alpha-9" FT /id="PRO_0000016316" FT TOPO_DOM 30..981 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 982..1002 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1003..1035 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 35..96 FT /note="FG-GAP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 111..174 FT /note="FG-GAP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 182..232 FT /note="FG-GAP 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 233..289 FT /note="FG-GAP 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 290..349 FT /note="FG-GAP 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 351..408 FT /note="FG-GAP 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 411..474 FT /note="FG-GAP 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT MOTIF 1005..1009 FT /note="GFFKR motif" FT BINDING 312 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 314 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 316 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 320 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 373 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 375 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 377 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 381 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 435 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 437 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 439 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT BINDING 443 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P08648" FT SITE 565..566 FT /note="Cleavage" FT /evidence="ECO:0000255" FT CARBOHYD 225 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 476 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 493 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 612 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 654 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 658 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 672 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 676 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 807 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 854 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 904 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 87..97 FT /evidence="ECO:0000250" FT DISULFID 142..162 FT /evidence="ECO:0000250" FT DISULFID 179..194 FT /evidence="ECO:0000250" FT DISULFID 482..491 FT /evidence="ECO:0000250" FT DISULFID 497..555 FT /evidence="ECO:0000250" FT DISULFID 620..625 FT /evidence="ECO:0000250" FT DISULFID 696..706 FT /evidence="ECO:0000250" FT DISULFID 855..891 FT /evidence="ECO:0000250" FT DISULFID 898..903 FT /evidence="ECO:0000250" FT VARIANT 507 FT /note="G -> E (in dbSNP:rs267561)" FT /evidence="ECO:0000269|PubMed:8245132, FT ECO:0000269|PubMed:8290272" FT /id="VAR_055091" FT VARIANT 750 FT /note="R -> C (in a breast cancer sample; somatic mutation; FT dbSNP:rs781472543)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036073" SQ SEQUENCE 1035 AA; 114489 MW; B812EDA867A3E836 CRC64; MGGPAAPRGA GRLRALLLAL VVAGIPAGAY NLDPQRPVHF QGPADSFFGY AVLEHFHDNT RWVLVGAPKA DSKYSPSVKS PGAVFKCRVH TNPDRRCTEL DMARGKNRGT SCGKTCREDR DDEWMGVSLA RQPKADGRVL ACAHRWKNIY YEADHILPHG FCYIIPSNLQ AKGRTLIPCY EEYKKKYGEE HGSCQAGIAG FFTEELVVMG APGSFYWAGT IKVLNLTDNT YLKLNDEVIM NRRYTYLGYA VTAGHFSHPS TIDVVGGAPQ DKGIGKVYIF RADRRSGTLI KIFQASGKKM GSYFGSSLCA VDLNGDGLSD LLVGAPMFSE IRDEGQVTVY INRGNGALEE QLALTGDGAY NAHFGESIAS LDDLDNDGFP DVAIGAPKED DFAGAVYIYH GDAGGIVPQY SMKLSGQKIN PVLRMFGQSI SGGIDMDGNG YPDVTVGAFM SDSVVLLRAR PVITVDVSIF LPGSINITAP QCHDGQQPVN CLNVTTCFSF HGKHVPGEIG LNYVLMADVA KKEKGQMPRV YFVLLGETMG QVTEKLQLTY MEETCRHYVA HVKRRVQDVI SPIVFEAAYS LSEHVTGEEE RELPPLTPVL RWKKGQKIAQ KNQTVFERNC RSEDCAADLQ LQGKLLLSSM DEKTLYLALG AVKNISLNIS ISNLGDDAYD ANVSFNVSRE LFFINMWQKE EMGISCELLE SDFLKCSVGF PFMRSKSKYE FSVIFDTSHL SGEEEVLSFI VTAQSGNTER SESLHDNTLV LMVPLMHEVD TSITGIMSPT SFVYGESVDA ANFIQLDDLE CHFQPINITL QVYNTGPSTL PGSSVSISFP NRLSSGGAEM FHVQEMVVGQ EKGNCSFQKN PTPCIIPQEQ ENIFHTIFAF FTKSGRKVLD CEKPGISCLT AHCNFSALAK EESRTIDIYM LLNTEILKKD SSSVIQFMSR AKVKVDPALR VVEIAHGNPE EVTVVFEALH NLEPRGYVVG WIIAISLLVG ILIFLLLAVL LWKMGFFRRR YKEIIEAEKN RKENEDSWDW VQKNQ //