ID ITA6_HUMAN STANDARD; PRT; 1073 AA. AC P23229; Q14646; Q16508; Q08443; DT 01-NOV-1991 (REL. 20, CREATED) DT 15-JUL-1998 (REL. 36, LAST SEQUENCE UPDATE) DT 15-DEC-1998 (REL. 37, LAST ANNOTATION UPDATE) DE INTEGRIN ALPHA-6 PRECURSOR (VLA-6) (CD49F). GN ITGA6. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; OC PRIMATES; CATARRHINI; HOMINIDAE; HOMO. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PANCREAS; RX MEDLINE; 91009492. RA TAMURA R.N., ROZZO C., STARR L., CHAMBERS J., REICHARDT L.F., RA COOPER H.M., QUARANTA V.; RT "Epithelial integrin alpha 6 beta 4: complete primary structure of RT alpha 6 and variant forms of beta 4."; RL J. CELL BIOL. 111:1593-1604(1990). RN [2] RP REVISIONS TO 78 AND 323. RA QUARANTA V.; RL SUBMITTED (JUN-1991) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [3] RP SEQUENCE OF 7-1073 FROM N.A. RX MEDLINE; 91301154. RA HOGERVORST F., KUIKMAN I., GEURTS VAN KESSEL A., SONNENBERG A.; RT "Molecular cloning of the human alpha 6 integrin subunit. Alternative RT splicing of alpha 6 mRNA and chromosomal localization of the alpha 6 RT and beta 4 genes."; RL EUR. J. BIOCHEM. 199:425-433(1991). RN [4] RP SEQUENCE OF 709-810 FROM N.A. RX MEDLINE; 93119630. RA STARR L., QUARANTA V.; RT "An efficient and reliable method for cloning PCR-amplification RT products: a survey of point mutations in integrin cDNA."; RL BIOTECHNIQUES 13:612-618(1992). RN [5] RP SEQUENCE OF 927-1073 FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE; 92052235. RA TAMURA R.N., COOPER H.M., COLLO G., QUARANTA V.; RT "Cell type-specific integrin variants with alternative alpha chain RT cytoplasmic domains."; RL PROC. NATL. ACAD. SCI. U.S.A. 88:10183-10187(1991). RN [6] RP SEQUENCE OF 24-46. RX MEDLINE; 89251596. RA KAJIJI S., TAMURA R.N., QUARANTA V.; RT "A novel integrin (alpha E beta 4) from human epithelial cells RT suggests a fourth family of integrin adhesion receptors."; RL EMBO J. 8:673-680(1989). RN [7] RP SEQUENCE OF 23-44. RX MEDLINE; 89197963. RA HEMLER M.E., CROUSE C., SONNENBERG A.; RT "Association of the VLA alpha 6 subunit with a novel protein. A RT possible alternative to the common VLA beta 1 subunit on certain cell RT lines."; RL J. BIOL. CHEM. 264:6529-6535(1989). CC -!- FUNCTION: INTEGRIN ALPHA-6/BETA-4 MAY MEDIATE ADHESIVE AND/OR CC MIGRATORY FUNCTIONS OF EPITHELIAL CELLS. ON PLATELETS, INTEGRIN CC ALPHA-6/BETA-1 FUNCTIONS AS A LAMININ RECEPTOR. CC -!- SUBUNIT: DIMER OF AN ALPHA AND BETA SUBUNIT. ALPHA-6 CAN CC ASSOCIATE WITH BETA-1 (FORMING THE PLATELET LAMININ RECEPTOR) CC OR BETA-4 (PREDOMINANTLY ON EPITHELIAL CELLS). CC -!- SUBUNIT: THE ALPHA SUBUNIT MAY BE CLEAVED POST-TRANSLATIONALLY CC TO GIVE TWO POLYPEPTIDES JOINED BY A DISULFIDE BRIDGE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- TISSUE SPECIFICITY: INTEGRIN ALPHA-6/BETA-4 IS PREDOMINANTLY CC EXPRESSED BY EPITHELIA. CC -!- PTM: PHOSPHORYLATED IN VIVO. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS; ALPHA-6A (SHOWN HERE) AND ALPHA- CC 6B; ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- SIMILARITY: BELONGS TO THE INTEGRIN ALPHA CHAIN FAMILY. CC -!- DATABASE: NAME=PROW; NOTE=CD guide CD49f entry; CC WWW="http://www.ncbi.nlm.nih.gov/prow/cd/cd49f.htm". CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; X53586; G33944; -. DR EMBL; X59512; G33942; -. DR EMBL; S52135; G263064; -. DR EMBL; S66213; G239160; -. DR EMBL; S66196; G239158; -. DR PIR; B36429; B36429. DR PIR; S06962; S06962. DR MIM; 147556; -. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. DR PFAM; PF00357; integrin_A; 1. DR HSSP; P11215; 1A8X. KW INTEGRIN; CELL ADHESION; GLYCOPROTEIN; TRANSMEMBRANE; SIGNAL; KW EXTRACELLULAR MATRIX; CYTOSKELETON; PHOSPHORYLATION; REPEAT; KW ALTERNATIVE SPLICING. FT SIGNAL 1 23 FT CHAIN 24 1073 INTEGRIN ALPHA-6. FT CHAIN 24 899 INTEGRIN ALPHA-6 HEAVY CHAIN (POTENTIAL). FT CHAIN 903 1073 INTEGRIN ALPHA-6 LIGHT CHAIN (POTENTIAL). FT DOMAIN 24 1011 EXTRACELLULAR. FT TRANSMEM 1012 1037 POTENTIAL. FT DOMAIN 1038 1073 CYTOPLASMIC. FT DOMAIN 42 470 7 X APPROXIMATE REPEATS. FT REPEAT 42 79 I. FT REPEAT 113 145 II. FT REPEAT 185 217 III. FT REPEAT 256 292 IV. FT REPEAT 314 352 V. FT REPEAT 375 411 VI. FT REPEAT 430 470 VII. FT DISULFID 86 94 BY SIMILARITY. FT DISULFID 131 154 BY SIMILARITY. FT DISULFID 175 188 BY SIMILARITY. FT DISULFID 489 496 BY SIMILARITY. FT DISULFID 502 562 BY SIMILARITY. FT DISULFID 626 632 BY SIMILARITY. FT DISULFID 726 737 BY SIMILARITY. FT DISULFID 881 928 INTERCHAIN (BY SIMILARITY). FT DISULFID 934 939 BY SIMILARITY. FT CARBOHYD 223 223 POTENTIAL. FT CARBOHYD 284 284 POTENTIAL. FT CARBOHYD 370 370 POTENTIAL. FT CARBOHYD 731 731 POTENTIAL. FT CARBOHYD 748 748 POTENTIAL. FT CARBOHYD 891 891 POTENTIAL. FT CARBOHYD 927 927 POTENTIAL. FT CARBOHYD 958 958 POTENTIAL. FT MOD_RES 1071 1071 PHOSPHORYLATION (BY CAM-KINASE II) FT (POTENTIAL). FT VARSPLIC 1045 1073 NKKDHYDATYHKAEIHAQPSDKERLTSDA -> SRYDDSVP FT RYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNRNESYS FT (IN ALPHA-6B). FT CONFLICT 462 462 F -> L (IN REF. 3). FT CONFLICT 766 766 D -> Y (IN REF. 1). SQ SEQUENCE 1073 AA; 119462 MW; F566BF17 CRC32; MAAAGQLCLL YLSAGLLSRL GAAFNLDTRE DNVIRKYGDP GSLFGFSLAM HWQLQPEDKR LLLVGAPRGE ALPLQRANRT GGLYSCDITA RGPCTRIEFD NDADPTSESK EDQWMGVTVQ SQGPGGKVVT CAHRYEKRQH VNTKQESRDI FGRCYVLSQN LRIEDDMDGG DWSFCDGRLR GHEKFGSCQQ GVAATFTKDF HYIVFGAPGT YNWKGIVRVE QKNNTFFDMN IFEDGPYEVG GETEHDESLV PVPANSYLGF SLDSGKGIVS KDEITFVSGA PRANHSGAVV LLKRDMKSAH LLPEHIFDGE GLASSFGYDV AVVDLNKDGW QDIVIGAPQY FDRDGEVGGA VYVYMNQQGR WNNVKPIRLN GTKDSMFGIA VKNIGDINQD GYPDIAVGAP YDDLGKVFIY HGSANGINTK PTQVLKGISP YFGYSIAGNM DLDRNSYPDV AVGSLSDSVT IFRSRPVINI QKTITVTPNR IDLRQKTACG APSGICLQVK SCFEYTANPA GYNPSISIVG TLEAEKERRK SGLSSRVQFR NQGSEPKYTQ ELTLKRQKQK VCMEETLWLQ DNIRDKLRPI PITASVEIQE PSSRRRVNSL PEVLPILNSD EPKTAHIDVH FLKEGCGDDN VCNSNLKLEY KFCTREGNQD KFSYLPIQKG VPELVLKDQK DIALEITVTN SPSNPRNPTK DGDDAHEAKL IATFPDTLTY SAYRELRAFP EKQLSCVANQ NGSQADCELG NPFKRNSNVT FYLVLSTTEV TFDTPDLDIN LKLETTSNQD NLAPITAKAK VVIELLLSVS GVAKPSQVYF GGTVVGEQAM KSEDEVGSLI EYEFRVINLG KPLTNLGTAT LNIQWPKEIS NGKWLLYLVK VESKGLEKVT CEPQKEINSL NLTESHNSRK KREITEKQID DNRKFSLFAE RKYQTLNCSV NVNCVNIRCP LRGLDSKASL ILRSRLWNST FLEEYSKLNY LDILMRAFID VTAAAENIRL PNAGTQVRVT VFPSKTVAQY SGVPWWIILV AILAGILMLA LLVFILWKCG FFKRNKKDHY DATYHKAEIH AQPSDKERLT SDA //