ID ITA6_HUMAN STANDARD; PRT; 1073 AA. AC P23229; DT 01-NOV-1991 (REL. 20, CREATED) DT 01-NOV-1991 (REL. 20, LAST SEQUENCE UPDATE) DT 01-MAY-1992 (REL. 22, LAST ANNOTATION UPDATE) DE INTEGRIN ALPHA-6 PRECURSOR (VLA-6) (INTEGRIN ALPHA-E). OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PANCREAS; RM 91009492 RA TAMURA R.N., ROZZO C., STARR L., CHAMBERS J., REICHARDT L.F., RA COOPER H.M., QUARANTA V.; 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 24-46. RM 89251596 RA KAJIJI S., TAMURA R.N., QUARANTA V.; RL EMBO J. 8:673-680(1989). RN [4] RP SEQUENCE OF 23-44. RM 89197963 RA HEMLER M.E., CROUSE C., SONNENBERG A.; 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 -!- TISSUE SPECIFICITY: INTEGRIN ALPHA-6/BETA-4 IS PREDOMINANTLY CC EXPRESSED BY EPITHELIA. CC -!- SIMILARITY: WITH OTHER ALPHA CHAINS FROM THE INTEGRIN FAMILY OF CC CELL-SURFACE RECEPTOR. 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; HSINTA6R. DR PIR; B36429; B36429. DR PIR; S06962; S06962. DR PROSITE; PS00242; INTEGRIN_ALPHA. KW INTEGRIN; CELL ADHESION; GLYCOPROTEIN; TRANSMEMBRANE; SIGNAL; KW EXTRACELLULAR MATRIX; CYTOSKELETON. FT SIGNAL 1 23 FT CHAIN 24 1073 INTEGRIN ALPHA-6. FT CHAIN 24 902 HEAVY CHAIN (POTENTIAL). FT CHAIN 903 1073 LIGHT CHAIN (POTENTIAL). FT DOMAIN 24 1011 EXTRACELLULAR. FT TRANSMEM 1012 1037 POTENTIAL. FT DOMAIN 1038 1073 CYTOPLASMIC. FT REPEAT 42 79 DOMAIN I. FT REPEAT 113 145 DOMAIN II. FT REPEAT 185 217 DOMAIN III. FT REPEAT 256 292 DOMAIN IV. FT REPEAT 314 352 DOMAIN V. FT REPEAT 375 411 DOMAIN VI. FT REPEAT 430 470 DOMAIN VII. 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. SQ SEQUENCE 1073 AA; 119510 MW; 5954980 CN; 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 TFDTPYLDIN 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 //