ITB6_CAVPO
ID ITB6_CAVPO Reviewed; 577 AA.
AC P18563;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Integrin beta-6;
DE Flags: Fragment;
GN Name=ITGB6;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley;
RX PubMed=2365683; DOI=10.1016/s0021-9258(19)38425-x;
RA Sheppard D., Rozzo C., Starr L., Quaranta V., Erle D.J., Pytela R.;
RT "Complete amino acid sequence of a novel integrin beta subunit (beta 6)
RT identified in epithelial cells using the polymerase chain reaction.";
RL J. Biol. Chem. 265:11502-11507(1990).
CC -!- FUNCTION: Integrin alpha-V:beta-6 (ITGAV:ITGB6) is a receptor for
CC fibronectin and cytotactin (By similarity). It recognizes the sequence
CC R-G-D in its ligands (By similarity). ITGAV:ITGB6 acts as a receptor
CC for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to
CC FBN1 (By similarity). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-
CC G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1)
CC from regulatory Latency-associated peptide (LAP), thereby playing a key
CC role in TGF-beta-1 activation (By similarity).
CC {ECO:0000250|UniProtKB:P18564, ECO:0000250|UniProtKB:Q9Z0T9}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By similarity).
CC Interacts with FLNB. Interacts with HAX1. ITGAV:ITGB6 interacts with
CC FBN1 (By similarity). ITGAV:ITGB6 interacts with TGFB1 (By similarity).
CC {ECO:0000250|UniProtKB:P18564, ECO:0000250|UniProtKB:Q9Z0T9}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell junction, focal adhesion {ECO:0000250|UniProtKB:P18564}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; M35197; AAA37043.1; -; mRNA.
DR PIR; B37057; B37057.
DR AlphaFoldDB; P18563; -.
DR SMR; P18563; -.
DR STRING; 10141.ENSCPOP00000011065; -.
DR PRIDE; P18563; -.
DR eggNOG; KOG1226; Eukaryota.
DR InParanoid; P18563; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0034685; C:integrin alphav-beta6 complex; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR015436; Integrin_bsu-6.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF11; PTHR10082:SF11; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Disulfide bond; Glycoprotein; Integrin;
KW Membrane; Receptor; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..>577
FT /note="Integrin beta-6"
FT /id="PRO_0000174223"
FT TOPO_DOM <1..566
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..>577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN <1..230
FT /note="VWFA"
FT REPEAT 315..360
FT /note="I"
FT REPEAT 361..402
FT /note="II"
FT REPEAT 403..441
FT /note="III"
FT REPEAT 442..478
FT /note="IV"
FT REGION 315..478
FT /note="Cysteine-rich tandem repeats"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..63
FT /evidence="ECO:0000250|UniProtKB:P18564"
FT DISULFID 111..152
FT /evidence="ECO:0000250|UniProtKB:P18564"
FT DISULFID 253..265
FT /evidence="ECO:0000250"
FT DISULFID 285..529
FT /evidence="ECO:0000250"
FT DISULFID 311..315
FT /evidence="ECO:0000250"
FT DISULFID 326..338
FT /evidence="ECO:0000250"
FT DISULFID 335..370
FT /evidence="ECO:0000250"
FT DISULFID 340..349
FT /evidence="ECO:0000250"
FT DISULFID 351..361
FT /evidence="ECO:0000250"
FT DISULFID 376..381
FT /evidence="ECO:0000250"
FT DISULFID 378..411
FT /evidence="ECO:0000250"
FT DISULFID 383..396
FT /evidence="ECO:0000250"
FT DISULFID 398..403
FT /evidence="ECO:0000250"
FT DISULFID 417..422
FT /evidence="ECO:0000250"
FT DISULFID 419..450
FT /evidence="ECO:0000250"
FT DISULFID 424..433
FT /evidence="ECO:0000250"
FT DISULFID 435..442
FT /evidence="ECO:0000250"
FT DISULFID 456..461
FT /evidence="ECO:0000250"
FT DISULFID 458..504
FT /evidence="ECO:0000250"
FT DISULFID 463..473
FT /evidence="ECO:0000250"
FT DISULFID 476..479
FT /evidence="ECO:0000250"
FT DISULFID 483..492
FT /evidence="ECO:0000250"
FT DISULFID 489..561
FT /evidence="ECO:0000250"
FT DISULFID 508..537
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 577
SQ SEQUENCE 577 AA; 62299 MW; B83B468C83EDCCF9 CRC64;
SASMDDDLNT IKELGSLLSK EMSKLTSNFR LGFGSFVEKP VSPFMKTTPE EIANPCSSIP
YICLPTFGFK HILPLTNDAE RFNEIVKKQK ISANIDNPEG GFDAIMQAAV CKEKIGWRND
SLHLLVFVSD ADSHFGMDSK LAGIVIPNDG LCHLDSKNEY SMSTVMEYPT IGQLIDKVVQ
NNVLLIFAVT QEQVPLYENY AKLIPGATVG LLHKDSGNIL QLIISAYEEL RSEVELEVLG
DTEGLNLSFS AVCNNGTLFP HQKKCLHMKV GETASFNVTV SIPNCERKSR HVIIKPVGLG
DTLEILVSPE CSCDCQKEVE VNSSKCHNGN GSYQCGVCAC NPGHMGPHCE CGEDTLSTDS
CKETPDHPSC SGRGDCYCGQ CICHLSPYGN IYGPYCQCDN FSCVRHKGLL CGDNGDCECG
ECVCRSGWTG EYCNCTTSTD TCISEDGTLC SGRGDCVCGK CVCTNPGASG PTCERCPTCS
DPCNSKRSCI ECHLSADGQP GEECVDKCKL AGVTISKEAD FSKDSSVSCS LQGENECLIT
FLISTDNEGK TIIHNISEKD CPKPPNIPMI MLGVSLA
