ITB8_RABIT
ID ITB8_RABIT Reviewed; 768 AA.
AC P26013;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Integrin beta-8 {ECO:0000305};
DE Flags: Precursor;
GN Name=ITGB8;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand white; TISSUE=Placenta;
RX PubMed=1918072; DOI=10.1016/s0021-9258(18)55042-0;
RA Moyle M., Napier M.A., McLean J.W.;
RT "Cloning and expression of a divergent integrin subunit beta 8.";
RL J. Biol. Chem. 266:19650-19658(1991).
CC -!- FUNCTION: Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for
CC fibronectin (By similarity). It recognizes the sequence R-G-D in its
CC ligands (By similarity). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates
CC R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-
CC 1) from regulatory Latency-associated peptide (LAP), thereby playing a
CC key role in TGF-beta-1 activation on the surface of activated
CC regulatory T-cells (Tregs) (By similarity). Required during
CC vasculogenesis (By similarity). {ECO:0000250|UniProtKB:P26012,
CC ECO:0000250|UniProtKB:Q0VBD0}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-8 (ITGB8)
CC associates with alpha-V (ITGAV) to form ITGAV:ITGB8. ITGAV:ITGB8
CC interacts with TGFB1. {ECO:0000250|UniProtKB:P26012}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26012};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Placenta, kidney, brain, ovary, uterus and in
CC several transformed cells. {ECO:0000269|PubMed:1918072}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; M73781; AAA31280.1; -; mRNA.
DR PIR; B41029; B41029.
DR RefSeq; NP_001075773.1; NM_001082304.1.
DR AlphaFoldDB; P26013; -.
DR SMR; P26013; -.
DR STRING; 9986.ENSOCUP00000001898; -.
DR Ensembl; ENSOCUT00000047062; ENSOCUP00000035707; ENSOCUG00000002197.
DR GeneID; 100009141; -.
DR KEGG; ocu:100009141; -.
DR CTD; 3696; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR HOGENOM; CLU_011772_3_1_1; -.
DR InParanoid; P26013; -.
DR OMA; DFSCPYY; -.
DR OrthoDB; 473040at2759; -.
DR Proteomes; UP000001811; Chromosome 10.
DR Bgee; ENSOCUG00000002197; Expressed in skeletal muscle tissue and 15 other tissues.
DR GO; GO:0034686; C:integrin alphav-beta8 complex; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
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 GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR015442; Integrin_bsu-8.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF9; PTHR10082:SF9; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; Integrin;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..768
FT /note="Integrin beta-8"
FT /id="PRO_0000016355"
FT TOPO_DOM 43..683
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 684..703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 704..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 146..384
FT /note="VWFA"
FT REPEAT 471..510
FT /note="I"
FT REPEAT 511..552
FT /note="II"
FT REPEAT 553..592
FT /note="III"
FT REPEAT 593..629
FT /note="IV"
FT REGION 471..629
FT /note="Cysteine-rich tandem repeats"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..469
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 55..65
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 58..94
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 68..83
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 211..218
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 266..307
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 407..419
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 467..471
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 481..494
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 491..520
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 526..531
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 528..561
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 533..546
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 567..572
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 574..583
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 607..612
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 609..657
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 614..624
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 627..630
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 634..643
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
SQ SEQUENCE 768 AA; 84406 MW; C3F6DF0322FFB544 CRC64;
MCGSALGLPP AAFVRLRSCR PGPAAFLRAA WVLSLVLGLG RSENSRCASS HAVSCSECLA
LGPDCGWCVH EDFISGGPRS ERCDIVSNLI SKGCPVDSIE YPSVHVTIPS ENEVNTQVTP
GEVSIQLRPG AAANFMLKIH PLKKYPVDLY YLVDVSASMH NNIEKLNSVG NDLSRKMAFF
SRDFRLGFGS YVDKTVSPYI SIHPERIHNQ CSDYNLDCMP PHGYIHVLSL TENITEFERA
VHRQKISGNI DTPEGGFDAM LQAAVCESHI GWRKEAKRLL LVMTDQTSHL ALDSKLAGIV
VPNDGNCHLR NNVYVKSTTM EHPSLGQLSE KLIDNNINVI FAVQGKQFHW YKDLLPLLPG
TIAGEIESKA ANLNNLVVEA YQKLISEVKV QVESKVPGVY FNVTAICPDG ARKLGMEGCS
NVTSSDEVLF NVTVTMEKCS VTGGKNYAII KPIGFNETSK IHIHQNCGCE CEASRGGAAK
CAEEAPLDST CPQCQESQCH QEEAQSPSQG CKAHEDQPVC SGRGVCVCGK CLCHKMKLGK
VYGKYCEKDD FSCPYHHGSL CAGHGECEAG RCQCFSGWEG DRCQCPSAAA QHCVNSKGQV
CSGRGTCVCG RCECSDPRSI GRFCEHCPTC PTACSENWNC VQCLHPHNLS QAILDQCRTS
CASMEQPYVE QASECFSSPS YLRIFFIIFI VTFLIGLLKI LIIRQVILQW NSSKIKSSSD
YRVSASKKDK LILQSVCTRA VTYRREKPEE IKLDISKLNA HETFRCNF
