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Database: UniProt
Entry: P26013
LinkDB: P26013
Original site: P26013 
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   10-APR-2019, entry version 131.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=New Zealand white; TISSUE=Placenta;
RX   PubMed=1918072;
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
CC       its ligands (By similarity). Integrin alpha-V:beta-6 (ITGAV:ITGB6)
CC       mediates R-G-D-dependent release of transforming growth factor
CC       beta-1 (TGF-beta-1) from regulatory Latency-associated peptide
CC       (LAP), thereby playing a key role in TGF-beta-1 activation on the
CC       surface of activated regulatory T-cells (Tregs) (By similarity).
CC       Required during vasculogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:P26012, ECO:0000250|UniProtKB:Q0VBD0}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-8
CC       (ITGB8) associates with alpha-V (ITGAV) to form ITGAV:ITGB8.
CC       ITGAV:ITGB8 interacts with TGFB1. {ECO:0000250|UniProtKB:P26012}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P26012}; Single-pass type I membrane
CC       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.
CC       {ECO:0000305}.
DR   EMBL; M73781; AAA31280.1; -; mRNA.
DR   PIR; B41029; B41029.
DR   RefSeq; NP_001075773.1; NM_001082304.1.
DR   UniGene; Ocu.1889; -.
DR   ProteinModelPortal; P26013; -.
DR   SMR; P26013; -.
DR   STRING; 9986.ENSOCUP00000001898; -.
DR   PRIDE; P26013; -.
DR   Ensembl; ENSOCUT00000002200; ENSOCUP00000001898; ENSOCUG00000002197.
DR   GeneID; 100009141; -.
DR   KEGG; ocu:100009141; -.
DR   CTD; 3696; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P26013; -.
DR   KO; K06591; -.
DR   OMA; SASAQHC; -.
DR   OrthoDB; 473040at2759; -.
DR   Proteomes; UP000001811; Chromosome 10.
DR   Bgee; ENSOCUG00000002197; Expressed in 3 organ(s), highest expression level in adult mammalian kidney.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0034686; C:integrin alphav-beta8 complex; ISS:UniProtKB.
DR   GO; GO:1990430; F:extracellular matrix protein binding; IEA:Ensembl.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   GO; GO:0001573; P:ganglioside metabolic process; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
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; IPR013032; EGF-like_CS.
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; Complete proteome; Disulfide bond;
KW   Glycoprotein; Integrin; Membrane; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     42       {ECO:0000255}.
FT   CHAIN        43    768       Integrin beta-8.
FT                                /FTId=PRO_0000016355.
FT   TOPO_DOM     43    683       Extracellular. {ECO:0000255}.
FT   TRANSMEM    684    703       Helical. {ECO:0000255}.
FT   TOPO_DOM    704    768       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      146    384       VWFA.
FT   REPEAT      471    510       I.
FT   REPEAT      511    552       II.
FT   REPEAT      553    592       III.
FT   REPEAT      593    629       IV.
FT   REGION      471    629       Cysteine-rich tandem repeats.
FT   CARBOHYD    233    233       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    402    402       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    421    421       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    431    431       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    456    456       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    648    648       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     47    469       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID     55     65       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID     58     94       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID     68     83       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    211    218       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    266    307       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    407    419       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    467    471       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    481    494       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    491    520       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    526    531       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    528    561       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    533    546       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    567    572       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    574    583       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    607    612       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    609    657       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    614    624       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    627    630       {ECO:0000255|PIRSR:PIRSR002512-1}.
FT   DISULFID    634    643       {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
//
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