ID A0A671FAZ4_RHIFE Unreviewed; 767 AA.
AC A0A671FAZ4;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB8 {ECO:0000313|Ensembl:ENSRFEP00010022690.1};
GN ORFNames=mRhiFer1_007028 {ECO:0000313|EMBL:KAF6301788.1};
OS Rhinolophus ferrumequinum (Greater horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Rhinolophoidea;
OC Rhinolophidae; Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=59479 {ECO:0000313|Ensembl:ENSRFEP00010022690.1, ECO:0000313|Proteomes:UP000472240};
RN [1] {ECO:0000313|Ensembl:ENSRFEP00010022690.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25689317; DOI=10.1146/annurev-animal-090414-014900;
RA Koepfli K.P., Paten B., O'Brien S.J., Koepfli K.P., Paten B., Antunes A.,
RA Belov K., Bustamante C., Castoe T.A., Clawson H., Crawford A.J.,
RA Diekhans M., Distel D., Durbin R., Earl D., Fujita M.K., Gamble T.,
RA Georges A., Gemmell N., Gilbert M.T., Graves J.M., Green R.E., Hickey G.,
RA Jarvis E.D., Johnson W., Komissarov A., Korf I., Kuhn R., Larkin D.M.,
RA Lewin H., Lopez J.V., Ma J., Marques-Bonet T., Miller W., Murphy R.,
RA Pevzner P., Shapiro B., Steiner C., Tamazian G., Venkatesh B., Wang J.,
RA Wayne R., Wiley E., Yang H., Zhang G., Haussler D., Ryder O., O'Brien S.J.;
RT "The Genome 10K Project: a way forward.";
RL Annu Rev Anim Biosci 3:57-111(2015).
RN [2] {ECO:0000313|Ensembl:ENSRFEP00010022690.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=29166127; DOI=10.1146/annurev-animal-022516-022811;
RA Teeling E.C., Vernes S.C., Davalos L.M., Ray D.A., Gilbert M.T.P.,
RA Myers E.;
RT "Bat Biology, Genomes, and the Bat1K Project: To Generate Chromosome-Level
RT Genomes for All Living Bat Species.";
RL Annu Rev Anim Biosci 6:23-46(2018).
RN [3] {ECO:0000313|Ensembl:ENSRFEP00010022690.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Teeling E., Myers G., Vernes S., Pippel M., Winkler S., Fedrigo O.,
RA Rhie A., Koren S., Phillippy A., Lewin H., Damas J., Howe K.,
RA Mountcastle J., Jarvis E.D.;
RT "G10K-VGP greater horseshoe bat female genome, primary haplotype.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KAF6301788.1, ECO:0000313|Proteomes:UP000585614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRhiFer1 {ECO:0000313|EMBL:KAF6301788.1};
RC TISSUE=Lung {ECO:0000313|EMBL:KAF6301788.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
RN [5] {ECO:0000313|Ensembl:ENSRFEP00010022690.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2025) to UniProtKB.
CC -!- FUNCTION: Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for
CC fibronectin. It recognizes the sequence R-G-D in its ligands. Integrin
CC alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of
CC transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-
CC associated peptide (LAP), thereby playing a key role in TGF-beta-1
CC activation on the surface of activated regulatory T-cells (Tregs).
CC Required during vasculogenesis. {ECO:0000256|ARBA:ARBA00056437}.
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:0000256|ARBA:ARBA00063793}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR EMBL; JACAGC010000019; KAF6301788.1; -; Genomic_DNA.
DR RefSeq; XP_032944459.1; XM_033088568.1.
DR AlphaFoldDB; A0A671FAZ4; -.
DR Ensembl; ENSRFET00010024697.1; ENSRFEP00010022690.1; ENSRFEG00010015208.1.
DR GeneID; 117012361; -.
DR KEGG; rfq:117012361; -.
DR CTD; 3696; -.
DR GeneTree; ENSGT01150000286919; -.
DR OMA; NCRRGPA; -.
DR OrthoDB; 410592at2759; -.
DR Proteomes; UP000472240; Chromosome 20.
DR Proteomes; UP000585614; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:TreeGrafter.
DR GO; GO:0034686; C:integrin alphav-beta8 complex; IEA:Ensembl.
DR GO; GO:1990430; F:extracellular matrix protein binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:TreeGrafter.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:TreeGrafter.
DR GO; GO:0001573; P:ganglioside metabolic process; IEA:Ensembl.
DR GO; GO:0060022; P:hard palate development; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0061520; P:Langerhans cell differentiation; IEA:Ensembl.
DR GO; GO:0043379; P:memory T cell differentiation; IEA:Ensembl.
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:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR FunFam; 2.10.25.10:FF:000076; Integrin beta; 1.
DR FunFam; 2.10.25.10:FF:000370; Integrin beta; 1.
DR FunFam; 2.60.40.1510:FF:000010; Integrin beta; 1.
DR FunFam; 3.30.1680.10:FF:000002; Integrin beta; 1.
DR FunFam; 3.40.50.410:FF:000002; Integrin beta; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR057073; EGF_integrin_2.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR057243; Integrin_I-EGF_CS.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF9; INTEGRIN BETA-8; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF23105; EGF_integrin; 1.
DR Pfam; PF23106; EGF_Teneurin; 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; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS00243; I_EGF_1; 1.
DR PROSITE; PS52047; I_EGF_2; 3.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU000633};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR002512-1};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000472240};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..767
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044626316"
FT TRANSMEM 680..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 571..582
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS00022"
FT DISULFID 47..468
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 55..65
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 58..94
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 68..83
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 210..217
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 265..306
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 406..418
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 466..470
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 490..519
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 525..530
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 527..560
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 532..545
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 566..571
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 573..582
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 606..611
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 608..656
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 613..623
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 626..629
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 633..642
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 767 AA; 85714 MW; 89A60307FCB60BF6 CRC64;
MCRSALAFFT AAFVCLQNCR PGPAPFLRAA WVFSVVLGLS QSENNRCASS NAASCARCLA
LGPECGWCAQ EDFTSGGTRS ERCDIVSNLI SKGCSIDSIE YPSVHVIPSE NEINTQVTPG
EVLIQLRPGA EANFMLKIHP LKKYPVDLYY LVDVSASMHN NIEKLNSVGN DLSRKMAFFS
RDFRLGFGSY VDKTVSPYIS IHPERIHNQC SDYNLDCMPP HGYIHVLSLT ENITEFEKAV
HRQKISGNID TPEGGFDAML QAAVCESHIG WRKEAKRLLL VMTDQTSHLA LDSKLAGIVV
PNDGNCHLKN NVYVRSTSME HPSLGQLSEK LIENNINVIF AVQGKQFHWY KDLLPLLPGT
IAGEIESKAA NLNNLVVEAY QKLISEVKVQ VENQIEGVYL NITAICPDGT RKPGTDGCRN
VTSNDEVLFN VTVIMERCDV TRGKSYAVIK PIGFNETTKI HIHKNCSCQC EDSSAPKRKC
VDETFLDSKC FQCDENKCHF DEDQFSSESC KSHEDQPVCS GRGVCMCGKC LCHRIKLGKV
YGKYCEKDDF SCPYHHGNLC AGHGECEAGR CRCFSGWEGD RCQCPSTSAQ HCVNPKGQVC
SGRGTCVCGR CECTDPRSIG RFCEHCPTCH TTCNENWNCV QCLHPHNLSQ VILDRCKTSC
AFMEQHYVDQ ASECFSSPSY LRIFFIIFIV TFLIGLLKVL IIRQVILQWN SNKIKSSADY
RVSASKKDKL ILQSVCTRAV TYRREKPEEI KMDISKLNAH ETFRCNF
//
