GenomeNet

Database: UniProt
Entry: M3W6P3_FELCA
LinkDB: M3W6P3_FELCA
Original site: M3W6P3_FELCA 
ID   M3W6P3_FELCA            Unreviewed;       767 AA.
AC   M3W6P3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN   Name=ITGB8 {ECO:0000313|Ensembl:ENSFCAP00000006400.3,
GN   ECO:0000313|VGNC:VGNC:67857};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000006400.3, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000006400.3, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000006400.3,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000006400.3, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000006400.3,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000006400.3}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000006400.3};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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; AANG04003224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003982883.1; XM_003982834.4.
DR   AlphaFoldDB; M3W6P3; -.
DR   STRING; 9685.ENSFCAP00000006400; -.
DR   PaxDb; 9685-ENSFCAP00000006400; -.
DR   Ensembl; ENSFCAT00000006895.6; ENSFCAP00000006400.3; ENSFCAG00000006893.6.
DR   GeneID; 101087724; -.
DR   KEGG; fca:101087724; -.
DR   CTD; 3696; -.
DR   VGNC; VGNC:67857; ITGB8.
DR   eggNOG; KOG1226; Eukaryota.
DR   GeneTree; ENSGT01090000259987; -.
DR   HOGENOM; CLU_011772_3_1_1; -.
DR   InParanoid; M3W6P3; -.
DR   OMA; SKIDNPC; -.
DR   OrthoDB; 5475862at2759; -.
DR   Proteomes; UP000011712; Chromosome A2.
DR   Bgee; ENSFCAG00000006893; Expressed in brain and 10 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0034686; C:integrin alphav-beta8 complex; IEA:Ensembl.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:1990430; F:extracellular matrix protein binding; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0001573; P:ganglioside metabolic process; IEA:Ensembl.
DR   GO; GO:0060022; P:hard palate development; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0061520; P:Langerhans 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:1901388; P:regulation of transforming growth factor beta activation; 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   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-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
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; 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; 2.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   Pfam; PF17205; PSI_integrin; 1.
DR   PIRSF; PIRSF002512; Integrin_B; 2.
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; INTEGRIN_BETA; 1.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|RuleBase:RU000633};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712};
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..42
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           43..767
FT                   /note="Integrin beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004041629"
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;  85549 MW;  F54F2614AF967FD7 CRC64;
     MCRSALAFFT AAFVCLQNCR PGPAPFLRAA WVFLVVLGLG QSEDNRCTSS NAASCTKCLA
     LGPECGWCAQ EDFISGGSRS ERCDIISNLI SKGCSIDSIE YPSVHVIPSE NEMNTQVTPG
     EVLIQLRPEA EANFMLKIHP LKKYPVDLYY LVDVSASMHN NIEKLNSVGN DLSRKMSYFS
     RDFRLGFGSY VDKTVSPYIS IHPERIHNQC SDYNLDCMPP HGYIHVLSLT ENITEFEKAV
     HRQKISGNID TPEGGFDAML QAAVCESHIG WRKEAKRLLL VMTDQTSHLA LDSKLAGIVV
     PNDGNCHLKN NIYVRSTSME HPSLGQLSEK LIDNNINVIF AVQGKQFHWY KDLLPLLPGT
     IAGEIESKAA NLNNLVVEAY QKLISEVKVQ VENQVKGVYF NITAICPDGT RKAGTDGCGN
     VTSNDEVLFN VTVTMKKCDV TGGKSYAIIK PIGFNETTKI HIHRNCSCQC EDSRGPKRKC
     IDEIFLDAKC FQCNENKCHF DEDQFPSESC KSHKDQPVCS GRGVCVCGKC LCHKIKLGKV
     YGKYCEKDDF SCPYYHGNLC AGHGECEAGR CQCFSGWEGD RCQCPSASAQ HCVNPKGQVC
     SGRGTCVCGK CQCTDPRSIG RFCEHCPTCH TACSENWNCV QCLHPHNLSQ AILDHCKTSC
     ALTEQHYMDQ TSECFSSPSY LRIFFIIFIV TFLIGLLKVL IIRQVILQWN SNKIKSSADY
     RVSASKKDKL ILQSVCTRTV TYRREKPEEI KMDISKLNAH ETFRCNF
//
DBGET integrated database retrieval system