ID M3YR68_MUSPF Unreviewed; 767 AA.
AC M3YR68;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB8 {ECO:0000313|Ensembl:ENSMPUP00000013827.1,
GN ECO:0000313|RefSeq:XP_004743426.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000013827.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000013827.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004743426.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004743426.1};
RG RefSeq;
RL Submitted (NOV-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}.
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DR EMBL; AEYP01012926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01012927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01012928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004743426.1; XM_004743369.3.
DR STRING; 9669.ENSMPUP00000013827; -.
DR Ensembl; ENSMPUT00000014047.1; ENSMPUP00000013827.1; ENSMPUG00000013932.1.
DR GeneID; 101675667; -.
DR KEGG; mpuf:101675667; -.
DR CTD; 3696; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01090000259987; -.
DR HOGENOM; CLU_011772_3_1_1; -.
DR OMA; SKIDNPC; -.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
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: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; IEA:UniProtKB-KW.
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; 1.
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:UP000000715};
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_5041118242"
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; 85571 MW; 8C987E87307B2C22 CRC64;
MCHSALAFFT AAFVCLQNCR PGPATFLWAA WVFLVVLGLG QSEDNRCASS NAVSCTKCLA
LGPECGWCAQ EDFISGGSRS ERCDIISNLI SKGCSIDSIE YPSVHVIPSE NEINTQVTPG
EVLIQLRPEA EANFMLKIHP LKKYPVDLYY LVDVSASMHN NIEKLNSVGN DLSRKMAYFS
RDFRLGFGSY VDKTVSPYIS IHPERIHNQC SDYNLDCMPP HGYIHVLSLT ENITEFEKAV
HRQKISGNID TPEGGFDAML QAAVCESHIG WRKEAKRLLL VMTDQTSHLA LDSKLAGIVV
PNDGNCHLKN NIYVRSTSME HPSLGQLSEK LIDNNINVIF AVQGKQFHWY KDLLPLLPGT
IAGEIESKAA NLNNLVVEAY QKLISEVKVQ VENQVKGVYF NITAICPDGT RKPGTDGCGN
VTSNDEVLFN ITVTMKKCDV TGGKTYAIIK PIGFNETTKI HIHRNCSCQC DDRRGPKRKC
VDEVSLDAKC FQCNENKCHF DEDQFPSESC KLHKDQPVCS GRGVCVCGKC LCHKIKLGKV
YGKYCEKDDF SCPYHHGNLC AGHGECEAGR CQCFSGWEGD RCQCPSASAQ HCVNSKGQVC
SGRGTCVCGR CECTDPRSIG RFCEHCPTCH TACSENWNCV QCLHPYNLSQ AILDRCKTSC
ALMEQHYMDQ TSECFSSPSY LRIFFIIFIV TFLIGLLKVL IIRQVILQWN SNKIKSSADY
RGSASKKDKL ILQSVCTRAV TYRREKPEEI KMDISKLNAH ETFRCNF
//
