ID G1QXM3_NOMLE Unreviewed; 788 AA.
AC G1QXM3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB3 {ECO:0000313|Ensembl:ENSNLEP00000005694.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000005694.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000005694.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000005694.1}
RP IDENTIFICATION.
RG Ensembl;
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; ADFV01061412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01061413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003270746.1; XM_003270698.3.
DR AlphaFoldDB; G1QXM3; -.
DR Ensembl; ENSNLET00000005990.2; ENSNLEP00000005694.1; ENSNLEG00000004670.2.
DR GeneID; 100593791; -.
DR KEGG; nle:100593791; -.
DR CTD; 3690; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01090000259987; -.
DR HOGENOM; CLU_011772_0_1_1; -.
DR OrthoDB; 5475862at2759; -.
DR TreeFam; TF105392; -.
DR Proteomes; UP000001073; Chromosome 19.
DR GO; GO:0008305; C:integrin complex; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1240.30; -; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 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; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
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:SF25; INTEGRIN BETA-3; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 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; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
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|PIRSR:PIRSR002512-1};
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:UP000001073};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..788
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003419948"
FT TRANSMEM 719..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..76
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 38..461
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 634..718
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 742..788
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 31..461
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 39..49
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 42..75
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 52..64
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 203..210
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 258..299
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 400..412
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 432..681
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 459..463
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 474..486
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 483..521
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 488..497
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 499..512
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 527..532
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 529..562
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 534..547
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 549..554
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 568..573
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 570..601
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 575..584
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 586..593
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 607..612
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 609..657
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 614..624
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 627..630
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 634..643
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 640..713
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 661..689
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 788 AA; 87017 MW; 08B430F38C7E0C14 CRC64;
MRARPRPRPL WATVLALGAL AGVGVGGPNI CTTRGVSSCQ QCLAVSPMCA WCSDEALPLG
SPRCDLKENL LKDNCAPESI EFPVSEARVL EDRPLSDKGS GDSSQVTQVS PQRIALRLRP
DDSKNFSIQV RQVEDYPVDI YYLMDLSYSM KDDLWSIQNL GTKLATQMRK LTSNLRIGFG
AFVDKPVSPY MYISPPEALE NPCYDMKTTC LPMFGYKHVL TLTDQVTRFN EEVKKQSVSR
NRDAPEGGFD AIMQATVCDE KIGWRNDASH LLVFTTDAKT HIALDGRLAG IVQPNDGQCH
VGSDNHYSAS TTMDYPSLGL MTEKLSQKNI NLIFAVTENV VSLYQNYSEL IPGTTVGVLS
MDSSNVLQLI VDAYGKIRSK VELEVRDLPE ELSLSFNATC LNNEVIPGLK SCMGLKIGDT
VSFSIEAKVR GCPQEKEKSF SIKPVGFKDS LIVQVTFDCD CACQAQAEPN SHRCNNGNGT
FECGVCRCGP GWLGSQCECS EEDYRPSQQD ECSPREGQPV CSQRGECLCG QCVCHSSDFG
KITGKYCECD DFSCVRYKGE MCSGHGQCSC GDCLCDSDWT GYYCNCTTRT DTCMSSNGLL
CSGRGKCECG SCVCIQPGSY GDTCEKCPTC PDACTFKKEC VECKKFDRGA LHDENTCNRY
CRDEIESVKE LKDTGKDAVN CTYKNEDDCV VRFQYYEDSS GKSILYVVEE PECPKGPDIL
VVLLSVMGAI LLIGLAALLI WKLLITIHDR KEFAKFEEER ARAKWDTANN PLYKEATSTF
TNITYRGT
//
