ID H0YY94_TAEGU Unreviewed; 797 AA.
AC H0YY94;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB3 {ECO:0000313|Ensembl:ENSTGUP00000003271.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000003271.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000003271.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000003271.2}
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}.
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 AlphaFoldDB; H0YY94; -.
DR STRING; 59729.ENSTGUP00000003271; -.
DR Ensembl; ENSTGUT00000003303.2; ENSTGUP00000003271.2; ENSTGUG00000003122.2.
DR GeneTree; ENSGT01090000259987; -.
DR HOGENOM; CLU_011772_0_1_1; -.
DR InParanoid; H0YY94; -.
DR OMA; AKWDTTH; -.
DR OrthoDB; 5475862at2759; -.
DR TreeFam; TF105392; -.
DR Proteomes; UP000007754; Chromosome 27.
DR GO; GO:0071133; C:alpha9-beta1 integrin-ADAM8 complex; IEA:Ensembl.
DR GO; GO:0035868; C:alphav-beta3 integrin-HMGB1 complex; IEA:Ensembl.
DR GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; IEA:Ensembl.
DR GO; GO:0035866; C:alphav-beta3 integrin-PKCalpha complex; IEA:Ensembl.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0031527; C:filopodium membrane; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0034683; C:integrin alphav-beta3 complex; IEA:Ensembl.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:Ensembl.
DR GO; GO:0031528; C:microvillus membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
DR GO; GO:0019960; F:C-X3-C chemokine binding; IEA:Ensembl.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0038132; F:neuregulin binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:Ensembl.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0043277; P:apoptotic cell clearance; IEA:Ensembl.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IEA:Ensembl.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0050919; P:negative chemotaxis; IEA:Ensembl.
DR GO; GO:0010888; P:negative regulation of lipid storage; IEA:Ensembl.
DR GO; GO:0032369; P:negative regulation of lipid transport; IEA:Ensembl.
DR GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; IEA:Ensembl.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IEA:Ensembl.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR GO; GO:0051611; P:regulation of serotonin uptake; IEA:Ensembl.
DR GO; GO:1901163; P:regulation of trophoblast cell migration; IEA:Ensembl.
DR GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
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; 4.
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 InterPro; IPR007527; Znf_SWIM.
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.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 3: Inferred from homology;
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
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}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..797
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025677771"
FT TRANSMEM 727..749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 459..493
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DISULFID 40..469
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 48..58
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 51..84
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 61..73
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 211..218
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 266..307
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 408..420
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 440..689
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 467..471
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 482..494
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 491..529
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 496..505
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 507..520
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 535..540
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 537..570
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 542..555
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 557..562
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 576..581
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 578..609
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 583..592
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 594..601
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 615..620
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 617..665
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 622..632
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 635..638
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 642..651
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 648..721
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 669..697
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 797 AA; 87617 MW; DED9B0A9D852E799 CRC64;
MEGLLQAVPP LRGSGKMGQL SVTLGILLLC AAGSWGGNIC STRGVNSCKQ CLAVSPLCAW
CSAEVWAHSA PRCDLHANLL HNGCGQDHIE FPSSSVTILE DRPLSNKGSG GSTTTQMSPQ
RIQLNLRPDD SQVFHVQVRQ VEDYPVDIYY LMDLSNSMKD DLRNIQNLGT KLASEMRKLT
SNLRIGFGAF VDKPISPYMY ISPPEAIKNP CYEIGETCLP MFGYKHVLSL TDEVTRFNEE
VRKQSVSRNR DAPEGGFDAI IQATVCDEKI GWRNDASHLL VFTTDAKTHI ALDGRLAGIV
QPNDAQCHID KDNFYSATTT LDYPSLGLMT EKLSQKNINL IFAVTDTVVG LYQNYSELIP
GTTVGTLSRD SSNVLQLIVD SYGKIRSKVE LEVRDLPEEL SLTFNATCLN DEVILGLKSC
MGLKIGDTVS FSIEAKVRGC PQEQQKSFTI KPVGFKDSLT VVVNFDCECS CESHAEANSP
SCSHGNGTLE CGVCRCHPGR LGSHCECSEE EYNPSQQDNC SPRPGQPLCS QRGECICGQC
VCHSSDFGKV TGKYCECDDF SCVRFKGQMC SGHGQCSCGD CLCNSDWTGD YCNCTTRTDT
CMSSNGLVCS GHGSCVCGRC ECTQPGSYGD TCEKCPTCPD ACTIKKDCVE CKKFERGKLM
DQQSCSRMCR DEIETVQELS DGGKNAVNCT YKDENDCVMR FQYYEDSSGK SILYVIEEPD
CPKGPDILVV LLSVTGAILL IGLAALLIWK LLITIHDRRE FAHFEEEKAR AKWDTTHNPL
YKEATSTFTN ITYRGNM
//
