ID A0A8C5NJ69_JUNHY Unreviewed; 781 AA.
AC A0A8C5NJ69;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
OS Junco hyemalis (Dark-eyed junco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passerellidae; Junco.
OX NCBI_TaxID=40217 {ECO:0000313|Ensembl:ENSJHYP00000002455.1, ECO:0000313|Proteomes:UP000694408};
RN [1] {ECO:0000313|Ensembl:ENSJHYP00000002455.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSJHYP00000002455.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cell membrane {ECO:0000256|RuleBase:RU000633}; Single-pass type I
CC membrane protein {ECO:0000256|RuleBase:RU000633}. Cell projection,
CC lamellipodium membrane {ECO:0000256|ARBA:ARBA00004121}. Postsynaptic
CC cell membrane {ECO:0000256|ARBA:ARBA00035006}; Single-pass type I
CC membrane protein {ECO:0000256|ARBA:ARBA00035006}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR AlphaFoldDB; A0A8C5NJ69; -.
DR Ensembl; ENSJHYT00000003059.1; ENSJHYP00000002455.1; ENSJHYG00000002074.1.
DR OMA; AKWDTTH; -.
DR Proteomes; UP000694408; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR GO; GO:0005925; C:focal adhesion; IEA:TreeGrafter.
DR GO; GO:0008305; C:integrin complex; IEA:TreeGrafter.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070051; F:fibrinogen binding; IEA:TreeGrafter.
DR GO; GO:0001968; F:fibronectin binding; IEA:TreeGrafter.
DR GO; GO:0005178; F:integrin binding; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:TreeGrafter.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:TreeGrafter.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0070527; P:platelet aggregation; IEA:TreeGrafter.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:UniProtKB-ARBA.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:0045124; P:regulation of bone resorption; IEA:UniProtKB-ARBA.
DR GO; GO:0051049; P:regulation of transport; IEA:UniProtKB-ARBA.
DR FunFam; 1.20.5.100:FF:000002; Integrin beta; 1.
DR FunFam; 2.10.25.10:FF:000036; Integrin beta; 1.
DR FunFam; 2.10.25.10:FF:000075; Integrin beta; 1.
DR FunFam; 2.60.40.1510:FF:000004; 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 FunFam; 4.10.1240.30:FF:000001; Integrin beta; 1.
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; EGF_integrin_1.
DR InterPro; IPR057073; EGF_integrin_2.
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; IPR057243; Integrin_I-EGF_CS.
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; PF23105; EGF_integrin; 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 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; I_EGF_1; 1.
DR PROSITE; PS52047; I_EGF_2; 4.
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 junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Reference proteome {ECO:0000313|Proteomes:UP000694408};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..781
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034596775"
FT TRANSMEM 711..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..453
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 626..710
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 734..780
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 32..42
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 35..68
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 45..57
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 195..202
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 250..291
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 392..404
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 424..673
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 451..455
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 466..478
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 475..513
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 480..489
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 491..504
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 519..524
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 521..554
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 526..539
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 541..546
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 560..565
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 562..593
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 567..576
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 578..585
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 599..604
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 601..649
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 606..616
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 619..622
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 626..635
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 632..705
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 653..681
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 781 AA; 86094 MW; E6D6AD9EFF0C51D3 CRC64;
MDPRSVSLGI LLLCAAGTWG GNICTTRGVN SCKQCLAVSP LCAWCSAEVW AQSSPRCDLH
ANLLHHGCRQ EHIEFPSSSV TILEARPLSN KGSGGSATTQ MSPQRIQLNL RPDDSQVFHV
QVRQVEDYPV DIYYLMDLSN SMKDDLRNIQ NLGTKLASEM RKLTSNLRIG FGAFVDKPIS
PYMYISPPEA IKNPCYEIGE TCLPMFGYKH VLSLTDEVTR FNEEVRKQSV SRNRDAPEGG
FDAIIQATVC DEKIGWRNDA SHLLVFTTDA KTHIALDGRL AGIVQPNDAQ CHIDKDNFYS
ATTTLDYPSL GLMTEKLSQK NINLIFAVTD TVVGLYQNYS ELIPGTTVGT LSRDSSNVLQ
LIVDSYGKIR SKVELEVRDL PEELSLTFNA TCLNDEVIPG LKSCMGLKIG DTVSFSIEAK
VRGCPQEQQK SFTIKPVGFK DSLTVVVNFD CECSCESHAE SGSPSCSHGN GTLECGVCRC
NPGRLGSHCE CSEEEYNPSQ QDNCSPRPGQ PLCSQRGECI CGQCVCHSSD FGKVTGKYCE
CDDFSCVRFK GQMCSGHGQC SCGDCVCNSD WTGDYCNCTT RTDTCMSNNG LVCSGHGSCV
CGRCECTQPG SYGDTCEKCP TCPDACTIKK DCVECKKFER GKLAEQQSCS RMCRDEIETV
QELSDRGKDA VNCTYKDEND CVMRFQYYED SSGKSILYVI EEPDCPKGPD VLVVLLSVTG
AILLIGLAAL LIWKLLITIH DRREFAHFEE EKARAKWDTT HNPLYKEATS TFTNVTYRGN
M
//
