ID A0A2K6T692_SAIBB Unreviewed; 798 AA.
AC A0A2K6T692;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB1 {ECO:0000313|Ensembl:ENSSBOP00000015171.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000015171.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000015171.1}
RP IDENTIFICATION.
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}. Cell
CC projection, invadopodium membrane {ECO:0000256|ARBA:ARBA00004297};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004297}.
CC Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cell
CC projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004199}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004199}.
CC Melanosome {ECO:0000256|ARBA:ARBA00004223}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {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 RefSeq; XP_010347351.1; XM_010349049.1.
DR AlphaFoldDB; A0A2K6T692; -.
DR Ensembl; ENSSBOT00000031970.1; ENSSBOP00000015171.1; ENSSBOG00000024301.1.
DR GeneTree; ENSGT01090000259987; -.
DR OMA; NCVCGAC; -.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0008305; C:integrin complex; IEA:UniProt.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0007517; P:muscle organ development; 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; 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 PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF28; INTEGRIN BETA-1; 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 junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..798
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014338907"
FT TRANSMEM 729..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..76
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 34..464
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 640..728
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 752..798
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT REGION 75..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 35..45
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 38..75
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 48..64
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 207..213
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 261..301
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 435..691
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 462..466
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 477..489
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 486..525
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 491..500
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 502..516
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 531..536
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 533..568
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 538..553
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 555..560
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 574..579
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 576..607
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 581..590
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 592..599
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 613..618
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 615..661
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 620..630
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 633..636
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 640..649
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 646..723
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 665..699
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 798 AA; 88390 MW; DA380CE35325B112 CRC64;
MNLQLIFWIG LISSVCCVFG QTDENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT
SARCDDLEAL KKKGCPPDDI ENPRGSKDIK KNKNVTNRSK GTAEKLKPED ITQIQPQQLV
LRLRSGEPQT FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTNKGE VFNELVGKQR
ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
CHLENNMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
SANSSNVIQL IIDAYNSLSS EVILENGKLS EGVTISYKSY CKNGVNGTGE NGRKCSNISI
GDEVQFEISI TSNKCPKKDS DTFKIRPLGF TEEVEVILQY ICECECQSEG IPGSPKCHEG
NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CICGQCVCRK
RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCKCRVCE CYPNYTGSAC DCSLDTSTCV
ASNGQICNGR GICECGVCKC TDPKFQGQTC EMCQTCLGVC AEHKECVQCR AFNKGEKKDT
CAQECSYFNI TKVESREKLP QPVQPDPVSH CKEKDVDDCW FYFTYSVNGN NEIMVHVVEN
PECPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN
PIYKSAVTTV VNPKYEGK
//
