ID F6WLF2_CALJA Unreviewed; 1087 AA.
AC F6WLF2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB1 {ECO:0000313|Ensembl:ENSCJAP00000025265.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000025265.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000025265.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000025265.4}
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}. 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}.
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; F6WLF2; -.
DR STRING; 9483.ENSCJAP00000025265; -.
DR Ensembl; ENSCJAT00000026698.5; ENSCJAP00000025265.4; ENSCJAG00000013701.5.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01090000259987; -.
DR InParanoid; F6WLF2; -.
DR OMA; NCVCGAC; -.
DR TreeFam; TF105392; -.
DR Proteomes; UP000008225; Chromosome 7.
DR Bgee; ENSCJAG00000013701; Expressed in ovary and 6 other cell types or tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0034665; C:integrin alpha1-beta1 complex; IEA:Ensembl.
DR GO; GO:0034680; C:integrin alpha10-beta1 complex; IEA:Ensembl.
DR GO; GO:0034681; C:integrin alpha11-beta1 complex; IEA:Ensembl.
DR GO; GO:0034666; C:integrin alpha2-beta1 complex; IEA:Ensembl.
DR GO; GO:0034667; C:integrin alpha3-beta1 complex; IEA:Ensembl.
DR GO; GO:0034674; C:integrin alpha5-beta1 complex; IEA:Ensembl.
DR GO; GO:0034682; C:integrin alphav-beta1 complex; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0019960; F:C-X3-C chemokine binding; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0023035; P:CD40 signaling pathway; IEA:Ensembl.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; 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:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:2000811; P:negative regulation of anoikis; IEA:Ensembl.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
DR GO; GO:0010710; P:regulation of collagen catabolic process; 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 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 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 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:UP000008225};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1015..1037
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..362
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 320..750
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 926..1014
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 1038..1084
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT REGION 98..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1087 AA; 119466 MW; A678134E19465CA4 CRC64;
MDFQINLSKA AHNSPFSKTF PIPTLRGTHG LPQVFTFFLD TRKHILTPGK QSWLSQFPSR
RTTLFLPPWS PAGSGAQVPI CLGTEGGASW VQDLTGSKRD ISGQTGREVG RAAPRKRNQK
TLAQEATPGT RGALGRTRPL TPFTEEETEA RDGLCGVSAP PSTVSPKARS RAGRFLCPGS
ASCLLLAPGP ADAAGEECVS GGSGRRLRPR ERDRTRREGG AAASFLPGGG SGPPSPLLPP
LRGRSRRRPP RPRPGRPRQP AREAEREPRS SRPEPTAPGL GRRAGKMNLQ LIFWIGLISS
VCCVFGQTDE NRCLKANAKS CGECIQAGPN CGWCTNSTFL QEGMPTSARC DDLEALKKKG
CPPDDIENPR GSKDIKKNKN VTNRSKGTAE KLKPEDITQI QPQQLVLRLR SGEPQTFTLK
FKRAEDYPID LYYLMDLSYS MKDDLENVKS LGTDLMNEMR RITSDFRIGF GSFVEKTVMP
YISTTPAKLR NPCTSEQNCT SPFSYKNVLS LTNKGEVFNE LVGKQRISGN LDSPEGGFDA
IMQVAVCGSL IGWRNVTRLL VFSTDAGFHF AGDGKLGGIV LPNDGQCHLE NNMYTMSHYY
DYPSIAHLVQ KLSENNIQTI FAVTEEFQPV YKELKNLIPK SAVGTLSSNS SNVIQLIIDA
YNSLSSEVIL ENSKLSEGVT ISYKSYCKNG VNGTGENGRK CSNISIGDEV QFEISITSNK
CPKKDSDAFK IRPLGFTEEV EVILQYICEC ECQSEGIPGS PKCHEGNGTF ECGACRCNEG
RVGRHCECST DEVNSEDMDA YCRKENSSEI CSNNGECICG QCVCRKRDNT NEIYSGKFCE
CDNFNCDRSN GLICGGNGVC KCRVCECYPN YTGSACDCSL DTSTCVASNG QICNGRGICE
CGVCKCTDPK FQGQTCEMCQ TCLGVCAEHK ECVQCRAFNK GEKKDTCAQE CSYFNITKVE
SREKLPQPVQ PDPVSHCKEK DVDDCWFYFT YSVNGNNEIM VHVVENPECP TGPDIIPIVA
GVVAGIVLIG LALLLIWKLL MIIHDRREFA KFEKEKMNAK WDTQENPIYK SPINNFKNPN
YGRKTGL
//