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Database: UniProt
Entry: F6WLF2_CALJA
LinkDB: F6WLF2_CALJA
Original site: F6WLF2_CALJA 
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}.
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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
//
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