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Database: UniProt
Entry: ITB5_BOVIN
LinkDB: ITB5_BOVIN
Original site: ITB5_BOVIN 
ID   ITB5_BOVIN              Reviewed;         800 AA.
AC   P80747; A3KMX2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   24-JAN-2024, entry version 117.
DE   RecName: Full=Integrin beta-5;
DE   Flags: Precursor;
GN   Name=ITGB5;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 25-37.
RC   TISSUE=Mammary gland;
RX   PubMed=9154926; DOI=10.1021/bi963119m;
RA   Andersen M.H., Berglund L., Rasmussen J.T., Petersen T.E.;
RT   "Bovine PAS-6/7 binds alpha v beta 5 integrins and anionic phospholipids
RT   through two domains.";
RL   Biochemistry 36:5441-5446(1997).
CC   -!- FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for
CC       fibronectin. It recognizes the sequence R-G-D in its ligand.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-5 (ITGB5)
CC       associates with alpha-V (ITGAV). Interacts with MYO10. Interacts with
CC       DAB2. Integrin ITGAV:ITGB5 interacts with FBLN5 (via N-terminus) (By
CC       similarity). ITGAV:ITGB5 interacts with CCN3 (By similarity). Interacts
CC       with tensin TNS3; TNS3 also interacts with PEAK1, thus acting as an
CC       adapter molecule to bridge the association of PEAK1 with ITGB5 (By
CC       similarity). {ECO:0000250|UniProtKB:O70309,
CC       ECO:0000250|UniProtKB:P18084}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The VWFA domain (or beta I domain) contains three cation-
CC       binding sites: the ligand-associated metal ion-binding site (LIMBS or
CC       SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent
CC       MIDAS site (ADMIDAS). This domain is also part of the ligand-binding
CC       site. {ECO:0000250|UniProtKB:P05106}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR   EMBL; BC133358; AAI33359.1; -; mRNA.
DR   AlphaFoldDB; P80747; -.
DR   SMR; P80747; -.
DR   STRING; 9913.ENSBTAP00000018278; -.
DR   GlyCosmos; P80747; 6 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000018278; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   InParanoid; P80747; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR   PANTHER; PTHR10082:SF26; INTEGRIN BETA-5; 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   SMART; SM00327; VWA; 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; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS00243; INTEGRIN_BETA; 2.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Integrin; Magnesium;
KW   Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:9154926"
FT   CHAIN           25..800
FT                   /note="Integrin beta-5"
FT                   /id="PRO_0000174221"
FT   TOPO_DOM        25..722
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        723..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        744..800
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..76
FT                   /note="PSI"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          136..378
FT                   /note="VWFA"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DOMAIN          465..512
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DOMAIN          513..554
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DOMAIN          555..593
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DOMAIN          594..630
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="in MIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         149
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /note="in ADMIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="in MIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /note="in ADMIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         153
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /note="in ADMIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         184
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in LIMBS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         242
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in LIMBS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         244
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in LIMBS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         246
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in LIMBS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         247
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in LIMBS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="in MIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         362
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /note="in ADMIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   MOD_RES         771
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18084"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        479
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        552
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        586
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        655
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        706
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..46
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        36..463
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        39..64
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        49..75
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        202..211
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        259..300
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        401..413
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        433..461
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        465..484
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        476..487
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        489..498
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        500..530
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        513..528
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        522..533
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        535..548
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        550..571
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        555..569
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        563..574
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        576..585
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        587..610
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        594..608
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        602..613
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        615..625
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        628..631
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        635..683
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        641..662
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        644..658
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        691..715
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
SQ   SEQUENCE   800 AA;  88057 MW;  5ED0B33C9E7E2939 CRC64;
     MPRAPALLFS CLLGLCALVP RLPGLNICTS GSATSCEECL LIHPKCAWCF KEDFGSLRSV
     TSRCDLKANL IRNGCGVEFE SPASSTQVLR SLPLSSKGSS PAGSDVIQLT PQEVTVTLRP
     GDRTAFQLQV RQVEDYPVDL YYLMDLSLSM KDDLENIRSL GTKLAEEMRK LTSNFRLGFG
     SFVDKNISPF SYTAPRYQTN PCIGYKLFPN CVPSFGFRHL LPLTDRVDSF NEEVRKQRVS
     RNRDAPEGGF DAVLQAAVCK EKIGWRKDAL HLLVFTTDDV PHIALDGKLG GLVQPHDGQC
     HLNEANEYTA SNQMDYPSLA LLGEKLAENN INLIFAVTKN HYMLYKNFTA LIPGTTVEIL
     HGDSKNILQL IINAYNSIRS KVELSVWDQP EDLNLFFTAT CQDGVSYPGQ RKCEGLKIGD
     TASFEVSVEA RSCPSKHVQH TFTLRPVGFR DSLEVGVTYN CRCGCSAGLE PDSARCSSNG
     TYVCGLCECN PGYLGTRCEC QEGESQSGYQ NLCREAEGKP LCSGRGQCSC NQCSCFESEF
     GKIYGSFCEC DNFSCARNKG VLCSGHGECH CGECKCHAGY IGDNCNCSTD ISTCQARDGH
     ICSDRGHCVC GQCQCTEPGA FGETCEKCPT CPDACSTKRD CVECLLLHSG SSADNQTCQN
     LCKDEVITRV DTIVKDDQEA VLCFYKTAKD CVMMFTYSEL PSGKSNLTVL REPECGTAPS
     AMTILLAVVG SILLTGFALL VIWKLLVTIH DRREFAKFQS ERSRARYEMA SNPLYRKPIS
     THTVDFTFNK FNKSYNGTVD
//
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