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}.
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 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
//