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 25-MAY-2022, entry version 111.
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).
CC {ECO:0000250|UniProtKB:O70309, ECO:0000250|UniProtKB:P18084}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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 PaxDb; P80747; -.
DR PRIDE; P80747; -.
DR eggNOG; KOG1226; Eukaryota.
DR InParanoid; P80747; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR027067; Integrin_beta-5.
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; PTHR10082; 1.
DR PANTHER; PTHR10082:SF26; PTHR10082:SF26; 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; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 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 Cell adhesion; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Integrin; Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW 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 DOMAIN 136..378
FT /note="VWFA"
FT REPEAT 465..512
FT /note="I"
FT REPEAT 513..554
FT /note="II"
FT REPEAT 555..593
FT /note="III"
FT REPEAT 594..630
FT /note="IV"
FT REGION 465..630
FT /note="Cysteine-rich tandem repeats"
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..463
FT /evidence="ECO:0000250"
FT DISULFID 36..46
FT /evidence="ECO:0000250"
FT DISULFID 39..75
FT /evidence="ECO:0000250"
FT DISULFID 49..64
FT /evidence="ECO:0000250"
FT DISULFID 202..211
FT /evidence="ECO:0000250"
FT DISULFID 259..300
FT /evidence="ECO:0000250"
FT DISULFID 401..413
FT /evidence="ECO:0000250"
FT DISULFID 433..683
FT /evidence="ECO:0000250"
FT DISULFID 461..465
FT /evidence="ECO:0000250"
FT DISULFID 476..487
FT /evidence="ECO:0000250"
FT DISULFID 484..522
FT /evidence="ECO:0000250"
FT DISULFID 489..498
FT /evidence="ECO:0000250"
FT DISULFID 500..513
FT /evidence="ECO:0000250"
FT DISULFID 528..533
FT /evidence="ECO:0000250"
FT DISULFID 530..563
FT /evidence="ECO:0000250"
FT DISULFID 535..548
FT /evidence="ECO:0000250"
FT DISULFID 550..555
FT /evidence="ECO:0000250"
FT DISULFID 569..574
FT /evidence="ECO:0000250"
FT DISULFID 571..602
FT /evidence="ECO:0000250"
FT DISULFID 576..585
FT /evidence="ECO:0000250"
FT DISULFID 587..594
FT /evidence="ECO:0000250"
FT DISULFID 608..613
FT /evidence="ECO:0000250"
FT DISULFID 610..658
FT /evidence="ECO:0000250"
FT DISULFID 615..625
FT /evidence="ECO:0000250"
FT DISULFID 628..631
FT /evidence="ECO:0000250"
FT DISULFID 635..644
FT /evidence="ECO:0000250"
FT DISULFID 641..715
FT /evidence="ECO:0000250"
FT DISULFID 662..691
FT /evidence="ECO:0000250"
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
