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Database: UniProt
Entry: P80747
LinkDB: P80747
Original site: P80747 
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   13-FEB-2019, entry version 105.
DE   RecName: Full=Integrin beta-5;
DE   Flags: Precursor;
GN   Name=ITGB5;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
RT   phospholipids 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
CC       (ITGB5) associates with alpha-V (ITGAV). Interacts with MYO10.
CC       Interacts with DAB2. Integrin ITGAV:ITGB5 interacts with FBLN5
CC       (via N-terminus) (By similarity). ITGAV:ITGB5 interacts with CCN3
CC       (By similarity). {ECO:0000250|UniProtKB:O70309,
CC       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.
CC       {ECO:0000305}.
DR   EMBL; BC133358; AAI33359.1; -; mRNA.
DR   UniGene; Bt.9502; -.
DR   ProteinModelPortal; P80747; -.
DR   SMR; P80747; -.
DR   STRING; 9913.ENSBTAP00000018278; -.
DR   PaxDb; P80747; -.
DR   PRIDE; P80747; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
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: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; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Integrin; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:9154926}.
FT   CHAIN        25    800       Integrin beta-5.
FT                                /FTId=PRO_0000174221.
FT   TOPO_DOM     25    722       Extracellular. {ECO:0000255}.
FT   TRANSMEM    723    743       Helical. {ECO:0000255}.
FT   TOPO_DOM    744    800       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       27     76       PSI.
FT   DOMAIN      136    378       VWFA.
FT   REPEAT      465    512       I.
FT   REPEAT      513    554       II.
FT   REPEAT      555    593       III.
FT   REPEAT      594    630       IV.
FT   REGION      465    630       Cysteine-rich tandem repeats.
FT   MOD_RES     771    771       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P18084}.
FT   CARBOHYD    347    347       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    479    479       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    552    552       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    586    586       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    655    655       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    706    706       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     28    463       {ECO:0000250}.
FT   DISULFID     36     46       {ECO:0000250}.
FT   DISULFID     39     75       {ECO:0000250}.
FT   DISULFID     49     64       {ECO:0000250}.
FT   DISULFID    202    211       {ECO:0000250}.
FT   DISULFID    259    300       {ECO:0000250}.
FT   DISULFID    401    413       {ECO:0000250}.
FT   DISULFID    433    683       {ECO:0000250}.
FT   DISULFID    461    465       {ECO:0000250}.
FT   DISULFID    476    487       {ECO:0000250}.
FT   DISULFID    484    522       {ECO:0000250}.
FT   DISULFID    489    498       {ECO:0000250}.
FT   DISULFID    500    513       {ECO:0000250}.
FT   DISULFID    528    533       {ECO:0000250}.
FT   DISULFID    530    563       {ECO:0000250}.
FT   DISULFID    535    548       {ECO:0000250}.
FT   DISULFID    550    555       {ECO:0000250}.
FT   DISULFID    569    574       {ECO:0000250}.
FT   DISULFID    571    602       {ECO:0000250}.
FT   DISULFID    576    585       {ECO:0000250}.
FT   DISULFID    587    594       {ECO:0000250}.
FT   DISULFID    608    613       {ECO:0000250}.
FT   DISULFID    610    658       {ECO:0000250}.
FT   DISULFID    615    625       {ECO:0000250}.
FT   DISULFID    628    631       {ECO:0000250}.
FT   DISULFID    635    644       {ECO:0000250}.
FT   DISULFID    641    715       {ECO:0000250}.
FT   DISULFID    662    691       {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
//
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