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Database: UniProt
Entry: O70309
LinkDB: O70309
Original site: O70309 
ID   ITB5_MOUSE              Reviewed;         798 AA.
AC   O70309; O70308; O88347;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   13-FEB-2019, entry version 155.
DE   RecName: Full=Integrin beta-5;
DE   Flags: Precursor;
GN   Name=Itgb5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-5A AND BETA-5B).
RC   TISSUE=Liver;
RX   PubMed=9531507; DOI=10.1042/bj3310631;
RA   Zhang H., Tan S.M., Lu J.;
RT   "cDNA cloning reveals two mouse beta5 integrin transcripts distinct in
RT   cytoplasmic domains as a result of alternative splicing.";
RL   Biochem. J. 331:631-637(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-5A).
RC   TISSUE=Brain;
RX   PubMed=9880508; DOI=10.1074/jbc.274.3.1366;
RA   Feng X., Teitelbaum S.L., Quiroz M.E., Towler D.A., Ross F.P.;
RT   "Cloning of the murine beta5 integrin subunit promoter. Identification
RT   of a novel sequence mediating granulocyte-macrophage colony-
RT   stimulating factor-dependent repression of beta5 integrin gene
RT   transcription.";
RL   J. Biol. Chem. 274:1366-1374(1999).
RN   [3]
RP   INTERACTION WITH FBLN5.
RX   PubMed=11805835; DOI=10.1038/415171a;
RA   Nakamura T., Lozano P.R., Ikeda Y., Iwanaga Y., Hinek A.,
RA   Minamisawa S., Cheng C.F., Kobuke K., Dalton N., Takada Y.,
RA   Tashiro K., Ross J., Honjo T., Chien K.R.;
RT   "Fibulin-5/DANCE is essential for elastogenesis in vivo.";
RL   Nature 415:171-175(2002).
RN   [4]
RP   INTERACTION WITH DAB2.
RX   PubMed=12606711; DOI=10.1073/pnas.262791999;
RA   Calderwood D.A., Fujioka Y., de Pereda J.M., Garcia-Alvarez B.,
RA   Nakamoto T., Margolis B., McGlade C.J., Liddington R.C.,
RA   Ginsberg M.H.;
RT   "Integrin beta cytoplasmic domain interactions with phosphotyrosine-
RT   binding domains: a structural prototype for diversity in integrin
RT   signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2272-2277(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
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) (Probable). Interacts with
CC       MYO10 (By similarity). Interacts with DAB2. Integrin ITGAV:ITGB5
CC       interacts with FBLN5 (via N-terminus) (PubMed:11805835).
CC       ITGAV:ITGB5 interacts with CCN3 (By similarity).
CC       {ECO:0000250|UniProtKB:P18084, ECO:0000269|PubMed:11805835,
CC       ECO:0000269|PubMed:12606711, ECO:0000305|PubMed:11805835}.
CC   -!- INTERACTION:
CC       P97479:Myo7a; NbExp=3; IntAct=EBI-8401821, EBI-1149557;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Beta-5A;
CC         IsoId=O70309-1; Sequence=Displayed;
CC       Name=Beta-5B;
CC         IsoId=O70309-2; Sequence=VSP_002752;
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; AF043257; AAC40110.1; -; mRNA.
DR   EMBL; AF043256; AAC40109.1; -; mRNA.
DR   EMBL; AF022110; AAD08782.1; -; mRNA.
DR   CCDS; CCDS28135.1; -. [O70309-2]
DR   RefSeq; NP_001139356.1; NM_001145884.1.
DR   RefSeq; NP_034710.2; NM_010580.2.
DR   UniGene; Mm.6424; -.
DR   ProteinModelPortal; O70309; -.
DR   SMR; O70309; -.
DR   BioGrid; 200832; 2.
DR   ComplexPortal; CPX-3131; Integrin alphav-beta5 complex.
DR   IntAct; O70309; 2.
DR   MINT; O70309; -.
DR   STRING; 10090.ENSMUSP00000069416; -.
DR   iPTMnet; O70309; -.
DR   PhosphoSitePlus; O70309; -.
DR   EPD; O70309; -.
DR   jPOST; O70309; -.
DR   MaxQB; O70309; -.
DR   PaxDb; O70309; -.
DR   PeptideAtlas; O70309; -.
DR   PRIDE; O70309; -.
DR   GeneID; 16419; -.
DR   KEGG; mmu:16419; -.
DR   CTD; 3693; -.
DR   MGI; MGI:96614; Itgb5.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; O70309; -.
DR   KO; K06588; -.
DR   OrthoDB; 473040at2759; -.
DR   ChiTaRS; Itgb5; mouse.
DR   PRO; PR:O70309; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0099699; C:integral component of synaptic membrane; IDA:SynGO.
DR   GO; GO:0034684; C:integrin alphav-beta5 complex; IDA:BHF-UCL.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; IPI:BHF-UCL.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0090136; P:epithelial cell-cell adhesion; ISO:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
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   Alternative splicing; Cell adhesion; Complete proteome;
KW   Disulfide bond; Glycoprotein; Integrin; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    798       Integrin beta-5.
FT                                /FTId=PRO_0000016349.
FT   TOPO_DOM     24    719       Extracellular. {ECO:0000255}.
FT   TRANSMEM    720    742       Helical. {ECO:0000255}.
FT   TOPO_DOM    743    798       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     770    770       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P18084}.
FT   CARBOHYD    347    347       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    460    460       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    479    479       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    505    505       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    586    586       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    654    654       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    705    705       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    682       {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    657       {ECO:0000250}.
FT   DISULFID    615    625       {ECO:0000250}.
FT   DISULFID    628    631       {ECO:0000250}.
FT   DISULFID    635    644       {ECO:0000250}.
FT   DISULFID    641    714       {ECO:0000250}.
FT   DISULFID    661    690       {ECO:0000250}.
FT   VAR_SEQ     760    798       ERSRARYEMASNPLYRKPISTHTVDFAFNKFNKSYNGSV
FT                                -> LKPPVQKAHLHTHCRFRLQQVQQILQWLSGLRLLDGWR
FT                                GTKDEDSGVPWTSWTICSR (in isoform Beta-5B).
FT                                {ECO:0000303|PubMed:9531507}.
FT                                /FTId=VSP_002752.
FT   CONFLICT     96     96       S -> C (in Ref. 2; AAD08782).
FT                                {ECO:0000305}.
FT   CONFLICT    259    259       C -> Y (in Ref. 2; AAD08782).
FT                                {ECO:0000305}.
FT   CONFLICT    595    595       K -> R (in Ref. 2; AAD08782).
FT                                {ECO:0000305}.
SQ   SEQUENCE   798 AA;  87909 MW;  34B9D8B07E2688B0 CRC64;
     MPRVPATLYA CLLGLCALVP RLAGLNICTS GSATSCEECL LIHPKCAWCS KEYFGNPRSI
     TSRCDLKANL IRNGCEGEIE SPASSTHVLR NLPLSSKGSS ATGSDVIQMT PQEIAVSLRP
     GEQTTFQLQV RQVEDYPVDL YYLMDLSLSM KDDLENIRSL GTKLAEEMRK LTSNFRLGFG
     SFVDKDISPF SYTAPRYQTN PCIGYKLFPN CVPSFGFRHL LPLTDRVDSF NEEVRKQRVS
     RNRDAPEGGF DAVLQAAVCK EKIGWRKDAL HLLVFTTDDV PHIALDGKLG GLVQPHDGQC
     HLNEANEYTA SNQMDYPSLA LLGEKLAENN INLIFAVTKN HYMLYKNFTA LIPGTTVEIL
     HGDSKNIIQL IINAYSSIRA KVELSVWDQP EDLNLFFTAT CQDGISYPGQ RKCEGLKIGD
     TASFEVSVEA RSCPGRQAAQ SFTLRPVGFR DSLQVEVAYN CTCGCSTGLE PNSARCSGNG
     TYTCGLCECD PGYLGTRCEC QEGENQSGYQ NLCREAEGKP LCSGRGECSC NQCSCFESEF
     GRIYGPFCEC DSFSCARNKG VLCSGHGECH CGECKCHAGY IGDNCNCSTD VSTCKAKDGQ
     ICSDRGRCVC GQCQCTEPGA FGETCEKCPT CPDACSSKRD CVECLLLHQG KPDNQTCHHQ
     CKDEVITWVD TIVKDDQEAV LCFYKTAKDC VMMFSYTELP NGRSNLTVLR EPECGSAPNA
     MTILLAVVGS ILLIGMALLA IWKLLVTIHD RREFAKFQSE RSRARYEMAS NPLYRKPIST
     HTVDFAFNKF NKSYNGSV
//
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