ITB5_MOUSE
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 03-AUG-2022, entry version 170.
DE RecName: Full=Integrin beta-5;
DE Flags: Precursor;
GN Name=Itgb5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 of a
RT novel sequence mediating granulocyte-macrophage colony-stimulating factor-
RT dependent repression of beta5 integrin gene 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., Minamisawa S.,
RA Cheng C.F., Kobuke K., Dalton N., Takada Y., Tashiro K., Ross J., Honjo T.,
RA 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., Ginsberg M.H.;
RT "Integrin beta cytoplasmic domain interactions with phosphotyrosine-binding
RT domains: a structural prototype for diversity in integrin 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 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 (ITGB5)
CC associates with alpha-V (ITGAV) (Probable). Interacts with MYO10 (By
CC similarity). Interacts with DAB2. Integrin ITGAV:ITGB5 interacts with
CC FBLN5 (via N-terminus) (PubMed:11805835). ITGAV:ITGB5 interacts with
CC CCN3 (By similarity). {ECO:0000250|UniProtKB:P18084,
CC ECO:0000269|PubMed:11805835, ECO:0000269|PubMed:12606711,
CC ECO:0000305|PubMed:11805835}.
CC -!- INTERACTION:
CC O70309; P97479: Myo7a; NbExp=3; IntAct=EBI-8401821, EBI-1149557;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane 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. {ECO:0000305}.
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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 AlphaFoldDB; O70309; -.
DR SMR; O70309; -.
DR BioGRID; 200832; 10.
DR ComplexPortal; CPX-3131; Integrin alphav-beta5 complex.
DR IntAct; O70309; 1.
DR MINT; O70309; -.
DR STRING; 10090.ENSMUSP00000069416; -.
DR ChEMBL; CHEMBL4523628; -.
DR GlyConnect; 2406; 1 N-Linked glycan (1 site).
DR GlyGen; O70309; 7 sites, 1 N-linked glycan (1 site).
DR iPTMnet; O70309; -.
DR PhosphoSitePlus; O70309; -.
DR EPD; O70309; -.
DR MaxQB; O70309; -.
DR PaxDb; O70309; -.
DR PeptideAtlas; O70309; -.
DR PRIDE; O70309; -.
DR ProteomicsDB; 268900; -. [O70309-1]
DR ProteomicsDB; 268901; -. [O70309-2]
DR DNASU; 16419; -.
DR GeneID; 16419; -.
DR KEGG; mmu:16419; -.
DR CTD; 3693; -.
DR MGI; MGI:96614; Itgb5.
DR eggNOG; KOG1226; Eukaryota.
DR InParanoid; O70309; -.
DR OrthoDB; 473040at2759; -.
DR Reactome; R-MMU-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-MMU-3000170; Syndecan interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR BioGRID-ORCS; 16419; 13 hits in 74 CRISPR screens.
DR ChiTaRS; Itgb5; mouse.
DR PRO; PR:O70309; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70309; protein.
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: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:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
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; Disulfide bond; Glycoprotein;
KW Integrin; Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..798
FT /note="Integrin beta-5"
FT /id="PRO_0000016349"
FT TOPO_DOM 24..719
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..798
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 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18084"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
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 505
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 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 705
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..682
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..657
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..714
FT /evidence="ECO:0000250"
FT DISULFID 661..690
FT /evidence="ECO:0000250"
FT VAR_SEQ 760..798
FT /note="ERSRARYEMASNPLYRKPISTHTVDFAFNKFNKSYNGSV -> LKPPVQKAH
FT LHTHCRFRLQQVQQILQWLSGLRLLDGWRGTKDEDSGVPWTSWTICSR (in
FT isoform Beta-5B)"
FT /evidence="ECO:0000303|PubMed:9531507"
FT /id="VSP_002752"
FT CONFLICT 96
FT /note="S -> C (in Ref. 2; AAD08782)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="C -> Y (in Ref. 2; AAD08782)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="K -> R (in Ref. 2; AAD08782)"
FT /evidence="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
