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P11688 (ITA5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin alpha-5
Alternative name(s):
CD49 antigen-like family member E
Fibronectin receptor subunit alpha
Integrin alpha-F
VLA-5
CD_antigen=CD49e
Gene names
Name:Itga5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1053 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Integrin alpha-5/beta-1 is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. May play a role in the survival of adult skeletal muscle.

Subunit structure

Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-5 associates with beta-1. Interacts with NISCH. Interacts with HPS5 By similarity. Interacts with RAB21 and COMP. Interacts with CIB1 By similarity. Ref.5 Ref.6 Ref.7

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Proteolytic cleavage by PCSK5 mediates activation of the precursor By similarity.

Disruption phenotype

Mice die at day E10-E11. They show both extraembryonic and embryonic vascular defects, and severe abnormalities in the development of the posterior trunk. Ref.4

Sequence similarities

Belongs to the integrin alpha chain family.

Contains 7 FG-GAP repeats.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionIntegrin
Receptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell-cell adhesion mediated by integrin

Inferred from mutant phenotype PubMed 8557754. Source: MGI

cell-substrate junction assembly

Inferred from direct assay PubMed 12867986. Source: MGI

heterophilic cell-cell adhesion

Inferred from mutant phenotype PubMed 8557754. Source: MGI

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

leukocyte cell-cell adhesion

Inferred from mutant phenotype PubMed 8557754. Source: MGI

memory

Inferred from mutant phenotype PubMed 12904471. Source: MGI

negative regulation of anoikis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

wound healing, spreading of epidermal cells

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from direct assay PubMed 8306881. Source: MGI

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from direct assay PubMed 8557754PubMed 9553049. Source: MGI

focal adhesion

Inferred from electronic annotation. Source: Ensembl

integrin complex

Inferred from electronic annotation. Source: Ensembl

ruffle membrane

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from direct assay PubMed 12904471. Source: MGI

   Molecular_functionintegrin binding

Inferred from physical interaction PubMed 8601592. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4444 By similarity
Chain45 – 10531009Integrin alpha-5
PRO_0000016252
Chain45 – 898854Integrin alpha-5 heavy chain
PRO_0000016253
Chain899 – 1053155Integrin alpha-5 light chain
PRO_0000016254

Regions

Topological domain45 – 999955Extracellular Potential
Transmembrane1000 – 102526Helical; Potential
Topological domain1026 – 105328Cytoplasmic Potential
Repeat46 – 11166FG-GAP 1
Repeat131 – 19161FG-GAP 2
Repeat196 – 24853FG-GAP 3
Repeat262 – 31857FG-GAP 4
Repeat319 – 38062FG-GAP 5
Repeat381 – 44060FG-GAP 6
Repeat444 – 50764FG-GAP 7
Calcium binding283 – 2919 By similarity
Calcium binding337 – 3459 Potential
Calcium binding404 – 4129 Potential
Calcium binding468 – 4769 Potential
Motif1024 – 10285GFFKR motif

Sites

Metal binding2831Calcium 1 By similarity
Metal binding2851Calcium 1 By similarity
Metal binding2871Calcium 1 By similarity
Metal binding2891Calcium 1; via carbonyl oxygen By similarity
Metal binding2911Calcium 1 By similarity
Metal binding3371Calcium 2 By similarity
Metal binding3391Calcium 2 By similarity
Metal binding3411Calcium 2 By similarity
Metal binding3431Calcium 2; via carbonyl oxygen By similarity
Metal binding3451Calcium 2 By similarity
Metal binding4041Calcium 3 By similarity
Metal binding4061Calcium 3 By similarity
Metal binding4081Calcium 3 By similarity
Metal binding4101Calcium 3; via carbonyl oxygen By similarity
Metal binding4121Calcium 3 By similarity
Metal binding4681Calcium 4 By similarity
Metal binding4701Calcium 4 By similarity
Metal binding4721Calcium 4 By similarity
Metal binding4741Calcium 4; via carbonyl oxygen By similarity
Metal binding4761Calcium 4 By similarity
Binding site2651Arg of R-G-D substrate By similarity
Binding site2721Arg of R-G-D substrate By similarity

Amino acid modifications

Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Ref.9
Glycosylation3001N-linked (GlcNAc...) Ref.8
Glycosylation3101N-linked (GlcNAc...) Ref.8
Glycosylation3191N-linked (GlcNAc...) Potential
Glycosylation5271N-linked (GlcNAc...) Potential
Glycosylation5331N-linked (GlcNAc...) Potential
Glycosylation5961N-linked (GlcNAc...) Ref.8 Ref.9
Glycosylation6121N-linked (GlcNAc...) Ref.8 Ref.9
Glycosylation6751N-linked (GlcNAc...); atypical Ref.8
Glycosylation6781N-linked (GlcNAc...) Ref.8 Ref.9
Glycosylation6851N-linked (GlcNAc...); atypical Ref.8
Glycosylation7151N-linked (GlcNAc...) Ref.9
Glycosylation7271N-linked (GlcNAc...) Ref.9
Glycosylation7761N-linked (GlcNAc...) Potential
Glycosylation8721N-linked (GlcNAc...) Potential
Glycosylation8761N-linked (GlcNAc...) Ref.9
Disulfide bond102 ↔ 111 By similarity
Disulfide bond159 ↔ 179 By similarity
Disulfide bond195 ↔ 208 By similarity
Disulfide bond516 ↔ 525 By similarity
Disulfide bond531 ↔ 587 By similarity
Disulfide bond648 ↔ 654 By similarity
Disulfide bond721 ↔ 734 By similarity
Disulfide bond873 ↔ 915Interchain (between heavy and light chains) By similarity
Disulfide bond920 ↔ 925 By similarity

Experimental info

Sequence conflict681E → Q in CAA55638. Ref.1
Sequence conflict3771G → A in CAA55638. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P11688 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 8624AEF83E4A9C07

FASTA1,053115,043
        10         20         30         40         50         60 
MGSWTPRSPR SPLHAVLLRW GPRRLPPLLP LLLLLWPPPL QVGGFNLDAE APAVLSGPPG 

        70         80         90        100        110        120 
SLFGFSVEFY RPGRDGVSVL VGAPKANTSQ PGVLQGGAVY VCPWGTSPIQ CTTIQFDSKG 

       130        140        150        160        170        180 
SRILESSLYS AKGEEPVEYK SLQWFGATVR AHGSSILACA PLYSWRTEKD PQNDPVGTCY 

       190        200        210        220        230        240 
LSTENFTRIL EYAPCRSDFG SAAGQGYCQG GFSAEFTKTG RVVLGGPGSY FWQGQILSAT 

       250        260        270        280        290        300 
QEQISESYYP EYLINPVQGQ LQTRQASSVY DDSYLGYSVA VGEFSGDDTE DFVAGVPKGN 

       310        320        330        340        350        360 
LTYGYVTVLN GSDIHSLYNV SGEQMASYFG YAVAATDTNG DGLDDLLVGA PLLMERTADG 

       370        380        390        400        410        420 
RPQEVGRVYI YLQRPAGIDP TPTLTLTGQD EFSRFGSSLT PLGDLDQDGY NDVAIGAPFG 

       430        440        450        460        470        480 
GEAQQGVVFI FPGGPGGLST KPSQVLQPLW AAGRTPDFFG SALRGGRDLD GNGYPDLIVG 

       490        500        510        520        530        540 
SFGVDKALVY RGRPIISASA SLTIFPSMFN PEERSCSLEG NPVSCINLSF CLNASGKHVP 

       550        560        570        580        590        600 
NSIGFEVELQ LDWQKQKGGV RRALFLTSKQ ATLTQTLLIQ NGAREDCREM KIYLRNESEF 

       610        620        630        640        650        660 
RDKLSPIHIA LNFSLDPKAP MDSHGLRPVL HYQSKSRIED KAQILLDCGE DNICVPDLQL 

       670        680        690        700        710        720 
DVYGEKKHVY LGDKNALNLT FHAQNLGEGG AYEAELRVTA PLEAEYSGLV RHPGNFSSLS 

       730        740        750        760        770        780 
CDYFAVNQSR QLVCDLGNPM KAGTSLWGGL RFTVPHLQDT KKTIQFDFQI LSKNLNNSQS 

       790        800        810        820        830        840 
NVVSFPLSVE AQAQVSLNGV SKPEAVIFPV SDWNPQDQPQ KEEDLGPAVH HVYELINQGP 

       850        860        870        880        890        900 
SSISQGVLEL SCPQALEGQQ LLYVTKVTGL SNCTSNYTPN SQGLELDPET SPHHLQKREA 

       910        920        930        940        950        960 
PGRSSTASGT QVLKCPEAKC FRLRCEFGPL HRQESRSLQL HFRVWAKTFL QREYQPFSLQ 

       970        980        990       1000       1010       1020 
CEAVYEALKM PYQILPRQLP QKKLQVATAV QWTKAEGSNG VPLWIIILAI LFGLLLLGLL 

      1030       1040       1050 
IYVLYKLGFF KRSLPYGTAM EKAQLKPPAT SDA 

« Hide

References

« Hide 'large scale' references
[1]Morrisey E., Dutt P., Patel V.
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone marrow.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Molecular cloning of a murine fibronectin receptor and its expression during inflammation. Expression of VLA-5 is increased in activated peritoneal macrophages in a manner discordant from major histocompatibility complex class II."
Holers V.M., Ruff T.G., Parks D.L., McDonald J.A., Ballard L.L., Brown E.J.
J. Exp. Med. 169:1589-1605(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 645-1053.
Strain: BALB/c.
[4]"Embryonic mesodermal defects in alpha 5 integrin-deficient mice."
Yang J.T., Rayburn H., Hynes R.O.
Development 119:1093-1105(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[5]"Nischarin, a novel protein that interacts with the integrin alpha5 subunit and inhibits cell migration."
Alahari S.K., Lee J.W., Juliano R.L.
J. Cell Biol. 151:1141-1154(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NISCH.
Strain: ICR.
Tissue: Brain.
[6]"A membrane proximal region of the integrin alpha5 subunit is important for its interaction with nischarin."
Alahari S.K., Nasrallah H.
Biochem. J. 377:449-457(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NISCH.
[7]"The integrin-binding protein Nischarin regulates cell migration by inhibiting PAK."
Alahari S.K., Reddig P.J., Juliano R.L.
EMBO J. 23:2777-2788(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NISCH.
[8]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300; ASN-310; ASN-596; ASN-612; ASN-675; ASN-678 AND ASN-685.
Tissue: Myoblast.
[9]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185; ASN-596; ASN-612; ASN-678; ASN-715; ASN-727 AND ASN-876.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79003 mRNA. Translation: CAA55638.1.
AC131721 Genomic DNA. No translation available.
X15203 mRNA. Translation: CAA33273.1.
PIRS44250.
RefSeqNP_034707.3. NM_010577.3.
UniGeneMm.16234.

3D structure databases

ProteinModelPortalP11688.
SMRP11688. Positions 45-1037.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200818. 3 interactions.
IntActP11688. 3 interactions.
MINTMINT-4098865.
STRING10090.ENSMUSP00000023128.

PTM databases

PhosphoSiteP11688.

Proteomic databases

PaxDbP11688.
PRIDEP11688.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023128; ENSMUSP00000023128; ENSMUSG00000000555.
GeneID16402.
KEGGmmu:16402.
UCSCuc007xyb.3. mouse.

Organism-specific databases

CTD3678.
MGIMGI:96604. Itga5.

Phylogenomic databases

eggNOGNOG26407.
GeneTreeENSGT00750000117267.
HOGENOMHOG000231603.
HOVERGENHBG006186.
InParanoidP11688.
KOK06484.
OMAERSCSLE.
OrthoDBEOG7HQN77.
TreeFamTF105391.

Gene expression databases

ArrayExpressP11688.
BgeeP11688.
CleanExMM_ITGA5.
GenevestigatorP11688.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]
PfamPF01839. FG-GAP. 3 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSPR01185. INTEGRINA.
SMARTSM00191. Int_alpha. 5 hits.
[Graphical view]
PROSITEPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITGA5. mouse.
NextBio289561.
PROP11688.
SOURCESearch...

Entry information

Entry nameITA5_MOUSE
AccessionPrimary (citable) accession number: P11688
Secondary accession number(s): E9QN40
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot