Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Integrin alpha-5

Gene

Itga5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei265 – 2651Arg of R-G-D substrateBy similarity
Binding sitei272 – 2721Arg of R-G-D substrateBy similarity
Metal bindingi283 – 2831Calcium 1By similarity
Metal bindingi285 – 2851Calcium 1By similarity
Metal bindingi287 – 2871Calcium 1By similarity
Metal bindingi289 – 2891Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi291 – 2911Calcium 1By similarity
Metal bindingi337 – 3371Calcium 2By similarity
Metal bindingi339 – 3391Calcium 2By similarity
Metal bindingi341 – 3411Calcium 2By similarity
Metal bindingi343 – 3431Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi345 – 3451Calcium 2By similarity
Metal bindingi404 – 4041Calcium 3By similarity
Metal bindingi406 – 4061Calcium 3By similarity
Metal bindingi408 – 4081Calcium 3By similarity
Metal bindingi410 – 4101Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi412 – 4121Calcium 3By similarity
Metal bindingi468 – 4681Calcium 4By similarity
Metal bindingi470 – 4701Calcium 4By similarity
Metal bindingi472 – 4721Calcium 4By similarity
Metal bindingi474 – 4741Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi476 – 4761Calcium 4By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi283 – 2919By similarity
Calcium bindingi337 – 3459Sequence Analysis
Calcium bindingi404 – 4129Sequence Analysis
Calcium bindingi468 – 4769Sequence Analysis

GO - Molecular functioni

  1. integrin binding Source: MGI
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cell-cell adhesion mediated by integrin Source: MGI
  2. cell-substrate adhesion Source: MGI
  3. cell-substrate junction assembly Source: MGI
  4. endodermal cell differentiation Source: MGI
  5. heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  6. heterotypic cell-cell adhesion Source: MGI
  7. integrin-mediated signaling pathway Source: UniProtKB-KW
  8. leukocyte cell-cell adhesion Source: MGI
  9. memory Source: MGI
  10. negative regulation of anoikis Source: MGI
  11. positive regulation of cell migration Source: Ensembl
  12. positive regulation of cell-substrate adhesion Source: Ensembl
  13. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  14. wound healing, spreading of epidermal cells Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198996. Elastic fibre formation.
REACT_204211. Fibronectin matrix formation.
REACT_215461. Signal transduction by L1.
REACT_216309. Integrin cell surface interactions.
REACT_225233. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following 2 chains:
Gene namesi
Name:Itga5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:96604. Itga5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini45 – 999955ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1000 – 102526HelicalSequence AnalysisAdd
BLAST
Topological domaini1026 – 105328CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cell surface Source: UniProtKB
  3. cytoplasmic vesicle Source: UniProtKB
  4. endoplasmic reticulum Source: UniProtKB
  5. external side of plasma membrane Source: MGI
  6. focal adhesion Source: MGI
  7. Golgi apparatus Source: UniProtKB
  8. integrin complex Source: Ensembl
  9. plasma membrane Source: UniProtKB
  10. ruffle membrane Source: Ensembl
  11. synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Mice die at day E10-E11. They show both extraembryonic and embryonic vascular defects, and severe abnormalities in the development of the posterior trunk.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4444By similarityAdd
BLAST
Chaini45 – 10531009Integrin alpha-5PRO_0000016252Add
BLAST
Chaini45 – 898854Integrin alpha-5 heavy chainPRO_0000016253Add
BLAST
Chaini899 – 1053155Integrin alpha-5 light chainPRO_0000016254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi87 – 871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi102 ↔ 111By similarity
Modified residuei130 – 1301PhosphoserineBy similarity
Disulfide bondi159 ↔ 179By similarity
Glycosylationi185 – 1851N-linked (GlcNAc...)1 Publication
Disulfide bondi195 ↔ 208By similarity
Glycosylationi300 – 3001N-linked (GlcNAc...)1 Publication
Glycosylationi310 – 3101N-linked (GlcNAc...)1 Publication
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi516 ↔ 525By similarity
Glycosylationi527 – 5271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi531 ↔ 587By similarity
Glycosylationi533 – 5331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi596 – 5961N-linked (GlcNAc...)2 Publications
Glycosylationi612 – 6121N-linked (GlcNAc...)2 Publications
Disulfide bondi648 ↔ 654By similarity
Glycosylationi675 – 6751N-linked (GlcNAc...); atypical1 Publication
Glycosylationi678 – 6781N-linked (GlcNAc...)2 Publications
Glycosylationi685 – 6851N-linked (GlcNAc...); atypical1 Publication
Glycosylationi715 – 7151N-linked (GlcNAc...)1 Publication
Disulfide bondi721 ↔ 734By similarity
Glycosylationi727 – 7271N-linked (GlcNAc...)1 Publication
Glycosylationi776 – 7761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi872 – 8721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi873 ↔ 915Interchain (between heavy and light chains)By similarity
Glycosylationi876 – 8761N-linked (GlcNAc...)1 Publication
Disulfide bondi920 ↔ 925By similarity

Post-translational modificationi

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

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP11688.
PaxDbiP11688.
PRIDEiP11688.

PTM databases

PhosphoSiteiP11688.

Expressioni

Gene expression databases

BgeeiP11688.
CleanExiMM_ITGA5.
ExpressionAtlasiP11688. baseline and differential.
GenevestigatoriP11688.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi200818. 3 interactions.
IntActiP11688. 3 interactions.
MINTiMINT-4098865.
STRINGi10090.ENSMUSP00000023128.

Structurei

3D structure databases

ProteinModelPortaliP11688.
SMRiP11688. Positions 45-992.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati46 – 11166FG-GAP 1Add
BLAST
Repeati131 – 19161FG-GAP 2Add
BLAST
Repeati196 – 24853FG-GAP 3Add
BLAST
Repeati262 – 31857FG-GAP 4Add
BLAST
Repeati319 – 38062FG-GAP 5Add
BLAST
Repeati381 – 44060FG-GAP 6Add
BLAST
Repeati444 – 50764FG-GAP 7Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1024 – 10285GFFKR motif

Sequence similaritiesi

Belongs to the integrin alpha chain family.Curated
Contains 7 FG-GAP repeats.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG26407.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP11688.
KOiK06484.
OMAiERSCSLE.
OrthoDBiEOG7HQN77.
TreeFamiTF105391.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]
PfamiPF01839. FG-GAP. 3 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSWTPRSPR SPLHAVLLRW GPRRLPPLLP LLLLLWPPPL QVGGFNLDAE
60 70 80 90 100
APAVLSGPPG SLFGFSVEFY RPGRDGVSVL VGAPKANTSQ PGVLQGGAVY
110 120 130 140 150
VCPWGTSPIQ CTTIQFDSKG SRILESSLYS AKGEEPVEYK SLQWFGATVR
160 170 180 190 200
AHGSSILACA PLYSWRTEKD PQNDPVGTCY LSTENFTRIL EYAPCRSDFG
210 220 230 240 250
SAAGQGYCQG GFSAEFTKTG RVVLGGPGSY FWQGQILSAT QEQISESYYP
260 270 280 290 300
EYLINPVQGQ LQTRQASSVY DDSYLGYSVA VGEFSGDDTE DFVAGVPKGN
310 320 330 340 350
LTYGYVTVLN GSDIHSLYNV SGEQMASYFG YAVAATDTNG DGLDDLLVGA
360 370 380 390 400
PLLMERTADG RPQEVGRVYI YLQRPAGIDP TPTLTLTGQD EFSRFGSSLT
410 420 430 440 450
PLGDLDQDGY NDVAIGAPFG GEAQQGVVFI FPGGPGGLST KPSQVLQPLW
460 470 480 490 500
AAGRTPDFFG SALRGGRDLD GNGYPDLIVG SFGVDKALVY RGRPIISASA
510 520 530 540 550
SLTIFPSMFN PEERSCSLEG NPVSCINLSF CLNASGKHVP NSIGFEVELQ
560 570 580 590 600
LDWQKQKGGV RRALFLTSKQ ATLTQTLLIQ NGAREDCREM KIYLRNESEF
610 620 630 640 650
RDKLSPIHIA LNFSLDPKAP MDSHGLRPVL HYQSKSRIED KAQILLDCGE
660 670 680 690 700
DNICVPDLQL DVYGEKKHVY LGDKNALNLT FHAQNLGEGG AYEAELRVTA
710 720 730 740 750
PLEAEYSGLV RHPGNFSSLS CDYFAVNQSR QLVCDLGNPM KAGTSLWGGL
760 770 780 790 800
RFTVPHLQDT KKTIQFDFQI LSKNLNNSQS NVVSFPLSVE AQAQVSLNGV
810 820 830 840 850
SKPEAVIFPV SDWNPQDQPQ KEEDLGPAVH HVYELINQGP SSISQGVLEL
860 870 880 890 900
SCPQALEGQQ LLYVTKVTGL SNCTSNYTPN SQGLELDPET SPHHLQKREA
910 920 930 940 950
PGRSSTASGT QVLKCPEAKC FRLRCEFGPL HRQESRSLQL HFRVWAKTFL
960 970 980 990 1000
QREYQPFSLQ CEAVYEALKM PYQILPRQLP QKKLQVATAV QWTKAEGSNG
1010 1020 1030 1040 1050
VPLWIIILAI LFGLLLLGLL IYVLYKLGFF KRSLPYGTAM EKAQLKPPAT

SDA
Length:1,053
Mass (Da):115,043
Last modified:July 27, 2011 - v3
Checksum:i8624AEF83E4A9C07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681E → Q in CAA55638 (Ref. 1) Curated
Sequence conflicti377 – 3771G → A in CAA55638 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79003 mRNA. Translation: CAA55638.1.
AC131721 Genomic DNA. No translation available.
X15203 mRNA. Translation: CAA33273.1.
CCDSiCCDS27903.1.
PIRiS44250.
RefSeqiNP_034707.3. NM_010577.3.
UniGeneiMm.16234.

Genome annotation databases

EnsembliENSMUST00000023128; ENSMUSP00000023128; ENSMUSG00000000555.
GeneIDi16402.
KEGGimmu:16402.
UCSCiuc007xyb.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79003 mRNA. Translation: CAA55638.1.
AC131721 Genomic DNA. No translation available.
X15203 mRNA. Translation: CAA33273.1.
CCDSiCCDS27903.1.
PIRiS44250.
RefSeqiNP_034707.3. NM_010577.3.
UniGeneiMm.16234.

3D structure databases

ProteinModelPortaliP11688.
SMRiP11688. Positions 45-992.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200818. 3 interactions.
IntActiP11688. 3 interactions.
MINTiMINT-4098865.
STRINGi10090.ENSMUSP00000023128.

PTM databases

PhosphoSiteiP11688.

Proteomic databases

MaxQBiP11688.
PaxDbiP11688.
PRIDEiP11688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023128; ENSMUSP00000023128; ENSMUSG00000000555.
GeneIDi16402.
KEGGimmu:16402.
UCSCiuc007xyb.3. mouse.

Organism-specific databases

CTDi3678.
MGIiMGI:96604. Itga5.

Phylogenomic databases

eggNOGiNOG26407.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP11688.
KOiK06484.
OMAiERSCSLE.
OrthoDBiEOG7HQN77.
TreeFamiTF105391.

Enzyme and pathway databases

ReactomeiREACT_198996. Elastic fibre formation.
REACT_204211. Fibronectin matrix formation.
REACT_215461. Signal transduction by L1.
REACT_216309. Integrin cell surface interactions.
REACT_225233. Cell surface interactions at the vascular wall.

Miscellaneous databases

ChiTaRSiItga5. mouse.
NextBioi289561.
PROiP11688.
SOURCEiSearch...

Gene expression databases

BgeeiP11688.
CleanExiMM_ITGA5.
ExpressionAtlasiP11688. baseline and differential.
GenevestigatoriP11688.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]
PfamiPF01839. FG-GAP. 3 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiITA5_MOUSE
AccessioniPrimary (citable) accession number: P11688
Secondary accession number(s): E9QN40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 27, 2011
Last modified: March 4, 2015
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.