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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. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei265Arg of R-G-D substrateBy similarity1
Binding sitei272Arg of R-G-D substrateBy similarity1
Metal bindingi283Calcium 1By similarity1
Metal bindingi285Calcium 1By similarity1
Metal bindingi287Calcium 1By similarity1
Metal bindingi289Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi291Calcium 1By similarity1
Metal bindingi337Calcium 2By similarity1
Metal bindingi339Calcium 2By similarity1
Metal bindingi341Calcium 2By similarity1
Metal bindingi343Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi345Calcium 2By similarity1
Metal bindingi404Calcium 3By similarity1
Metal bindingi406Calcium 3By similarity1
Metal bindingi408Calcium 3By similarity1
Metal bindingi410Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi412Calcium 3By similarity1
Metal bindingi468Calcium 4By similarity1
Metal bindingi470Calcium 4By similarity1
Metal bindingi472Calcium 4By similarity1
Metal bindingi474Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi476Calcium 4By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi283 – 291By similarity9
Calcium bindingi337 – 345Sequence analysis9
Calcium bindingi404 – 412Sequence analysis9
Calcium bindingi468 – 476Sequence analysis9

GO - Molecular functioni

  • integrin binding Source: MGI
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cell adhesion mediated by integrin Source: UniProtKB
  • cell-cell adhesion mediated by integrin Source: MGI
  • cell-substrate adhesion Source: MGI
  • cell-substrate junction assembly Source: MGI
  • endodermal cell differentiation Source: MGI
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  • heterotypic cell-cell adhesion Source: MGI
  • integrin-mediated signaling pathway Source: UniProtKB-KW
  • leukocyte cell-cell adhesion Source: MGI
  • memory Source: MGI
  • negative regulation of anoikis Source: MGI
  • positive regulation of cell migration Source: Ensembl
  • positive regulation of cell-substrate adhesion Source: Ensembl
  • positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of sprouting angiogenesis Source: MGI
  • regulation of angiogenesis Source: BHF-UCL
  • 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

ReactomeiR-MMU-1566948. Elastic fibre formation.
R-MMU-1566977. Fibronectin matrix formation.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-445144. Signal transduction by L1.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:96604. Itga5.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini45 – 999ExtracellularSequence analysisAdd BLAST955
Transmembranei1000 – 1025HelicalSequence analysisAdd BLAST26
Topological domaini1026 – 1053CytoplasmicSequence analysisAdd BLAST28

GO - Cellular componenti

  • cell-cell junction Source: Ensembl
  • cell surface Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • external side of plasma membrane Source: MGI
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • integrin complex Source: Ensembl
  • plasma membrane Source: UniProtKB
  • ruffle membrane Source: Ensembl
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 44By similarityAdd BLAST44
ChainiPRO_000001625245 – 1053Integrin alpha-5Add BLAST1009
ChainiPRO_000001625345 – 898Integrin alpha-5 heavy chainAdd BLAST854
ChainiPRO_0000016254899 – 1053Integrin alpha-5 light chainAdd BLAST155

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi87N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi102 ↔ 111By similarity
Modified residuei130PhosphoserineBy similarity1
Disulfide bondi159 ↔ 179By similarity
Glycosylationi185N-linked (GlcNAc...)1 Publication1
Disulfide bondi195 ↔ 208By similarity
Glycosylationi300N-linked (GlcNAc...)1 Publication1
Glycosylationi310N-linked (GlcNAc...)1 Publication1
Glycosylationi319N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi516 ↔ 525By similarity
Glycosylationi527N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi531 ↔ 587By similarity
Glycosylationi533N-linked (GlcNAc...)Sequence analysis1
Glycosylationi596N-linked (GlcNAc...)2 Publications1
Glycosylationi612N-linked (GlcNAc...)2 Publications1
Disulfide bondi648 ↔ 654By similarity
Glycosylationi675N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi678N-linked (GlcNAc...)2 Publications1
Glycosylationi685N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi715N-linked (GlcNAc...)1 Publication1
Disulfide bondi721 ↔ 734By similarity
Glycosylationi727N-linked (GlcNAc...)1 Publication1
Glycosylationi776N-linked (GlcNAc...)Sequence analysis1
Glycosylationi872N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi873 ↔ 915Interchain (between heavy and light chains)By similarity
Glycosylationi876N-linked (GlcNAc...)1 Publication1
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.
PeptideAtlasiP11688.
PRIDEiP11688.

PTM databases

iPTMnetiP11688.
PhosphoSitePlusiP11688.

Expressioni

Gene expression databases

BgeeiENSMUSG00000000555.
CleanExiMM_ITGA5.
GenevisibleiP11688. MM.

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 (PubMed:11121431, PubMed:14535848, PubMed:15229651). Interacts with HPS5 (By similarity). Interacts with RAB21 and COMP. Interacts with CIB1 (By similarity). ITGA5:ITGB1 interacts with NOV (By similarity). ITGA5:ITGB1 interacts with FBN1 (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
YwhaqP682542EBI-6477055,EBI-400675

GO - Molecular functioni

  • integrin binding Source: MGI

Protein-protein interaction databases

BioGridi200818. 31 interactors.
IntActiP11688. 33 interactors.
MINTiMINT-4098865.
STRINGi10090.ENSMUSP00000023128.

Structurei

3D structure databases

ProteinModelPortaliP11688.
SMRiP11688.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati46 – 111FG-GAP 1PROSITE-ProRule annotationAdd BLAST66
Repeati131 – 191FG-GAP 2PROSITE-ProRule annotationAdd BLAST61
Repeati196 – 248FG-GAP 3PROSITE-ProRule annotationAdd BLAST53
Repeati262 – 314FG-GAP 4PROSITE-ProRule annotationAdd BLAST53
Repeati315 – 380FG-GAP 5PROSITE-ProRule annotationAdd BLAST66
Repeati381 – 440FG-GAP 6PROSITE-ProRule annotationAdd BLAST60
Repeati444 – 507FG-GAP 7PROSITE-ProRule annotationAdd BLAST64

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1024 – 1028GFFKR motif5

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3637. Eukaryota.
ENOG410XPVZ. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP11688.
KOiK06484.
OMAiLHYQSKS.
OrthoDBiEOG091G05Z4.
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.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti68E → Q in CAA55638 (Ref. 1) Curated1
Sequence conflicti377G → A in CAA55638 (Ref. 1) Curated1

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_034707.5. NM_010577.4.
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_034707.5. NM_010577.4.
UniGeneiMm.16234.

3D structure databases

ProteinModelPortaliP11688.
SMRiP11688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200818. 31 interactors.
IntActiP11688. 33 interactors.
MINTiMINT-4098865.
STRINGi10090.ENSMUSP00000023128.

PTM databases

iPTMnetiP11688.
PhosphoSitePlusiP11688.

Proteomic databases

MaxQBiP11688.
PaxDbiP11688.
PeptideAtlasiP11688.
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

eggNOGiKOG3637. Eukaryota.
ENOG410XPVZ. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP11688.
KOiK06484.
OMAiLHYQSKS.
OrthoDBiEOG091G05Z4.
TreeFamiTF105391.

Enzyme and pathway databases

ReactomeiR-MMU-1566948. Elastic fibre formation.
R-MMU-1566977. Fibronectin matrix formation.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-445144. Signal transduction by L1.

Miscellaneous databases

ChiTaRSiItga5. mouse.
PROiP11688.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000555.
CleanExiMM_ITGA5.
GenevisibleiP11688. MM.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 164 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

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 one 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.