P17852 · ITA3_CRIGR

Function

function

Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration.

Features

Showing features for binding site.

110511002003004005006007008009001,000
TypeIDPosition(s)Description
Binding site315Ca2+ 1 (UniProtKB | ChEBI)
Binding site317Ca2+ 1 (UniProtKB | ChEBI)
Binding site319Ca2+ 1 (UniProtKB | ChEBI)
Binding site323Ca2+ 1 (UniProtKB | ChEBI)
Binding site378Ca2+ 2 (UniProtKB | ChEBI)
Binding site380Ca2+ 2 (UniProtKB | ChEBI)
Binding site382Ca2+ 2 (UniProtKB | ChEBI)
Binding site386Ca2+ 2 (UniProtKB | ChEBI)
Binding site439Ca2+ 3 (UniProtKB | ChEBI)
Binding site441Ca2+ 3 (UniProtKB | ChEBI)
Binding site443Ca2+ 3 (UniProtKB | ChEBI)
Binding site445Ca2+ 3 (UniProtKB | ChEBI)
Binding site447Ca2+ 3 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentanchoring junction
Cellular Componentexternal side of plasma membrane
Cellular Componentfilopodium membrane
Cellular Componentintegrin complex
Molecular Functionintegrin binding
Molecular Functionmetal ion binding
Molecular Functionprotein heterodimerization activity
Biological Processcell adhesion mediated by integrin
Biological Processcell-cell adhesion
Biological Processcell-matrix adhesion
Biological Processintegrin-mediated signaling pathway
Biological Processleukocyte migration
Biological Processpositive regulation of protein localization to plasma membrane

Keywords

Names & Taxonomy

Protein names

Gene names

    • Name
      ITGA3

Organism names

Accessions

  • Primary accession
    P17852

Proteomes

Subcellular Location

Cell membrane ; Single-pass type I membrane protein
Cell membrane
; Lipid-anchor
Cell projection, invadopodium membrane
; Single-pass type I membrane protein
Cell projection, filopodium membrane
; Single-pass type I membrane protein
Note: Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain33-991Extracellular
Transmembrane992-1019Helical
Topological domain1020-1051Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-32
ChainPRO_000001623633-872Integrin alpha-3 heavy chain
ChainPRO_000001623533-1051Integrin alpha-3
Glycosylation86N-linked (GlcNAc...) asparagine
Disulfide bond94↔103
Disulfide bond140↔162
Disulfide bond185↔197
Disulfide bond485↔490
Disulfide bond496↔550
Glycosylation500N-linked (GlcNAc...) asparagine
Glycosylation511N-linked (GlcNAc...) asparagine
Glycosylation573N-linked (GlcNAc...) asparagine
Glycosylation605N-linked (GlcNAc...) asparagine
Disulfide bond615↔621
Glycosylation656N-linked (GlcNAc...) asparagine
Disulfide bond694↔702
Glycosylation697N-linked (GlcNAc...) asparagine
Glycosylation841N-linked (GlcNAc...) asparagine
Disulfide bond846↔904Interchain (between heavy and light chains)
ChainPRO_0000016237876-1051Integrin alpha-3 light chain
Disulfide bond911↔916
Glycosylation923N-linked (GlcNAc...) asparagine
Glycosylation926N-linked (GlcNAc...) asparagine
Glycosylation935N-linked (GlcNAc...) asparagine
Glycosylation969N-linked (GlcNAc...) asparagine

Post-translational modification

Isoform 1, but not isoform 2, is phosphorylated on serine residues.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

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-3 associates with beta-1. Interacts with HPS5. Interacts with FAP (seprase); the interaction occurs at the cell surface of invadopodia membrane in a collagen-dependent manner.

Structure

Family & Domains

Features

Showing features for repeat, region, motif.

TypeIDPosition(s)Description
Repeat38-103FG-GAP 1
Repeat110-171FG-GAP 2
Repeat185-235FG-GAP 3
Repeat236-292FG-GAP 4
Repeat293-354FG-GAP 5
Repeat356-411FG-GAP 6
Repeat415-477FG-GAP 7
Region860-888Disordered
Motif1017-1021GFFKR motif

Sequence similarities

Belongs to the integrin alpha chain family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

P17852-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    1
  • Synonyms
    Alpha-3A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    1,051
  • Mass (Da)
    116,456
  • Last updated
    2011-09-21 v3
  • Checksum
    96A8983E8DCD9D5D
MGPGPRCAPGDPGWMLGALALMVAASGRFAFAFNLDTRFLVVKEAVNPGSLFGYSVALHRQTERQQRYLLLAGAPRDLSVADGYTNRTGAVYLCPLTALKDDCERMDISEKSDPDHHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGMEDQRRMVGKCYVRGNDLQLDPGDDWQTYHNEMCNSNTDYLQTGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKDWDLSEYSYKGSEDQGNLYIGYTVQVGSAVLHPTYITVVAGAPRHQHMGAVFLLSQESGGDLKRKQVLEGTQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAVYVFMNQAGTSFPDQPSLLLHGPSRSAFGISIASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSGGLLRQPQQIVHGDKLGLPGLSTFGYSLSGKMDVDDNSYPDLLVGSLSDHIVLLRARPVINILQRTLVARPAVLDPSLCTPTSCVQVELCFAYNQSAGNPSYRRNITLAYTLEADRDRRPPRLRFARSQSAVFHGFLSMPETHCQTLELLLMDNVRDKLRPIVIAMNYSLPLRMPDRLKLGMRSLDAYPVLNQAQALENHTEVHFQKECGPDNKCDSNLQMRAAFVSEQLQPLSRLQYSRDTKKLFLSINVTNTPSRERAGEDAHEALLTLEVPPALLLSSVRPSGTCQANETILCELGNPFKRNQRMELLIAFEVIGVTLHTRDLKAQLQLSTSSHQDNLQPMTLILQVDYTLQASLSLMTHRLQSFFGGTVMGEAGMKTVEDVGSPLKYEFQVSPVGDGLAALGTLVLGLEWPYEVTNGKWLLYPTEIIIHSNESWPCQPPGNLVNPLNLILSDPGDKPHSPQRRRRQLDPGGDQGSPPVTLAAAKKAKSETVLTCASGRARCVWLECPIPDTSNVTNVTVKARVWNSTFIEDYRDFDRVRVDGWATLFLRTSIPTINMENKTTWFSVDIDSELVEELPAEIELWLVLVAVSAGLLLLGLIIILLWKCGFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY

P17852-2

  • Name
    2
  • Synonyms
    Alpha-3B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1021-1051: RARTRALYEAKRQKAEMKSQPSETERLTDDY → PTRYYRIMPKYHAVRIREEERYPPPGSTLPTKKHWVTSWQIRDRYY

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0027201021-1051in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
J05281
EMBL· GenBank· DDBJ
AAA56794.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp