P17852 · ITA3_CRIGR
- ProteinIntegrin alpha-3
- GeneITGA3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1051 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 315 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 317 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 319 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 323 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 378 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 380 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 382 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 386 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 439 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 441 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 443 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 445 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 447 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | anchoring junction | |
Cellular Component | external side of plasma membrane | |
Cellular Component | filopodium membrane | |
Cellular Component | integrin complex | |
Molecular Function | integrin binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein heterodimerization activity | |
Biological Process | cell adhesion mediated by integrin | |
Biological Process | cell-cell adhesion | |
Biological Process | cell-matrix adhesion | |
Biological Process | integrin-mediated signaling pathway | |
Biological Process | leukocyte migration | |
Biological Process | positive regulation of protein localization to plasma membrane |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameIntegrin alpha-3
- Alternative names
- Cleaved into 2 chains
- CD Antigen Name
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Cricetulus
Accessions
- Primary accessionP17852
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 33-991 | Extracellular | ||||
Sequence: FNLDTRFLVVKEAVNPGSLFGYSVALHRQTERQQRYLLLAGAPRDLSVADGYTNRTGAVYLCPLTALKDDCERMDISEKSDPDHHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGMEDQRRMVGKCYVRGNDLQLDPGDDWQTYHNEMCNSNTDYLQTGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKDWDLSEYSYKGSEDQGNLYIGYTVQVGSAVLHPTYITVVAGAPRHQHMGAVFLLSQESGGDLKRKQVLEGTQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAVYVFMNQAGTSFPDQPSLLLHGPSRSAFGISIASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSGGLLRQPQQIVHGDKLGLPGLSTFGYSLSGKMDVDDNSYPDLLVGSLSDHIVLLRARPVINILQRTLVARPAVLDPSLCTPTSCVQVELCFAYNQSAGNPSYRRNITLAYTLEADRDRRPPRLRFARSQSAVFHGFLSMPETHCQTLELLLMDNVRDKLRPIVIAMNYSLPLRMPDRLKLGMRSLDAYPVLNQAQALENHTEVHFQKECGPDNKCDSNLQMRAAFVSEQLQPLSRLQYSRDTKKLFLSINVTNTPSRERAGEDAHEALLTLEVPPALLLSSVRPSGTCQANETILCELGNPFKRNQRMELLIAFEVIGVTLHTRDLKAQLQLSTSSHQDNLQPMTLILQVDYTLQASLSLMTHRLQSFFGGTVMGEAGMKTVEDVGSPLKYEFQVSPVGDGLAALGTLVLGLEWPYEVTNGKWLLYPTEIIIHSNESWPCQPPGNLVNPLNLILSDPGDKPHSPQRRRRQLDPGGDQGSPPVTLAAAKKAKSETVLTCASGRARCVWLECPIPDTSNVTNVTVKARVWNSTFIEDYRDFDRVRVDGWATLFLRTSIPTINMENKTTWFSVDIDSELVEELPAEIE | ||||||
Transmembrane | 992-1019 | Helical | ||||
Sequence: LWLVLVAVSAGLLLLGLIIILLWKCGFF | ||||||
Topological domain | 1020-1051 | Cytoplasmic | ||||
Sequence: KRARTRALYEAKRQKAEMKSQPSETERLTDDY |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-32 | |||||
Sequence: MGPGPRCAPGDPGWMLGALALMVAASGRFAFA | ||||||
Chain | PRO_0000016236 | 33-872 | Integrin alpha-3 heavy chain | |||
Sequence: FNLDTRFLVVKEAVNPGSLFGYSVALHRQTERQQRYLLLAGAPRDLSVADGYTNRTGAVYLCPLTALKDDCERMDISEKSDPDHHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGMEDQRRMVGKCYVRGNDLQLDPGDDWQTYHNEMCNSNTDYLQTGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKDWDLSEYSYKGSEDQGNLYIGYTVQVGSAVLHPTYITVVAGAPRHQHMGAVFLLSQESGGDLKRKQVLEGTQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAVYVFMNQAGTSFPDQPSLLLHGPSRSAFGISIASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSGGLLRQPQQIVHGDKLGLPGLSTFGYSLSGKMDVDDNSYPDLLVGSLSDHIVLLRARPVINILQRTLVARPAVLDPSLCTPTSCVQVELCFAYNQSAGNPSYRRNITLAYTLEADRDRRPPRLRFARSQSAVFHGFLSMPETHCQTLELLLMDNVRDKLRPIVIAMNYSLPLRMPDRLKLGMRSLDAYPVLNQAQALENHTEVHFQKECGPDNKCDSNLQMRAAFVSEQLQPLSRLQYSRDTKKLFLSINVTNTPSRERAGEDAHEALLTLEVPPALLLSSVRPSGTCQANETILCELGNPFKRNQRMELLIAFEVIGVTLHTRDLKAQLQLSTSSHQDNLQPMTLILQVDYTLQASLSLMTHRLQSFFGGTVMGEAGMKTVEDVGSPLKYEFQVSPVGDGLAALGTLVLGLEWPYEVTNGKWLLYPTEIIIHSNESWPCQPPGNLVNPLNLILSDPGDKPHSPQR | ||||||
Chain | PRO_0000016235 | 33-1051 | Integrin alpha-3 | |||
Sequence: FNLDTRFLVVKEAVNPGSLFGYSVALHRQTERQQRYLLLAGAPRDLSVADGYTNRTGAVYLCPLTALKDDCERMDISEKSDPDHHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGMEDQRRMVGKCYVRGNDLQLDPGDDWQTYHNEMCNSNTDYLQTGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKDWDLSEYSYKGSEDQGNLYIGYTVQVGSAVLHPTYITVVAGAPRHQHMGAVFLLSQESGGDLKRKQVLEGTQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAVYVFMNQAGTSFPDQPSLLLHGPSRSAFGISIASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSGGLLRQPQQIVHGDKLGLPGLSTFGYSLSGKMDVDDNSYPDLLVGSLSDHIVLLRARPVINILQRTLVARPAVLDPSLCTPTSCVQVELCFAYNQSAGNPSYRRNITLAYTLEADRDRRPPRLRFARSQSAVFHGFLSMPETHCQTLELLLMDNVRDKLRPIVIAMNYSLPLRMPDRLKLGMRSLDAYPVLNQAQALENHTEVHFQKECGPDNKCDSNLQMRAAFVSEQLQPLSRLQYSRDTKKLFLSINVTNTPSRERAGEDAHEALLTLEVPPALLLSSVRPSGTCQANETILCELGNPFKRNQRMELLIAFEVIGVTLHTRDLKAQLQLSTSSHQDNLQPMTLILQVDYTLQASLSLMTHRLQSFFGGTVMGEAGMKTVEDVGSPLKYEFQVSPVGDGLAALGTLVLGLEWPYEVTNGKWLLYPTEIIIHSNESWPCQPPGNLVNPLNLILSDPGDKPHSPQRRRRQLDPGGDQGSPPVTLAAAKKAKSETVLTCASGRARCVWLECPIPDTSNVTNVTVKARVWNSTFIEDYRDFDRVRVDGWATLFLRTSIPTINMENKTTWFSVDIDSELVEELPAEIELWLVLVAVSAGLLLLGLIIILLWKCGFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY | ||||||
Glycosylation | 86 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 94↔103 | |||||
Sequence: CPLTALKDDC | ||||||
Disulfide bond | 140↔162 | |||||
Sequence: CAHRYTQVLWSGMEDQRRMVGKC | ||||||
Disulfide bond | 185↔197 | |||||
Sequence: CNSNTDYLQTGMC | ||||||
Disulfide bond | 485↔490 | |||||
Sequence: CTPTSC | ||||||
Disulfide bond | 496↔550 | |||||
Sequence: CFAYNQSAGNPSYRRNITLAYTLEADRDRRPPRLRFARSQSAVFHGFLSMPETHC | ||||||
Glycosylation | 500 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 511 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 573 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 605 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 615↔621 | |||||
Sequence: CGPDNKC | ||||||
Glycosylation | 656 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 694↔702 | |||||
Sequence: CQANETILC | ||||||
Glycosylation | 697 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 841 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 846↔904 | Interchain (between heavy and light chains) | ||||
Sequence: CQPPGNLVNPLNLILSDPGDKPHSPQRRRRQLDPGGDQGSPPVTLAAAKKAKSETVLTC | ||||||
Chain | PRO_0000016237 | 876-1051 | Integrin alpha-3 light chain | |||
Sequence: QLDPGGDQGSPPVTLAAAKKAKSETVLTCASGRARCVWLECPIPDTSNVTNVTVKARVWNSTFIEDYRDFDRVRVDGWATLFLRTSIPTINMENKTTWFSVDIDSELVEELPAEIELWLVLVAVSAGLLLLGLIIILLWKCGFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY | ||||||
Disulfide bond | 911↔916 | |||||
Sequence: CVWLEC | ||||||
Glycosylation | 923 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 926 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 935 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 969 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Keywords
- PTM
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 38-103 | FG-GAP 1 | ||||
Sequence: RFLVVKEAVNPGSLFGYSVALHRQTERQQRYLLLAGAPRDLSVADGYTNRTGAVYLCPLTALKDDC | ||||||
Repeat | 110-171 | FG-GAP 2 | ||||
Sequence: EKSDPDHHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGMEDQRRMVGKCYVRGNDLQL | ||||||
Repeat | 185-235 | FG-GAP 3 | ||||
Sequence: CNSNTDYLQTGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKDWDLS | ||||||
Repeat | 236-292 | FG-GAP 4 | ||||
Sequence: EYSYKGSEDQGNLYIGYTVQVGSAVLHPTYITVVAGAPRHQHMGAVFLLSQESGGDL | ||||||
Repeat | 293-354 | FG-GAP 5 | ||||
Sequence: KRKQVLEGTQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAVYVFMNQAGTSFP | ||||||
Repeat | 356-411 | FG-GAP 6 | ||||
Sequence: QPSLLLHGPSRSAFGISIASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSGGLLR | ||||||
Repeat | 415-477 | FG-GAP 7 | ||||
Sequence: QIVHGDKLGLPGLSTFGYSLSGKMDVDDNSYPDLLVGSLSDHIVLLRARPVINILQRTLVARP | ||||||
Region | 860-888 | Disordered | ||||
Sequence: LSDPGDKPHSPQRRRRQLDPGGDQGSPPV | ||||||
Motif | 1017-1021 | GFFKR motif | ||||
Sequence: GFFKR |
Sequence similarities
Belongs to the integrin alpha chain family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe 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.
- Name1
- SynonymsAlpha-3A
- Length1,051
- Mass (Da)116,456
- Last updated2011-09-21 v3
- Checksum96A8983E8DCD9D5D
P17852-2
- Name2
- SynonymsAlpha-3B
- Differences from canonical
- 1021-1051: RARTRALYEAKRQKAEMKSQPSETERLTDDY → PTRYYRIMPKYHAVRIREEERYPPPGSTLPTKKHWVTSWQIRDRYY
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_002720 | 1021-1051 | in isoform 2 | |||
Sequence: RARTRALYEAKRQKAEMKSQPSETERLTDDY → PTRYYRIMPKYHAVRIREEERYPPPGSTLPTKKHWVTSWQIRDRYY |
Keywords
- Coding sequence diversity
- Technical term