Q27874 · PAT3_CAEEL
- ProteinIntegrin beta pat-3
- Genepat-3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids809 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Integrin alpha ina-1/beta pat-3 is a receptor for laminin. Integrin alpha pat-2/beta pat-3 recognizes the sequence R-G-D in its ligands (Probable). Plays a role in cell migration, morphogenesis and probably in cell-cell interactions (PubMed:17326220, PubMed:19023419, PubMed:23283987).
During gonad morphogenesis, involved in distal tip cell (DTC)-mediated guidance of gonad elongation, in maintaining their sharp tapering morphology and in their migration (PubMed:19023419).
Component of an integrin containing attachment complex, which is required for muscle development and maintenance (PubMed:22253611).
Involved in the assembly of dense bodies and M lines during body wall muscle embryonic development by recruiting one of their components, cpna-1, to integrin-mediated attachment sites (PubMed:23283987).
May play a similar role in the assembly of dense bodies in gonadal myoepithelial sheath cells (PubMed:17326220).
Probably by acting as a receptor for apoptotic cells, plays a role in the clearance of apoptotic cells during mid-embryogenesis (PubMed:20226672).
Required for ovulation (PubMed:17326220).
Dephosphorylated, probably within the alpha pat-2/beta pat-3 integrin receptor complex, by the phosphatase dep-1, which leads to down-stream effects including the negative regulation of let-23 signaling and vulval induction (PubMed:28135265).
When unphosphosphorylated, recruits the cytoplasmic adapter protein tln-1 to the plasma membrane of secondary vulval precursor cells (PubMed:28135265).
This promotes the linking of focal adhesion sites to the F-actin cytoskeleton, and it also acts to restrict the mobility of the let-23 receptor on the plasma membrane of vulval cells which thereby attenuates let-23 signaling (PubMed:28135265).
Plays a role in axon regeneration after injury (PubMed:31109965).
During gonad morphogenesis, involved in distal tip cell (DTC)-mediated guidance of gonad elongation, in maintaining their sharp tapering morphology and in their migration (PubMed:19023419).
Component of an integrin containing attachment complex, which is required for muscle development and maintenance (PubMed:22253611).
Involved in the assembly of dense bodies and M lines during body wall muscle embryonic development by recruiting one of their components, cpna-1, to integrin-mediated attachment sites (PubMed:23283987).
May play a similar role in the assembly of dense bodies in gonadal myoepithelial sheath cells (PubMed:17326220).
Probably by acting as a receptor for apoptotic cells, plays a role in the clearance of apoptotic cells during mid-embryogenesis (PubMed:20226672).
Required for ovulation (PubMed:17326220).
Dephosphorylated, probably within the alpha pat-2/beta pat-3 integrin receptor complex, by the phosphatase dep-1, which leads to down-stream effects including the negative regulation of let-23 signaling and vulval induction (PubMed:28135265).
When unphosphosphorylated, recruits the cytoplasmic adapter protein tln-1 to the plasma membrane of secondary vulval precursor cells (PubMed:28135265).
This promotes the linking of focal adhesion sites to the F-actin cytoskeleton, and it also acts to restrict the mobility of the let-23 receptor on the plasma membrane of vulval cells which thereby attenuates let-23 signaling (PubMed:28135265).
Plays a role in axon regeneration after injury (PubMed:31109965).
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIntegrin beta pat-3
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ27874
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Lateral cell membrane ; Single-pass type I membrane protein
Basolateral cell membrane ; Single-pass type I membrane protein
Note: In body wall muscle cells localizes to the base of thick filament M-lines, dense bodies (Z-disks) and in adhesion plaques which form between adjacent cells (PubMed:20385102, PubMed:22479198).
In body wall muscles, colocalizes with cpna-1 at integrin adhesion structures (M line and dense bodies) (PubMed:23283987).
Decreased localization to dense bodies during the L2/L3 molt (PubMed:20385102).
In myoepithelial sheath cells, colocalizes in dense bodies-like structures with actin thin filaments, deb-1/vinculin and unc-52 (PubMed:17326220).
In body wall muscles, colocalizes with cpna-1 at integrin adhesion structures (M line and dense bodies) (PubMed:23283987).
Decreased localization to dense bodies during the L2/L3 molt (PubMed:20385102).
In myoepithelial sheath cells, colocalizes in dense bodies-like structures with actin thin filaments, deb-1/vinculin and unc-52 (PubMed:17326220).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-737 | Extracellular | ||||
Sequence: ASDWKTGEVTGKVVEKSEFPCYSLSRDNYTCSACIQYHESCAWCGAPMFDEKKPYARCDSRAKLMEHGCPNSYIEDPATKLDITEDSKLSDQGQVESEEEAVQIKPQEMYVEIRPKSRVRFNVTYRQAVDYPVDLYYLMDLSYSMKDDKQKLSELGDLLAERMRTVTKNFRLGFGSFIDKKLMPFIDPRIEKQLSPCPTPCAEPYGFKHQMSLTTNTAKFKAEVDKAEISGNLDAPEGGFDAVVQALACNKTIGWRERARKMIVFSTDAGFHFAGDGRLAGVVEPNDGTCHLDREGYYTETLNQDYPSIALLHQMIKDRKANVIFAVTKNNQDLYTQLSNALPDVSSSVGVLANDSRNIVDLIEKEYLKISEKIIMVDNANASEGLKLTYRSMCLDGTTLKDTNVCEGIRVGDEVQFEVTLENTHCIDKRDFVLRIGPSGLDETLIVNVKVLCDCDCERQDRIVTNSADCNGGDMVCGVCRCKGGNVGKYCECNRPGMSTAALNEKCKRTNESAICEGRGVCNCGRCECNPRANPEEQISGEFCECDNFNCPRHDRKICAEHGECNCGKCICAPGWTGRACECPISTDSCLSANGKICNGKGECICGRCRCFDSPDGNRYSGAKCEICPTCPTKCVEYKNCVMCQQWQTGPLNETACDQCEFKVIPVEELPNLNETTPCQFVDPADDCTFYYLYYYDEATDNATVWVRKHKDCPPPVP | ||||||
Transmembrane | 738-758 | Helical | ||||
Sequence: VLAIVLGVIAGIVILGILLLL | ||||||
Topological domain | 759-809 | Cytoplasmic | ||||
Sequence: LWKLLTVLHDRSEYATFNNERLMAKWDTNENPIYKQATTTFKNPVYAGKAN |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown in distal tip cell (DTC) causes DTC migration and guidance defects during the second phase of gonad elongation resulting in a triangular shaped gonad (PubMed:19023419).
Embryos at the comma and 1.5-fold stages have increased number of cell corpses (PubMed:20226672).
RNAi-mediated knockdown causes an accumulation in the proximal gonad of endomitotic mature oocytes (PubMed:17326220).
RNAi-mediated knockdown results in increased mobility of let-23 receptor on the plasma membrane of vulval cells resulting in enhanced activity of the signaling pathway (PubMed:28135265).
RNAi-mediated knockdown in vulval precursor cells in a let-60 gain of function mutant background results in increased vulval induction and an adjacent primary fate (Apf) phenotype whereby secondary vulval precursor cells transform into primary-like vulval cells (PubMed:28135265).
RNAi-mediated knockdown results in impaired mobility, mitochondrial fragmentation and disrupted integrin attachment complexes in muscle (PubMed:22253611).
This leads to degradation of muscle proteins in the cytosol, myofibrillar defects and disruption of sarcomere organization (PubMed:22253611).
Embryos at the comma and 1.5-fold stages have increased number of cell corpses (PubMed:20226672).
RNAi-mediated knockdown causes an accumulation in the proximal gonad of endomitotic mature oocytes (PubMed:17326220).
RNAi-mediated knockdown results in increased mobility of let-23 receptor on the plasma membrane of vulval cells resulting in enhanced activity of the signaling pathway (PubMed:28135265).
RNAi-mediated knockdown in vulval precursor cells in a let-60 gain of function mutant background results in increased vulval induction and an adjacent primary fate (Apf) phenotype whereby secondary vulval precursor cells transform into primary-like vulval cells (PubMed:28135265).
RNAi-mediated knockdown results in impaired mobility, mitochondrial fragmentation and disrupted integrin attachment complexes in muscle (PubMed:22253611).
This leads to degradation of muscle proteins in the cytosol, myofibrillar defects and disruption of sarcomere organization (PubMed:22253611).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 790 | In ok804163; Impairs axon regeneration after injury. | ||||
Sequence: P → L | ||||||
Mutagenesis | 792 | In zh105; abolishes phosphorylation and enhances recruitment of tln-1 to the plasma membrane. Reduces the vulval lumen diameter and partially suppresses the Apf phenotype caused by hyperactive let-23 signaling in the double dep-1/lip-1 loss of function mutant. Increases vulval induction in the dep-1/lin-7 loss of function mutant. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 796-798 | Abolishes association with the phosphatase dep-1. | ||||
Sequence: TTT → AAA |
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MPPSTSLLLLAALLPFALP | ||||||
Chain | PRO_0000016358 | 20-809 | Integrin beta pat-3 | |||
Sequence: ASDWKTGEVTGKVVEKSEFPCYSLSRDNYTCSACIQYHESCAWCGAPMFDEKKPYARCDSRAKLMEHGCPNSYIEDPATKLDITEDSKLSDQGQVESEEEAVQIKPQEMYVEIRPKSRVRFNVTYRQAVDYPVDLYYLMDLSYSMKDDKQKLSELGDLLAERMRTVTKNFRLGFGSFIDKKLMPFIDPRIEKQLSPCPTPCAEPYGFKHQMSLTTNTAKFKAEVDKAEISGNLDAPEGGFDAVVQALACNKTIGWRERARKMIVFSTDAGFHFAGDGRLAGVVEPNDGTCHLDREGYYTETLNQDYPSIALLHQMIKDRKANVIFAVTKNNQDLYTQLSNALPDVSSSVGVLANDSRNIVDLIEKEYLKISEKIIMVDNANASEGLKLTYRSMCLDGTTLKDTNVCEGIRVGDEVQFEVTLENTHCIDKRDFVLRIGPSGLDETLIVNVKVLCDCDCERQDRIVTNSADCNGGDMVCGVCRCKGGNVGKYCECNRPGMSTAALNEKCKRTNESAICEGRGVCNCGRCECNPRANPEEQISGEFCECDNFNCPRHDRKICAEHGECNCGKCICAPGWTGRACECPISTDSCLSANGKICNGKGECICGRCRCFDSPDGNRYSGAKCEICPTCPTKCVEYKNCVMCQQWQTGPLNETACDQCEFKVIPVEELPNLNETTPCQFVDPADDCTFYYLYYYDEATDNATVWVRKHKDCPPPVPVLAIVLGVIAGIVILGILLLLLWKLLTVLHDRSEYATFNNERLMAKWDTNENPIYKQATTTFKNPVYAGKAN | ||||||
Glycosylation | 47 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 141 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 269 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 373 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 400 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 530 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 672 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 693 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 721 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 792 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylated. Dephosphorylated by dep-1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in body wall muscles (at protein level) (PubMed:20385102, PubMed:23283987).
Expressed in gonadal sheath cells and spermatheca (PubMed:17326220).
Expressed in vulval cells and along the basal laminae that separate the vulval cells from the uterus (at the protein level) (PubMed:28135265).
Expressed in gonadal sheath cells and spermatheca (PubMed:17326220).
Expressed in vulval cells and along the basal laminae that separate the vulval cells from the uterus (at the protein level) (PubMed:28135265).
Developmental stage
Expressed in embryos (PubMed:23283987, PubMed:9247263).
Highly expressed in mid to late L3 stage larvae (PubMed:28135265).
Expressed in adult animals (PubMed:20385102).
Highly expressed in mid to late L3 stage larvae (PubMed:28135265).
Expressed in adult animals (PubMed:20385102).
Gene expression databases
Interaction
Subunit
Heterodimer of an alpha and a beta subunit (Probable). Interacts with alpha subunit ina-1 (PubMed:9247263).
Interacts with alpha subunit pat-2 (Probable). Component of an integrin containing attachment complex, composed of at least pat-2, pat-3, pat-4, pat-6, unc-52, unc-97 and unc-112 (PubMed:22253611).
May interact with tns-1 (via C-terminus) (PubMed:31109965).
Interacts with alpha subunit pat-2 (Probable). Component of an integrin containing attachment complex, composed of at least pat-2, pat-3, pat-4, pat-6, unc-52, unc-97 and unc-112 (PubMed:22253611).
May interact with tns-1 (via C-terminus) (PubMed:31109965).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 153-352 | VWFA | ||||
Sequence: DLYYLMDLSYSMKDDKQKLSELGDLLAERMRTVTKNFRLGFGSFIDKKLMPFIDPRIEKQLSPCPTPCAEPYGFKHQMSLTTNTAKFKAEVDKAEISGNLDAPEGGFDAVVQALACNKTIGWRERARKMIVFSTDAGFHFAGDGRLAGVVEPNDGTCHLDREGYYTETLNQDYPSIALLHQMIKDRKANVIFAVTKNNQD |
Sequence similarities
Belongs to the integrin beta chain family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length809
- Mass (Da)90,138
- Last updated1996-11-01 v1
- Checksum70C4AB01C8FE9189
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U19744 EMBL· GenBank· DDBJ | AAA85704.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284603 EMBL· GenBank· DDBJ | CAA84677.1 EMBL· GenBank· DDBJ | Genomic DNA |