Q27874 · PAT3_CAEEL

  • Protein
    Integrin beta pat-3
  • Gene
    pat-3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

GO annotations

AspectTerm
Cellular Componentbasement membrane
Cellular Componentbasolateral plasma membrane
Cellular Componentcell surface
Cellular Componentfocal adhesion
Cellular Componentintegrin complex
Cellular Componentlateral plasma membrane
Cellular ComponentM band
Cellular Componentneuron projection
Cellular Componentneuronal cell body
Cellular Componentstriated muscle dense body
Cellular ComponentZ disc
Molecular Functionintegrin binding
Biological Processcell-cell adhesion
Biological Processintegrin-mediated signaling pathway
Biological Processmitochondrion organization
Biological Processmuscle cell cellular homeostasis
Biological Processmuscle cell development
Biological Processnegative regulation of epidermal growth factor receptor signaling pathway
Biological Processpositive regulation of axon regeneration
Biological Processpositive regulation of locomotion
Biological Processpositive regulation of myosin II filament organization
Biological Processpositive regulation of ovulation
Biological Processpositive regulation of sarcomere organization
Biological Processregulation of actin cytoskeleton organization
Biological Processregulation of distal tip cell migration
Biological Processregulation of vulval development
Biological Processstriated muscle cell development
Biological Processvulval cell fate specification

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Integrin beta pat-3
  • Alternative names
    • Paralyzed arrest at two-fold protein 3

Gene names

    • Name
      pat-3
    • ORF names
      ZK1058.2

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    Q27874

Proteomes

Organism-specific databases

Subcellular Location

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).

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain20-737Extracellular
Transmembrane738-758Helical
Topological domain759-809Cytoplasmic

Keywords

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).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis790In ok804163; Impairs axon regeneration after injury.
Mutagenesis792In 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.
Mutagenesis796-798Abolishes association with the phosphatase dep-1.

PTM/Processing

Features

Showing features for signal, chain, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000001635820-809Integrin beta pat-3
Glycosylation47N-linked (GlcNAc...) asparagine
Glycosylation141N-linked (GlcNAc...) asparagine
Glycosylation269N-linked (GlcNAc...) asparagine
Glycosylation373N-linked (GlcNAc...) asparagine
Glycosylation400N-linked (GlcNAc...) asparagine
Glycosylation530N-linked (GlcNAc...) asparagine
Glycosylation672N-linked (GlcNAc...) asparagine
Glycosylation693N-linked (GlcNAc...) asparagine
Glycosylation721N-linked (GlcNAc...) asparagine
Modified residue792Phosphotyrosine

Post-translational modification

Phosphorylated. Dephosphorylated by dep-1.

Keywords

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).

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).

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).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain153-352VWFA

Sequence similarities

Belongs to the integrin beta chain family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    809
  • Mass (Da)
    90,138
  • Last updated
    1996-11-01 v1
  • Checksum
    70C4AB01C8FE9189
MPPSTSLLLLAALLPFALPASDWKTGEVTGKVVEKSEFPCYSLSRDNYTCSACIQYHESCAWCGAPMFDEKKPYARCDSRAKLMEHGCPNSYIEDPATKLDITEDSKLSDQGQVESEEEAVQIKPQEMYVEIRPKSRVRFNVTYRQAVDYPVDLYYLMDLSYSMKDDKQKLSELGDLLAERMRTVTKNFRLGFGSFIDKKLMPFIDPRIEKQLSPCPTPCAEPYGFKHQMSLTTNTAKFKAEVDKAEISGNLDAPEGGFDAVVQALACNKTIGWRERARKMIVFSTDAGFHFAGDGRLAGVVEPNDGTCHLDREGYYTETLNQDYPSIALLHQMIKDRKANVIFAVTKNNQDLYTQLSNALPDVSSSVGVLANDSRNIVDLIEKEYLKISEKIIMVDNANASEGLKLTYRSMCLDGTTLKDTNVCEGIRVGDEVQFEVTLENTHCIDKRDFVLRIGPSGLDETLIVNVKVLCDCDCERQDRIVTNSADCNGGDMVCGVCRCKGGNVGKYCECNRPGMSTAALNEKCKRTNESAICEGRGVCNCGRCECNPRANPEEQISGEFCECDNFNCPRHDRKICAEHGECNCGKCICAPGWTGRACECPISTDSCLSANGKICNGKGECICGRCRCFDSPDGNRYSGAKCEICPTCPTKCVEYKNCVMCQQWQTGPLNETACDQCEFKVIPVEELPNLNETTPCQFVDPADDCTFYYLYYYDEATDNATVWVRKHKDCPPPVPVLAIVLGVIAGIVILGILLLLLWKLLTVLHDRSEYATFNNERLMAKWDTNENPIYKQATTTFKNPVYAGKAN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U19744
EMBL· GenBank· DDBJ
AAA85704.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284603
EMBL· GenBank· DDBJ
CAA84677.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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