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Protein

Integrin beta pat-3

Gene

pat-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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:19023419, PubMed:17326220, 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). 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).Curated5 Publications

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • integrin-mediated signaling pathway Source: UniProtKB-KW
  • muscle cell development Source: WormBase
  • negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  • positive regulation of distal tip cell migration Source: UniProtKB
  • positive regulation of locomotion Source: WormBase
  • positive regulation of myosin II filament organization Source: UniProtKB
  • positive regulation of ovulation Source: UniProtKB
  • positive regulation of sarcomere organization Source: UniProtKB
  • positive regulation of smooth muscle contraction Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of distal tip cell migration Source: UniProtKB
  • regulation of vulval development Source: UniProtKB
  • striated muscle cell development Source: UniProtKB
  • vulval cell fate specification Source: UniProtKB

Keywordsi

Molecular functionIntegrin, Receptor
Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-CEL-1566948. Elastic fibre formation.
R-CEL-216083. Integrin cell surface interactions.
R-CEL-445144. Signal transduction by L1.
R-CEL-446343. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
R-CEL-6798695. Neutrophil degranulation.
R-CEL-8874081. MET activates PTK2 signaling.
R-CEL-8875513. MET interacts with TNS proteins.
SignaLinkiQ27874.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin beta pat-3
Alternative name(s):
Paralyzed arrest at two-fold protein 3
Gene namesi
Name:pat-3
ORF Names:ZK1058.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiZK1058.2; CE01102; WBGene00003930; pat-3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 737ExtracellularSequence analysisAdd BLAST718
Transmembranei738 – 758HelicalSequence analysisAdd BLAST21
Topological domaini759 – 809CytoplasmicSequence analysisAdd BLAST51

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

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).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi792Y → F 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. 1 Publication1
Mutagenesisi796 – 798TTT → AAA: Abolishes association with the phosphatase dep-1. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001635820 – 809Integrin beta pat-3Add BLAST790

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi47N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi141N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi269N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi373N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi400N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi530N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi672N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi693N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi721N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei792Phosphotyrosine1 Publication1

Post-translational modificationi

Phosphorylated. Dephosphorylated by dep-1.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ27874.
PaxDbiQ27874.
PeptideAtlasiQ27874.
PRIDEiQ27874.

Expressioni

Tissue specificityi

Expressed in body wall muscles (at protein level) (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).3 Publications

Developmental stagei

Expressed in embryos (PubMed:9247263, PubMed:23283987). Highly expressed in mid to late L3 stage larvae (PubMed:28135265).3 Publications

Gene expression databases

BgeeiWBGene00003930.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit (Probable). Interacts with alpha subunit ina-1 (PubMed:9247263). Interacts with alpha subunit pat-2 (Probable).Curated1 Publication

Protein-protein interaction databases

BioGridi40742. 11 interactors.
DIPiDIP-27060N.
IntActiQ27874. 5 interactors.
MINTiMINT-1114713.
STRINGi6239.ZK1058.2.

Structurei

3D structure databases

ProteinModelPortaliQ27874.
SMRiQ27874.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini153 – 352VWFAAdd BLAST200

Sequence similaritiesi

Belongs to the integrin beta chain family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
InParanoidiQ27874.
KOiK05719.
OMAiFFDEDDC.
OrthoDBiEOG091G029W.
PhylomeDBiQ27874.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
InterProiView protein in InterPro
IPR013111. EGF_extracell.
IPR033760. Integrin_beta_N.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR012896. Integrin_bsu_tail.
IPR002369. Integrin_bsu_VWA.
IPR032695. Integrin_dom.
IPR002035. VWF_A.
PANTHERiPTHR10082. PTHR10082. 1 hit.
PfamiView protein in Pfam
PF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
PF17205. PSI_integrin. 1 hit.
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiView protein in SMART
SM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiView protein in PROSITE
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q27874-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPSTSLLLL AALLPFALPA SDWKTGEVTG KVVEKSEFPC YSLSRDNYTC
60 70 80 90 100
SACIQYHESC AWCGAPMFDE KKPYARCDSR AKLMEHGCPN SYIEDPATKL
110 120 130 140 150
DITEDSKLSD QGQVESEEEA VQIKPQEMYV EIRPKSRVRF NVTYRQAVDY
160 170 180 190 200
PVDLYYLMDL SYSMKDDKQK LSELGDLLAE RMRTVTKNFR LGFGSFIDKK
210 220 230 240 250
LMPFIDPRIE KQLSPCPTPC AEPYGFKHQM SLTTNTAKFK AEVDKAEISG
260 270 280 290 300
NLDAPEGGFD AVVQALACNK TIGWRERARK MIVFSTDAGF HFAGDGRLAG
310 320 330 340 350
VVEPNDGTCH LDREGYYTET LNQDYPSIAL LHQMIKDRKA NVIFAVTKNN
360 370 380 390 400
QDLYTQLSNA LPDVSSSVGV LANDSRNIVD LIEKEYLKIS EKIIMVDNAN
410 420 430 440 450
ASEGLKLTYR SMCLDGTTLK DTNVCEGIRV GDEVQFEVTL ENTHCIDKRD
460 470 480 490 500
FVLRIGPSGL DETLIVNVKV LCDCDCERQD RIVTNSADCN GGDMVCGVCR
510 520 530 540 550
CKGGNVGKYC ECNRPGMSTA ALNEKCKRTN ESAICEGRGV CNCGRCECNP
560 570 580 590 600
RANPEEQISG EFCECDNFNC PRHDRKICAE HGECNCGKCI CAPGWTGRAC
610 620 630 640 650
ECPISTDSCL SANGKICNGK GECICGRCRC FDSPDGNRYS GAKCEICPTC
660 670 680 690 700
PTKCVEYKNC VMCQQWQTGP LNETACDQCE FKVIPVEELP NLNETTPCQF
710 720 730 740 750
VDPADDCTFY YLYYYDEATD NATVWVRKHK DCPPPVPVLA IVLGVIAGIV
760 770 780 790 800
ILGILLLLLW KLLTVLHDRS EYATFNNERL MAKWDTNENP IYKQATTTFK

NPVYAGKAN
Length:809
Mass (Da):90,138
Last modified:November 1, 1996 - v1
Checksum:i70C4AB01C8FE9189
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19744 Genomic DNA. Translation: AAA85704.1.
Z35604 Genomic DNA. Translation: CAA84677.1.
PIRiA57283.
RefSeqiNP_497787.1. NM_065386.5.
UniGeneiCel.5347.

Genome annotation databases

EnsemblMetazoaiZK1058.2; ZK1058.2; WBGene00003930.
GeneIDi175504.
KEGGicel:CELE_ZK1058.2.
UCSCiZK1058.2. c. elegans.

Similar proteinsi

Entry informationi

Entry nameiPAT3_CAEEL
AccessioniPrimary (citable) accession number: Q27874
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: September 27, 2017
This is version 151 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families