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Q18825 (BAR1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-catenin/armadillo-related protein 1
Alternative name(s):
Protruding vulva protein 1
Suppressor of polyray 1
Gene names
Name:bar-1
Synonyms:pvl-1, spy-1
ORF Names:C54D1.6
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length811 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in the Wnt signaling pathway which affects cell fate and may regulate the stem cell divisions of seam cells during larval development. Functions as a transcriptional activator but is dependent on the interaction with pop-1. Involved in maintaining lin-39 Hox expression and regulating glr-1 abundance at the synapses. Required for mab-5 expression during Q neuroblast migration and for oxidative stress-induced daf-16 signaling. Has roles in egg laying, vulva precursor cell fate determination, Q neuroblast migration, posterior ectodermal cell P12 specification, movement, body length, male tail development and dauer induction. Functionally redundant to wrm-1 and hmp-2. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11

Subunit structure

Interacts with apr-1, axl-1, daf-16, lin-23, and pop-1 (via acidic region in N-terminus 1-44). Interacts (via ARM repeats) with pry-1. Ref.5 Ref.6 Ref.7 Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasm. Nucleus. Membrane. Cell junction. Note: Mostly cytoplasmic. Ref.1 Ref.10

Tissue specificity

Expressed in body wall muscle cells, hypodermal seam cells, gonad sheath cells and vulval precursor cells. Ref.1 Ref.4 Ref.10

Developmental stage

Detected throughout development from L1 to L4 and during adulthood. Detected from the P3.p cell stage through to P8.p. Ref.1 Ref.9 Ref.10

Miscellaneous

Worms lacking bar-1 exhibit abnormalities in vulval development due to incorrect cell fate specification, resulting in the following phenotypes, multivulva (Muv), protruding vulva (Pvl) and egg laying defective (Egl). Mutants also show defects in Q neuroblast migration, uncoordinated movement (Unc) and reduced superoxidase dismutase levels. Null mutants can be rescued by wrm-1 and hmp-2 when expressed from the bar-1 promoter. Double mutants also lacking dpy-22 show reduced body length, male tail morphology abnormalities (Mab) and dauer induction. Ref.4 Ref.6 Ref.8 Ref.10 Ref.11

Sequence similarities

Belongs to the beta-catenin family.

Contains 3 ARM repeats.

Caution

Alleles mu63 and mu349 were originally reported (Ref.3) as the mutations L130F and Q147STOP respectively. This is in conflict with WormBase and more recent literature (Ref.9) which is represented in this entry. Ref.8

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentCell junction
Cytoplasm
Membrane
Nucleus
   DomainRepeat
   Molecular functionActivator
Developmental protein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRas protein signal transduction

Inferred from genetic interaction Ref.4. Source: WormBase

Wnt signaling pathway

Inferred from mutant phenotype Ref.6. Source: WormBase

cell adhesion

Traceable author statement Ref.1. Source: UniProtKB

cell fate specification

Inferred from mutant phenotype Ref.1. Source: UniProtKB

hermaphrodite genitalia development

Inferred from mutant phenotype Ref.6. Source: WormBase

mating behavior

Inferred from mutant phenotype Ref.4. Source: WormBase

morphogenesis of an epithelium

Inferred from mutant phenotype Ref.6PubMed 15935762. Source: WormBase

oviposition

Inferred from mutant phenotype Ref.4Ref.6. Source: WormBase

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.6. Source: WormBase

positive regulation of vulval development

Inferred from mutant phenotype PubMed 12023306. Source: WormBase

regulation of backward locomotion

Inferred from mutant phenotype Ref.4. Source: WormBase

regulation of cell fate specification

Inferred from mutant phenotype Ref.4Ref.6. Source: WormBase

regulation of cell migration

Inferred from mutant phenotype Ref.4. Source: WormBase

regulation of vulval development

Inferred from mutant phenotype Ref.4Ref.6PubMed 15935762. Source: WormBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell junction

Inferred from direct assay Ref.1. Source: UniProtKB

cell-cell adherens junction

Inferred from direct assay Ref.1. Source: WormBase

cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Inferred from direct assay Ref.10. Source: WormBase

membrane

Inferred from direct assay Ref.10. Source: WormBase

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.5Ref.6Ref.7Ref.12. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.6. Source: WormBase

transcription factor binding

Inferred from physical interaction Ref.6PubMed 15935762. Source: WormBase

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 811811Beta-catenin/armadillo-related protein 1
PRO_0000372805

Regions

Repeat108 – 14740ARM 1
Repeat331 – 36939ARM 2
Repeat370 – 40839ARM 3
Region1 – 8585Involved in transcriptional activation Ref.6
Region541 – 811271Involved in transcriptional activation Ref.6

Experimental info

Mutagenesis2391S → L in ep451; interferes with neuroblast Q migration. Ref.9
Mutagenesis2781V → G in ep484; interferes with neuroblast Q migration; in association with Asn-281. Ref.9
Mutagenesis2811D → N in ep484; interferes with neuroblast Q migration; in association with Gly-278. Ref.9
Mutagenesis3691S → K in ep466; interferes with neuroblast Q migration. Ref.9
Mutagenesis4491E → K in ep487/ep478; variable interference with neuroblast Q migration. Ref.9
Mutagenesis4601R → W in ep461; interferes with neuroblast Q migration. Ref.9
Mutagenesis4821L → I in mu349; suppresses ectopic expression of mab-5 and interferes with neuroblast Q migration. Ref.3 Ref.9 Ref.11
Mutagenesis4981T → I in ep485; interferes with neuroblast Q migration. Ref.9
Mutagenesis5241G → D in ep460/mu63; suppresses ectopic expression of mab-5. Ref.3 Ref.9 Ref.11
Mutagenesis5241G → S in ep486; interferes with neuroblast Q migration. Ref.3 Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q18825 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: 97D6FFDE71BDFDFF

FASTA81192,228
        10         20         30         40         50         60 
MDLDPNLVIN HDDTNLSEAS FTMEQHTSSY SDIHMGSTPC TGHRKVDMWR NHNFDSGFQT 

        70         80         90        100        110        120 
MNHSEAPSII SSLHPSSHLS GMSSMADYEP IPTLSDQQKQ KFDGITQNQA DGQYNTVRAI 

       130        140        150        160        170        180 
PELTMLMKDQ DNEVVHKAVI LMQNIAKMEC DPMRRQNEAR IVDPRVIFTL RDLLRDKVEF 

       190        200        210        220        230        240 
PNIIRCTLGT FFHICNRQEG IDLVTRAIAE QPDIIPNLIR HIGTYPSSIY KYAILTMHSI 

       250        260        270        280        290        300 
LSDKQRGGQS VIIARQQDAI THVTPWLEAE KSEKLLPVIV DLIRVLCEKN TEQKIKFVKM 

       310        320        330        340        350        360 
GGPQKLLMLL QHRVYENLLW RTTQLLKTFS NFDAPNLVAF GGRQILANLL SHGSPRLVQS 

       370        380        390        400        410        420 
TLETLRNISD VPSKIKEDLL LKSLLELVNS RNTTIRLYSA QIMSNLVANN RHNKEFMCGN 

       430        440        450        460        470        480 
NGVVILVRAL TIATKEMGDL RDKEAQQMED YIESLICTLR HLCVGHPMSD KVQAFVFRDP 

       490        500        510        520        530        540 
ALFLHKLLTM RPVLLKHTLS LLLKVVSQHA LLAPFRSCRI GDKGFVEQLI HILRVACTQL 

       550        560        570        580        590        600 
NVQESIEGVR VKDIIHLCIQ ILRWITRDQD ILNEVVFFLQ TPENSRMGDG HTLPIFVLQK 

       610        620        630        640        650        660 
ANVEENTKSS ALALIYNLMH HEQMANVLDR DDVLVKMLQN VQMQSQTHPE LASLANNILK 

       670        680        690        700        710        720 
MMYEKREKTR NTLPRYNSYL ESQFGHMSMT TPRSEALNSS GEVCEGAGEQ WSTPLTDDTM 

       730        740        750        760        770        780 
MDSYCNSSGR DSSKPYNSPM YHSPPAMYPE YSIGPPETYL DPHATASCYP RPTPPQYNSY 

       790        800        810 
DRSPPVYNDL PSNPGPSSHS SDYYPSRNSR F 

« Hide

References

« Hide 'large scale' references
[1]"The beta-catenin homolog BAR-1 and LET-60 Ras coordinately regulate the Hox gene lin-39 during Caenorhabditis elegans vulval development."
Eisenmann D.M., Maloof J.N., Simske J.S., Kenyon C., Kim S.K.
Development 125:3667-3680(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Bristol N2.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"A Wnt signaling pathway controls hox gene expression and neuroblast migration in C. elegans."
Maloof J.N., Whangbo J., Harris J.M., Jongeward G.D., Kenyon C.
Development 126:37-49(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LEU-482 AND GLY-524.
[4]"Protruding vulva mutants identify novel loci and Wnt signaling factors that function during Caenorhabditis elegans vulva development."
Eisenmann D.M., Kim S.K.
Genetics 156:1097-1116(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[5]"Distinct beta-catenins mediate adhesion and signalling functions in C. elegans."
Korswagen H.C., Herman M.A., Clevers H.C.
Nature 406:527-532(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH POP-1.
[6]"The divergent Caenorhabditis elegans beta-catenin proteins BAR-1, WRM-1 and HMP-2 make distinct protein interactions but retain functional redundancy in vivo."
Natarajan L., Witwer N.E., Eisenmann D.M.
Genetics 159:159-172(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH APR-1 AND POP-1.
[7]"The axin-like protein PRY-1 is a negative regulator of a canonical Wnt pathway in C. elegans."
Korswagen H.C., Coudreuse D.Y.M., Betist M.C., van de Water S., Zivkovic D., Clevers H.C.
Genes Dev. 16:1291-1302(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRY-1.
[8]"A component of the transcriptional mediator complex inhibits RAS-dependent vulval fate specification in C. elegans."
Moghal N., Sternberg P.W.
Development 130:57-69(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Identification of evolutionarily conserved promoter elements and amino acids required for function of the C. elegans beta-catenin homolog BAR-1."
Natarajan L., Jackson B.M., Szyleyko E., Eisenmann D.M.
Dev. Biol. 272:536-557(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, MUTAGENESIS OF SER-239; VAL-278; ASP-281; SER-369; GLU-449; ARG-460; LEU-482; THR-498 AND GLY-524.
[10]"LIN-23-mediated degradation of beta-catenin regulates the abundance of GLR-1 glutamate receptors in the ventral nerve cord of C. elegans."
Dreier L., Burbea M., Kaplan J.M.
Neuron 46:51-64(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LIN-23.
[11]"Functional interaction between beta-catenin and FOXO in oxidative stress signaling."
Essers M.A.G., de Vries-Smits L.M.M., Barker N., Polderman P.E., Burgering B.M.T., Korswagen H.C.
Science 308:1181-1184(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DAF-16.
[12]"Two functionally distinct axin-like proteins regulate canonical Wnt signaling in C. elegans."
Oosterveen T., Coudreuse D.Y.M., Yang P.-T., Fraser E., Bergsma J., Dale T.C., Korswagen H.C.
Dev. Biol. 308:438-448(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXL-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF063646 mRNA. Translation: AAC17424.1.
FO080795 Genomic DNA. Translation: CCD66852.1.
PIRT43175.
RefSeqNP_509206.1. NM_076805.5.
UniGeneCel.5480.

3D structure databases

ProteinModelPortalQ18825.
SMRQ18825. Positions 109-678.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid45907. 183 interactions.
IntActQ18825. 4 interactions.
MINTMINT-214589.
STRING6239.C54D1.6.2.

Proteomic databases

PaxDbQ18825.
PRIDEQ18825.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC54D1.6; C54D1.6; WBGene00000238.
GeneID180982.
KEGGcel:CELE_C54D1.6.
UCSCC54D1.6.1. c. elegans.

Organism-specific databases

CTD180982.
WormBaseC54D1.6; CE08973; WBGene00000238; bar-1.

Phylogenomic databases

eggNOGNOG249506.
GeneTreeENSGT00730000110821.
HOGENOMHOG000095175.
InParanoidQ18825.
KOK02105.
OMANIAKMEC.
OrthoDBEOG7X0VMV.
PhylomeDBQ18825.

Enzyme and pathway databases

SignaLinkQ18825.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PRINTSPR01869. BCATNINFAMLY.
SMARTSM00185. ARM. 3 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

NextBio911834.

Entry information

Entry nameBAR1_CAEEL
AccessionPrimary (citable) accession number: Q18825
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: June 1, 1998
Last modified: June 11, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase