BAR1_CAEEL
ID BAR1_CAEEL Reviewed; 811 AA.
AC Q18825;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Beta-catenin/armadillo-related protein 1;
DE AltName: Full=Protruding vulva protein 1;
DE AltName: Full=Suppressor of polyray 1;
GN Name=bar-1 {ECO:0000312|WormBase:C54D1.6};
GN Synonyms=pvl-1 {ECO:0000312|WormBase:C54D1.6},
GN spy-1 {ECO:0000312|WormBase:C54D1.6};
GN ORFNames=C54D1.6 {ECO:0000312|WormBase:C54D1.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC17424.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 97-GLU--PHE-811.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC17424.1};
RX PubMed=9716532; DOI=10.1242/dev.125.18.3667;
RA Eisenmann D.M., Maloof J.N., Simske J.S., Kenyon C., Kim S.K.;
RT "The beta-catenin homolog BAR-1 and LET-60 Ras coordinately regulate the
RT Hox gene lin-39 during Caenorhabditis elegans vulval development.";
RL Development 125:3667-3680(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF LEU-482 AND GLY-524.
RX PubMed=9834184; DOI=10.1242/dev.126.1.37;
RA Maloof J.N., Whangbo J., Harris J.M., Jongeward G.D., Kenyon C.;
RT "A Wnt signaling pathway controls hox gene expression and neuroblast
RT migration in C. elegans.";
RL Development 126:37-49(1999).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 97-GLU--PHE-811.
RX PubMed=11063687; DOI=10.1093/genetics/156.3.1097;
RA Eisenmann D.M., Kim S.K.;
RT "Protruding vulva mutants identify novel loci and Wnt signaling factors
RT that function during Caenorhabditis elegans vulva development.";
RL Genetics 156:1097-1116(2000).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH POP-1.
RX PubMed=10952315; DOI=10.1038/35020099;
RA Korswagen H.C., Herman M.A., Clevers H.C.;
RT "Distinct beta-catenins mediate adhesion and signalling functions in C.
RT elegans.";
RL Nature 406:527-532(2000).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH APR-1 AND POP-1, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 97-GLU--PHE-811.
RX PubMed=11560894; DOI=10.1093/genetics/159.1.159;
RA Natarajan L., Witwer N.E., Eisenmann D.M.;
RT "The divergent Caenorhabditis elegans beta-catenin proteins BAR-1, WRM-1
RT and HMP-2 make distinct protein interactions but retain functional
RT redundancy in vivo.";
RL Genetics 159:159-172(2001).
RN [7] {ECO:0000305}
RP INTERACTION WITH PRY-1.
RX PubMed=12023307; DOI=10.1101/gad.981802;
RA Korswagen H.C., Coudreuse D.Y.M., Betist M.C., van de Water S.,
RA Zivkovic D., Clevers H.C.;
RT "The axin-like protein PRY-1 is a negative regulator of a canonical Wnt
RT pathway in C. elegans.";
RL Genes Dev. 16:1291-1302(2002).
RN [8] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 97-GLU--PHE-811 AND
RP GLY-524.
RX PubMed=12441291; DOI=10.1242/dev.00189;
RA Moghal N., Sternberg P.W.;
RT "A component of the transcriptional mediator complex inhibits RAS-dependent
RT vulval fate specification in C. elegans.";
RL Development 130:57-69(2003).
RN [9] {ECO:0000305}
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF SER-239; VAL-278; ASP-281; SER-369;
RP GLU-449; ARG-460; LEU-482; THR-498 AND GLY-524.
RX PubMed=15282167; DOI=10.1016/j.ydbio.2004.05.027;
RA Natarajan L., Jackson B.M., Szyleyko E., Eisenmann D.M.;
RT "Identification of evolutionarily conserved promoter elements and amino
RT acids required for function of the C. elegans beta-catenin homolog BAR-1.";
RL Dev. Biol. 272:536-557(2004).
RN [10] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LIN-23.
RX PubMed=15820693; DOI=10.1016/j.neuron.2004.12.058;
RA Dreier L., Burbea M., Kaplan J.M.;
RT "LIN-23-mediated degradation of beta-catenin regulates the abundance of
RT GLR-1 glutamate receptors in the ventral nerve cord of C. elegans.";
RL Neuron 46:51-64(2005).
RN [11] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DAF-16, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 97-GLU--PHE-811.
RX PubMed=15905404; DOI=10.1126/science.1109083;
RA Essers M.A.G., de Vries-Smits L.M.M., Barker N., Polderman P.E.,
RA Burgering B.M.T., Korswagen H.C.;
RT "Functional interaction between beta-catenin and FOXO in oxidative stress
RT signaling.";
RL Science 308:1181-1184(2005).
RN [12] {ECO:0000305}
RP INTERACTION WITH AXL-1.
RX PubMed=17601533; DOI=10.1016/j.ydbio.2007.05.043;
RA Oosterveen T., Coudreuse D.Y.M., Yang P.-T., Fraser E., Bergsma J.,
RA Dale T.C., Korswagen H.C.;
RT "Two functionally distinct axin-like proteins regulate canonical Wnt
RT signaling in C. elegans.";
RL Dev. Biol. 308:438-448(2007).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=35263319; DOI=10.1371/journal.pbio.3001581;
RA Sang Y., Ren J., Aballay A.;
RT "The transcription factor HLH-26 controls probiotic-mediated protection
RT against intestinal infection through up-regulation of the Wnt/BAR-1
RT pathway.";
RL PLoS Biol. 20:e3001581-e3001581(2022).
CC -!- FUNCTION: Participates in the Wnt signaling pathway which affects cell
CC fate and may regulate the stem cell divisions of seam cells during
CC larval development (PubMed:10952315). Functions as a transcriptional
CC activator but is dependent on the interaction with pop-1
CC (PubMed:10952315). Involved in maintaining lin-39 Hox expression and
CC regulating glr-1 abundance at the synapses (PubMed:15820693). Required
CC for mab-5 expression during Q neuroblast migration and for oxidative
CC stress-induced daf-16 signaling (PubMed:9834184, PubMed:15905404). Has
CC roles in egg laying, vulva precursor cell fate determination, Q
CC neuroblast migration, posterior ectodermal cell P12 specification,
CC movement, body length, male tail development and dauer induction
CC (PubMed:9716532, PubMed:9834184, PubMed:11063687, PubMed:11560894,
CC PubMed:12441291, PubMed:15905404). Functionally redundant to wrm-1 and
CC hmp-2 (PubMed:11560894). In the intestine, plays a role in probiotic-
CC mediated protection against infections by pathogens such as S.enterica
CC (PubMed:35263319). {ECO:0000269|PubMed:10952315,
CC ECO:0000269|PubMed:11063687, ECO:0000269|PubMed:11560894,
CC ECO:0000269|PubMed:12441291, ECO:0000269|PubMed:15820693,
CC ECO:0000269|PubMed:15905404, ECO:0000269|PubMed:35263319,
CC ECO:0000269|PubMed:9716532, ECO:0000269|PubMed:9834184}.
CC -!- SUBUNIT: Interacts with apr-1 (PubMed:11560894). Interacts with axl-1
CC (PubMed:17601533). Interacts with daf-16 (PubMed:15905404). Interacts
CC with lin-23 (PubMed:15820693). and. Interacts with pop-1 (via acidic
CC region in N-terminus 1-44) (PubMed:10952315, PubMed:11560894).
CC Interacts (via ARM repeats) with pry-1 (PubMed:12023307).
CC {ECO:0000269|PubMed:10952315, ECO:0000269|PubMed:11560894,
CC ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:15820693,
CC ECO:0000269|PubMed:15905404, ECO:0000269|PubMed:17601533}.
CC -!- INTERACTION:
CC Q18825; Q10666: pop-1; NbExp=6; IntAct=EBI-2528850, EBI-317870;
CC Q18825; O62090: pry-1; NbExp=3; IntAct=EBI-2528850, EBI-2917690;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15820693,
CC ECO:0000269|PubMed:9716532}. Nucleus {ECO:0000269|PubMed:15820693,
CC ECO:0000269|PubMed:9716532}. Membrane {ECO:0000269|PubMed:15820693,
CC ECO:0000269|PubMed:9716532}. Cell junction
CC {ECO:0000269|PubMed:15820693, ECO:0000269|PubMed:9716532}. Note=Mostly
CC cytoplasmic. {ECO:0000269|PubMed:15820693, ECO:0000269|PubMed:9716532}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscle cells, hypodermal
CC seam cells, gonad sheath cells and vulval precursor cells.
CC {ECO:0000269|PubMed:11063687, ECO:0000269|PubMed:9716532}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout development from L1 to L4 and
CC during adulthood (PubMed:15282167). Expressed in P3.p to P8.p vulval
CC precursor cells in the late L1 and early L2 larval stage
CC (PubMed:9716532). Not expressed in vulval precursor cells P1.p, P2.p,
CC P9.p, P10.p or P11.p in the mid-L3 larval stage (PubMed:9716532).
CC Expressed in other postembryonic cells including seam cells
CC (PubMed:9716532). {ECO:0000269|PubMed:15282167,
CC ECO:0000269|PubMed:9716532}.
CC -!- DISRUPTION PHENOTYPE: Abnormalities in vulval development due to
CC incorrect cell fate specification, resulting in the following
CC phenotypes, multivulva (Muv), protruding vulva (Pvl) and egg laying
CC defective (Egl) (PubMed:9716532, PubMed:11063687, PubMed:11560894,
CC PubMed:12441291). Mutants also show defects in Q neuroblast migration,
CC uncoordinated movement (Unc) and reduced superoxidase dismutase levels
CC (PubMed:15905404). Mutants can be rescued by wrm-1 and hmp-2 when
CC expressed from the bar-1 promoter (PubMed:11560894). Double knockout
CC with dpy-22 result in reduced body length, male tail morphology
CC abnormalities (Mab) and dauer induction (PubMed:12441291). RNAi-
CC mediated knockdown in the intestine decreases E.faecium-mediated
CC protection against S.enterica infection (PubMed:35263319).
CC {ECO:0000269|PubMed:11063687, ECO:0000269|PubMed:11560894,
CC ECO:0000269|PubMed:12441291, ECO:0000269|PubMed:15905404,
CC ECO:0000269|PubMed:35263319, ECO:0000269|PubMed:9716532}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000255}.
CC -!- CAUTION: Alleles mu63 and mu349 were originally reported
CC (PubMed:9834184) as the mutations L130F and Q147STOP respectively. This
CC is in conflict with WormBase and more recent literature
CC (PubMed:15282167) which is represented in this entry. {ECO:0000305,
CC ECO:0000305|PubMed:15282167, ECO:0000305|PubMed:9834184}.
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DR EMBL; AF063646; AAC17424.1; -; mRNA.
DR EMBL; BX284606; CCD66852.1; -; Genomic_DNA.
DR PIR; T43175; T43175.
DR RefSeq; NP_509206.1; NM_076805.5.
DR AlphaFoldDB; Q18825; -.
DR SMR; Q18825; -.
DR BioGRID; 45907; 203.
DR IntAct; Q18825; 20.
DR STRING; 6239.C54D1.6; -.
DR PaxDb; Q18825; -.
DR EnsemblMetazoa; C54D1.6.1; C54D1.6.1; WBGene00000238.
DR GeneID; 180982; -.
DR KEGG; cel:CELE_C54D1.6; -.
DR UCSC; C54D1.6.1; c. elegans.
DR CTD; 180982; -.
DR WormBase; C54D1.6; CE08973; WBGene00000238; bar-1.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_347902_0_0_1; -.
DR InParanoid; Q18825; -.
DR OMA; EAQQMED; -.
DR OrthoDB; 303939at2759; -.
DR PhylomeDB; Q18825; -.
DR Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6809371; Formation of the cornified envelope.
DR Reactome; R-CEL-8980692; RHOA GTPase cycle.
DR Reactome; R-CEL-9013026; RHOB GTPase cycle.
DR Reactome; R-CEL-9013106; RHOC GTPase cycle.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR SignaLink; Q18825; -.
DR PRO; PR:Q18825; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000238; Expressed in material anatomical entity and 5 other tissues.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:WormBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:WormBase.
DR GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
DR GO; GO:0001708; P:cell fate specification; IMP:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:ParkinsonsUK-UCL.
DR GO; GO:0040024; P:dauer larval development; IGI:ParkinsonsUK-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:ParkinsonsUK-UCL.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:UniProtKB.
DR GO; GO:0040035; P:hermaphrodite genitalia development; IMP:WormBase.
DR GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
DR GO; GO:0007617; P:mating behavior; IMP:WormBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:WormBase.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IGI:WormBase.
DR GO; GO:0043058; P:regulation of backward locomotion; IMP:WormBase.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0040028; P:regulation of vulval development; IMP:WormBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR013284; Beta-catenin.
DR PANTHER; PTHR45976; PTHR45976; 1.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Activator; Cell junction; Cytoplasm; Developmental protein; Membrane;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..811
FT /note="Beta-catenin/armadillo-related protein 1"
FT /id="PRO_0000372805"
FT REPEAT 108..147
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 331..369
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 370..408
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REGION 1..85
FT /note="Involved in transcriptional activation"
FT /evidence="ECO:0000269|PubMed:11560894"
FT REGION 541..811
FT /note="Involved in transcriptional activation"
FT /evidence="ECO:0000269|PubMed:11560894"
FT REGION 763..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 97..811
FT /note="Missing: In ga80; reduces survival. Abnormal Pn.p
FT cell fate specification leading to defective vulval
FT induction and a protruding vulval phenotype. Reduces sod-3
FT expression."
FT /evidence="ECO:0000269|PubMed:11063687,
FT ECO:0000269|PubMed:11560894, ECO:0000269|PubMed:12441291,
FT ECO:0000269|PubMed:15905404, ECO:0000269|PubMed:9716532"
FT MUTAGEN 239
FT /note="S->L: In ep451; interferes with neuroblast Q
FT migration."
FT /evidence="ECO:0000269|PubMed:15282167"
FT MUTAGEN 278
FT /note="V->G: In ep484; interferes with neuroblast Q
FT migration; in association with Asn-281."
FT /evidence="ECO:0000269|PubMed:15282167"
FT MUTAGEN 281
FT /note="D->N: In ep484; interferes with neuroblast Q
FT migration; in association with Gly-278."
FT /evidence="ECO:0000269|PubMed:15282167"
FT MUTAGEN 369
FT /note="S->K: In ep466; interferes with neuroblast Q
FT migration."
FT /evidence="ECO:0000269|PubMed:15282167"
FT MUTAGEN 449
FT /note="E->K: In ep487/ep478; variable interference with
FT neuroblast Q migration."
FT /evidence="ECO:0000269|PubMed:15282167"
FT MUTAGEN 460
FT /note="R->W: In ep461; interferes with neuroblast Q
FT migration."
FT /evidence="ECO:0000269|PubMed:15282167"
FT MUTAGEN 482
FT /note="L->I: In mu349; suppresses ectopic expression of
FT mab-5 and interferes with neuroblast Q migration."
FT /evidence="ECO:0000269|PubMed:15282167,
FT ECO:0000269|PubMed:9834184"
FT MUTAGEN 498
FT /note="T->I: In ep485; interferes with neuroblast Q
FT migration."
FT /evidence="ECO:0000269|PubMed:15282167"
FT MUTAGEN 524
FT /note="G->D: In ep460 and mu63; suppresses ectopic
FT expression of mab-5."
FT /evidence="ECO:0000269|PubMed:12441291,
FT ECO:0000269|PubMed:15282167, ECO:0000269|PubMed:9834184"
FT MUTAGEN 524
FT /note="G->S: In ep486; interferes with neuroblast Q
FT migration."
FT /evidence="ECO:0000269|PubMed:15282167,
FT ECO:0000269|PubMed:9834184"
SQ SEQUENCE 811 AA; 92228 MW; 97D6FFDE71BDFDFF CRC64;
MDLDPNLVIN HDDTNLSEAS FTMEQHTSSY SDIHMGSTPC TGHRKVDMWR NHNFDSGFQT
MNHSEAPSII SSLHPSSHLS GMSSMADYEP IPTLSDQQKQ KFDGITQNQA DGQYNTVRAI
PELTMLMKDQ DNEVVHKAVI LMQNIAKMEC DPMRRQNEAR IVDPRVIFTL RDLLRDKVEF
PNIIRCTLGT FFHICNRQEG IDLVTRAIAE QPDIIPNLIR HIGTYPSSIY KYAILTMHSI
LSDKQRGGQS VIIARQQDAI THVTPWLEAE KSEKLLPVIV DLIRVLCEKN TEQKIKFVKM
GGPQKLLMLL QHRVYENLLW RTTQLLKTFS NFDAPNLVAF GGRQILANLL SHGSPRLVQS
TLETLRNISD VPSKIKEDLL LKSLLELVNS RNTTIRLYSA QIMSNLVANN RHNKEFMCGN
NGVVILVRAL TIATKEMGDL RDKEAQQMED YIESLICTLR HLCVGHPMSD KVQAFVFRDP
ALFLHKLLTM RPVLLKHTLS LLLKVVSQHA LLAPFRSCRI GDKGFVEQLI HILRVACTQL
NVQESIEGVR VKDIIHLCIQ ILRWITRDQD ILNEVVFFLQ TPENSRMGDG HTLPIFVLQK
ANVEENTKSS ALALIYNLMH HEQMANVLDR DDVLVKMLQN VQMQSQTHPE LASLANNILK
MMYEKREKTR NTLPRYNSYL ESQFGHMSMT TPRSEALNSS GEVCEGAGEQ WSTPLTDDTM
MDSYCNSSGR DSSKPYNSPM YHSPPAMYPE YSIGPPETYL DPHATASCYP RPTPPQYNSY
DRSPPVYNDL PSNPGPSSHS SDYYPSRNSR F
