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 27-MAR-2024, entry version 169. 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}, spy-1 GN {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.C54D1.6.1; -. DR PaxDb; 6239-C54D1-6; -. 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 AGR; WB:WBGene00000238; -. 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; 2877677at2759; -. DR PhylomeDB; Q18825; -. DR Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-CEL-6798695; Neutrophil degranulation. DR Reactome; R-CEL-8980692; RHOA GTPase cycle. DR Reactome; R-CEL-9013406; RHOQ 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 cell types or 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; IMP:UniProtKB. 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:0040002; P:collagen and cuticulin-based cuticle development; IMP:UniProtKB. 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:0018991; P:egg-laying behavior; IMP:WormBase. DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:UniProtKB. 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: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 GO; GO:0040025; P:vulval development; IMP:WormBase. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR013284; Beta-catenin. DR PANTHER; PTHR45976; ARMADILLO SEGMENT POLARITY PROTEIN; 1. DR PANTHER; PTHR45976:SF5; BETA-CATENIN_ARMADILLO-RELATED PROTEIN 1; 1. DR PRINTS; PR01869; BCATNINFAMLY. DR SMART; SM00185; ARM; 3. DR SUPFAM; SSF48371; ARM repeat; 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 //