BAR1_CAEBR
ID BAR1_CAEBR Reviewed; 808 AA.
AC A8XBZ8;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 82.
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; Synonyms=pvl-1, spy-1; ORFNames=CBG10985;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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. Functions as a transcriptional activator but is
CC dependent on the interaction with pop-1. Involved in maintaining lin-39
CC Hox expression and regulating glr-1 abundance at the synapses. Required
CC for mab-5 expression during Q neuroblast migration and for oxidative
CC stress-induced daf-16 signaling. Has roles in egg laying, vulva
CC precursor cell fate determination, Q neuroblast migration, posterior
CC ectodermal cell P12 specification, movement, body length, male tail
CC development and dauer induction. Functionally redundant to wrm-1 and
CC hmp-2 (By similarity). {ECO:0000250|UniProtKB:Q18825}.
CC -!- SUBUNIT: Interacts with apr-1, axl-1, daf-16, lin-23, and pop-1 (via
CC acidic region in N-terminus 1-44). Interacts (via ARM repeats) with
CC pry-1 (By similarity). {ECO:0000250|UniProtKB:Q18825}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q18825}. Nucleus
CC {ECO:0000250|UniProtKB:Q18825}. Membrane
CC {ECO:0000250|UniProtKB:Q18825}. Cell junction
CC {ECO:0000250|UniProtKB:Q18825}. Note=Mostly cytoplasmic.
CC {ECO:0000250|UniProtKB:Q18825}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000255}.
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DR EMBL; HE601482; CAP30237.3; -; Genomic_DNA.
DR RefSeq; XP_002645000.1; XM_002644954.1.
DR AlphaFoldDB; A8XBZ8; -.
DR SMR; A8XBZ8; -.
DR STRING; 6238.CBG10985; -.
DR PRIDE; A8XBZ8; -.
DR EnsemblMetazoa; CBG10985a.1; CBG10985a.1; WBGene00032205.
DR GeneID; 8586998; -.
DR KEGG; cbr:CBG_10985; -.
DR CTD; 8586998; -.
DR WormBase; CBG10985a; CBP02677; WBGene00032205; Cbr-bar-1.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_347902_0_0_1; -.
DR InParanoid; A8XBZ8; -.
DR OMA; EAQQMED; -.
DR OrthoDB; 303939at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS: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; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 SMART; SM00185; ARM; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 3: Inferred from homology;
KW Activator; Cell junction; Cytoplasm; Developmental protein; Membrane;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..808
FT /note="Beta-catenin/armadillo-related protein 1"
FT /id="PRO_0000372804"
FT REPEAT 118..160
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 165..209
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 369..408
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REGION 1..85
FT /note="Involved in transcriptional activation"
FT /evidence="ECO:0000250|UniProtKB:Q18825"
FT REGION 541..808
FT /note="Involved in transcriptional activation"
FT /evidence="ECO:0000250|UniProtKB:Q18825"
FT REGION 702..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..758
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 91664 MW; 2AE8684144372863 CRC64;
MDLDPNLVIN HDDTNLSEIS YTMEQDSSSY SLEMGGTPSS AGHRKVDMWQ NHNFDSGFQT
MNHSEAPSII SSLHPSSHLS GMSSMAEYEP IPNLSEQQKQ KFDGITKNPT DGQYNTVRAI
PELTMLMKDQ DNEVVQKAVM IMQNIAKMEC DAMRRQNETK IVDPCVIFTL RNLLRDKVDH
PNIIRFTLGT LFNICNRQEG IDLVTRAISE QPDIIPNLIR HIGTFANSIY KYAILTMHSI
LSDKQRGGQS VTIARQQDAI IHVTPWLEAE KSEKLLPVIV DLIRVLCEKN TDQKVKFVKM
GGPQKLLHIL QQRGYENLLW RSTQLLKTFS NFDAPCLVAF GGRQILAGML SHGSPRLVLS
TLETLRNISD VPSKMKEELL LKSLLELVNS RNAVIRLYSA QTMSNLVANN RPNKEYMCSN
NGVVNLCRAL AIATKDWQNF QDKEAQQMED YAESLICTLR HLCVGHPLAE KVQAYVFREP
SIFLHKLMTM RPVLLKHTLN LLLKVVSQNA LLAPFLLCRI GEIGFVEQLI HILRVACTQL
NVQDVIEGVR VKDIVHLCIQ ILRLITRNPD ILNEVDFFLR SPENSRMGDG HTLPIFVLQK
ANVEENTKSS TLELIYNLMH HEKMADHLER DEILCKMLHS VQMQAANHPE LANLAANILK
LMSEKRERNR IHYGRHGSFE SQFGHLSVAA QRTEVLNSHG ETYEGAGEQW SQPMSDDSMM
ESYCNSSGRD SSKTYNSPMY HSPPSMYPEY PNGPPSGPYY DPHAFTSTRP TPPHYANYDS
PPVYNNIPSN QGPSSHLSDQ YPYRQGRF
