WRM1_CAEEL
ID WRM1_CAEEL Reviewed; 796 AA.
AC Q10953; O16145;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Armadillo repeat-containing protein wrm-1;
DE AltName: Full=Worm armadillo protein 1;
GN Name=wrm-1 {ECO:0000312|WormBase:B0336.1a};
GN ORFNames=B0336.1 {ECO:0000312|WormBase:B0336.1a};
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:AAC47748.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC47748.1};
RX PubMed=9288750; DOI=10.1016/s0092-8674(00)80531-0;
RA Rocheleau C.E., Downs W.D., Lin R., Wittmann C., Bei Y., Cha Y.-H., Ali M.,
RA Priess J.R., Mello C.C.;
RT "Wnt signaling and an APC-related gene specify endoderm in early C. elegans
RT embryos.";
RL Cell 90:707-716(1997).
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, IDENTIFICATION IN THE BETA-CATENIN-LIT-1 COMPLEX, AND INTERACTION
RP WITH LIT-1 AND POP-1.
RX PubMed=10380924; DOI=10.1016/s0092-8674(00)80784-9;
RA Rocheleau C.E., Yasuda J., Shin T.H., Lin R., Sawa H., Okano H.,
RA Priess J.R., Davis R.J., Mello C.C.;
RT "WRM-1 activates the LIT-1 protein kinase to transduce anterior/posterior
RT polarity signals in C. elegans.";
RL Cell 97:717-726(1999).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH LIT-1.
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 [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=11807036; DOI=10.1242/dev.129.2.443;
RA Siegfried K.R., Kimble J.;
RT "POP-1 controls axis formation during early gonadogenesis in C. elegans.";
RL Development 129:443-453(2002).
RN [6] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE BETA-CATENIN-LIT-1 COMPLEX, AND INTERACTION
RP WITH LIT-1.
RX PubMed=15066285; DOI=10.1016/s0092-8674(04)00203-x;
RA Lo M.-C., Gay F., Odom R., Shi Y., Lin R.;
RT "Phosphorylation by the beta-catenin/MAPK complex promotes 14-3-3-mediated
RT nuclear export of TCF/POP-1 in signal-responsive cells in C. elegans.";
RL Cell 117:95-106(2004).
RN [7] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15572126; DOI=10.1016/j.devcel.2004.10.008;
RA Walston T., Tuskey C., Edgar L., Hawkins N., Ellis G., Bowerman B.,
RA Wood W., Hardin J.;
RT "Multiple Wnt signaling pathways converge to orient the mitotic spindle in
RT early C. elegans embryos.";
RL Dev. Cell 7:831-841(2004).
RN [8] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16077003; DOI=10.1101/gad.1322805;
RA Takeshita H., Sawa H.;
RT "Asymmetric cortical and nuclear localizations of WRM-1/beta-catenin during
RT asymmetric cell division in C. elegans.";
RL Genes Dev. 19:1743-1748(2005).
RN [9] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH NHR-25.
RX PubMed=16890160; DOI=10.1016/j.devcel.2006.06.003;
RA Asahina M., Valenta T., Silhankova M., Korinek V., Jindra M.;
RT "Crosstalk between a nuclear receptor and beta-catenin signaling decides
RT cell fates in the C. elegans somatic gonad.";
RL Dev. Cell 11:203-211(2006).
RN [10] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17276345; DOI=10.1016/j.devcel.2007.01.004;
RA Mizumoto K., Sawa H.;
RT "Cortical beta-catenin and APC regulate asymmetric nuclear beta-catenin
RT localization during asymmetric cell division in C. elegans.";
RL Dev. Cell 12:287-299(2007).
RN [11]
RP FUNCTION.
RX PubMed=17476329; DOI=10.1371/journal.pone.0000407;
RA Fujita M., Takeshita H., Sawa H.;
RT "Cyclin E and CDK2 repress the terminal differentiation of quiescent cells
RT after asymmetric division in C. elegans.";
RL PLoS ONE 2:E407-E407(2007).
RN [12]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=25569233; DOI=10.1371/journal.pgen.1004921;
RA Uehara T., Kage-Nakadai E., Yoshina S., Imae R., Mitani S.;
RT "The tumor suppressor BCL7B functions in the Wnt signaling pathway.";
RL PLoS Genet. 11:E1004921-E1004921(2015).
CC -!- FUNCTION: Antagonistic role in the Wnt signaling pathway that operates
CC in embryogenesis. When located at the cortex it has been shown to
CC inhibit Wnt signaling during asymmetric cell division but when
CC relocated to the nucleus it shows positive regulation. Has a role in
CC blastomere signaling during endoderm specification. Component of the
CC beta-catenin-lit-1 complex which promotes phosphorylation, down-
CC regulation and subcellular relocation of pop-1 (PubMed:10380924).
CC Within the complex, activates lit-1-dependent kinase activity
CC (PubMed:10380924). Can substitute for bar-1 indicating functional
CC redundancy. Appears to have a role in centrosome positioning and can
CC activation transcription in yeast. Involved in the development of
CC distal tip cells (DTC) by regulating the asymmetric distribution of
CC cye-1 and cki-1 between the daughters of Z1.a and Z4.p cells
CC (PubMed:17476329). {ECO:0000269|PubMed:10380924,
CC ECO:0000269|PubMed:11560894, ECO:0000269|PubMed:11807036,
CC ECO:0000269|PubMed:15066285, ECO:0000269|PubMed:15572126,
CC ECO:0000269|PubMed:16077003, ECO:0000269|PubMed:16890160,
CC ECO:0000269|PubMed:17276345, ECO:0000269|PubMed:17476329,
CC ECO:0000269|PubMed:9288750}.
CC -!- SUBUNIT: Interacts (independently of ARM repeat) with nhr-25
CC (PubMed:16890160). Component of the beta-catenin-lit-1 complex (also
CC called the lit-1/wrm-1 complex or the wrm-1/lit-1 kinase complex) at
CC least composed of lit-1 and wrm-1 (PubMed:10380924, PubMed:15066285).
CC Interacts (via N-terminus) with lit-1; the interaction is direct and
CC activates lit-1 kinase activity which leads to the phosphorylation of
CC pop-1 (PubMed:10380924, PubMed:11560894, PubMed:15066285). This
CC promotes pop-1 interaction with par-5 and translocation of pop-1 from
CC the nucleus to the cytoplasm (PubMed:15066285).
CC {ECO:0000269|PubMed:10380924, ECO:0000269|PubMed:11560894,
CC ECO:0000269|PubMed:15066285, ECO:0000269|PubMed:16890160}.
CC -!- INTERACTION:
CC Q10953; Q9U9Y8: lit-1; NbExp=8; IntAct=EBI-2530558, EBI-318513;
CC Q10953; Q19345: nhr-25; NbExp=3; IntAct=EBI-2530558, EBI-3871243;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:16077003, ECO:0000269|PubMed:17276345,
CC ECO:0000269|PubMed:25569233}. Nucleus {ECO:0000269|PubMed:16077003,
CC ECO:0000269|PubMed:17276345}. Note=Located in the anterior cell cortex
CC before and during asymmetric cell division. After division, located
CC preferentially in the nucleus of the posterior daughter cell.
CC {ECO:0000269|PubMed:16077003, ECO:0000269|PubMed:17276345,
CC ECO:0000269|PubMed:25569233}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing cells of the embryo
CC including hypodermal cells, neuroblasts, and mesodermal cells
CC (PubMed:15572126). Expressed in seam cells in hermaphrodites at the L2
CC stage of larval development (PubMed:25569233).
CC {ECO:0000269|PubMed:25569233}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit premature cell cleavage during
CC embryogenesis, symmetrical cell division during gonadogenesis and
CC undifferentiated intestines. Embryos show a defect in centrosome
CC positioning that delays ABar spindle alignment and appear to lack
CC endoderm. {ECO:0000269|PubMed:9288750}.
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DR EMBL; AF013951; AAC47748.1; -; mRNA.
DR EMBL; BX284603; CCD61515.1; -; Genomic_DNA.
DR PIR; T03746; T03746.
DR RefSeq; NP_498236.1; NM_065835.6.
DR AlphaFoldDB; Q10953; -.
DR BioGRID; 41028; 23.
DR ComplexPortal; CPX-1130; Beta-catenin-lit-1 complex.
DR IntAct; Q10953; 22.
DR MINT; Q10953; -.
DR STRING; 6239.B0336.1; -.
DR EPD; Q10953; -.
DR PaxDb; Q10953; -.
DR PeptideAtlas; Q10953; -.
DR EnsemblMetazoa; B0336.1a.1; B0336.1a.1; WBGene00006943.
DR GeneID; 175802; -.
DR KEGG; cel:CELE_B0336.1; -.
DR UCSC; B0336.1; c. elegans.
DR CTD; 175802; -.
DR WormBase; B0336.1a; CE26743; WBGene00006943; wrm-1.
DR eggNOG; ENOG502T285; Eukaryota.
DR HOGENOM; CLU_352050_0_0_1; -.
DR InParanoid; Q10953; -.
DR OMA; QILVHII; -.
DR OrthoDB; 642513at2759; -.
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; Q10953; -.
DR PRO; PR:Q10953; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006943; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q10953; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IDA:WormBase.
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:0016922; F:nuclear receptor binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:WormBase.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:WormBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:WormBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0007492; P:endoderm development; IMP:UniProtKB.
DR GO; GO:0001714; P:endodermal cell fate specification; IMP:WormBase.
DR GO; GO:0061031; P:endodermal digestive tract morphogenesis; IMP:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; IMP:UniProtKB.
DR GO; GO:0051782; P:negative regulation of cell division; IGI:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0043282; P:pharyngeal muscle development; IMP:UniProtKB.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:ComplexPortal.
DR GO; GO:0010085; P:polarity specification of proximal/distal axis; IMP:WormBase.
DR GO; GO:1904787; P:positive regulation of asymmetric protein localization involved in cell fate determination; IMP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:UniProtKB.
DR GO; GO:1903226; P:positive regulation of endodermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:WormBase.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:WormBase.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:WormBase.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:1903224; P:regulation of endodermal cell differentiation; IGI:UniProtKB.
DR GO; GO:0042661; P:regulation of mesodermal cell fate specification; IGI:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IDA:WormBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:WormBase.
DR GO; GO:0044332; P:Wnt signaling pathway involved in dorsal/ventral axis specification; IMP:UniProtKB.
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.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Developmental protein; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..796
FT /note="Armadillo repeat-containing protein wrm-1"
FT /id="PRO_0000342701"
FT REPEAT 462..504
FT /note="ARM"
FT /evidence="ECO:0000255"
FT REGION 17..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 90349 MW; B517C7A804A7DEA8 CRC64;
MDVDCAETFS QPCTPLNFNP MTPSTSRVST PVRPSSTMSA RQYSGSPFKA QPQNMEPSNS
RVQELREAAV GKRSYTNAWM QGTYAPPQMA GQQQRFSRPP SVIGSTMSHM TNMSEMTAYS
YGGLSMLSVN TEMGEFNNFV NQAPYQRALT RVSQVSENQD PTNRQYPMTA PEIIENLEST
ELINQAAAIR ALEPIVKAGG MLQTWGPKGA EPIIRALFQV LIPRPVENEN VIRKAFEILH
HSILLSNKEI RRIDRMFFRL NAALMDPNGP PVFNVPKPYS IYEIVMTRAI QLDTKFESSA
MVLLVHLCCK PHFMKIFFGE DETQQSPAHR RLHKIVIEFA IGNLRRPETK SKNKGLCVSI
IKNLSNKNAT IKDMSERLGV VSLFHQIMQN EVIHEDLLWS TMQALTVFCG DVKNGTHFVQ
MGGAQVLCGL LSHGSTRLLH ELLKCLRRVS DLPAIQEQDM KESIHCIVQL IGCSDVTIVE
LATGTLRNIG LHNKMNKAFM VQDGVTSHAI AVLRTSEQFT YQPHANIDLY RKQILSIYEN
CLSVLNNVTS MAPQDIKESA VSACRMISEN ADSAYVLLHY FNVGNRKCRK LAVTVMKRVI
ETVPAFADPF VDLLGTTNEP LPILLLQRAF QSLDEWRKTS VEMMNCDGRS AEQRRELDDR
RKDHEDIVKR SVGLLTNLCS QANPRFFHSL KLVLTNGTLN PFQWLTHEMS DGILQEWLAF
ILSICSRDES LQTFMMYRFL EQAKMTEAFF AELKARRQNS NIQTMLSKII DLGRHQQRIV
SQQHQQHQMQ HHRQLM
