WRM1_CAEBR
ID WRM1_CAEBR Reviewed; 799 AA.
AC A8X811;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Armadillo repeat-containing protein wrm-1;
DE AltName: Full=Worm armadillo protein 1;
GN Name=wrm-1 {ECO:0000312|WormBase:CBG09006};
GN ORFNames=CBG09006 {ECO:0000312|WormBase:CBG09006};
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: Antagonistic role in the Wnt signaling pathway that operates
CC in embryogenesis (By similarity). When located at the cortex it has
CC been shown to inhibit Wnt signaling during asymmetric cell division but
CC when relocated to the nucleus it shows positive regulation (By
CC similarity). Has a role in blastomere signaling during endoderm
CC specification (By similarity). Component of the beta-catenin-lit-1
CC complex which promotes phosphorylation, down-regulation and subcellular
CC relocation of pop-1 (By similarity). Within the complex, activates lit-
CC 1-dependent kinase activity (By similarity). Can substitute for bar-1
CC indicating functional redundancy (By similarity). Appears to have a
CC role in centrosome positioning (By similarity). Involved in the
CC development of distal tip cells (DTC) by regulating the asymmetric
CC distribution of cye-1 and cki-1 between the daughters of Z1.a and Z4.p
CC cells (By similarity). {ECO:0000250|UniProtKB:Q10953}.
CC -!- SUBUNIT: Interacts (independently of ARM repeat) with nhr-25 (By
CC similarity). Component of the beta-catenin-lit-1 complex (also called
CC the lit-1/wrm-1 complex or the wrm-1/lit-1 kinase complex) at least
CC composed of lit-1 and wrm-1 (By similarity). Interacts (via N-terminus)
CC with lit-1; the interaction is direct and activates lit-1 kinase
CC activity which leads to the phosphorylation of pop-1 (By similarity).
CC This promotes pop-1 interaction with par-5 and translocation of pop-1
CC from the nucleus to the cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:Q10953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q10953}. Nucleus {ECO:0000250|UniProtKB:Q10953}.
CC Note=Located in the anterior cell cortex before and during asymmetric
CC cell division. After division, located preferentially in the nucleus of
CC the posterior daughter cell (By similarity).
CC {ECO:0000250|UniProtKB:Q10953}.
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DR EMBL; HE601284; CAP28772.3; -; Genomic_DNA.
DR RefSeq; XP_002641153.1; XM_002641107.1.
DR AlphaFoldDB; A8X811; -.
DR STRING; 6238.CBG09006; -.
DR EnsemblMetazoa; CBG09006.1; CBG09006.1; WBGene00030681.
DR GeneID; 8583146; -.
DR KEGG; cbr:CBG_09006; -.
DR CTD; 8583146; -.
DR WormBase; CBG09006; CBP08154; WBGene00030681; Cbr-wrm-1.
DR eggNOG; ENOG502T285; Eukaryota.
DR HOGENOM; CLU_352050_0_0_1; -.
DR InParanoid; A8X811; -.
DR OMA; QILVHII; -.
DR OrthoDB; 642513at2759; -.
DR Proteomes; UP000008549; Chromosome III.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IEA:EnsemblMetazoa.
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:0016922; F:nuclear receptor binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:EnsemblMetazoa.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:EnsemblMetazoa.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IEA:EnsemblMetazoa.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:EnsemblMetazoa.
DR GO; GO:0010172; P:embryonic body morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0007492; P:endoderm development; ISS:UniProtKB.
DR GO; GO:0001714; P:endodermal cell fate specification; IEA:EnsemblMetazoa.
DR GO; GO:0061031; P:endodermal digestive tract morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:EnsemblMetazoa.
DR GO; GO:0070986; P:left/right axis specification; IEA:EnsemblMetazoa.
DR GO; GO:0051782; P:negative regulation of cell division; IEA:EnsemblMetazoa.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0043282; P:pharyngeal muscle development; IEA:EnsemblMetazoa.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IEA:EnsemblMetazoa.
DR GO; GO:0010085; P:polarity specification of proximal/distal axis; IEA:EnsemblMetazoa.
DR GO; GO:1904787; P:positive regulation of asymmetric protein localization involved in cell fate determination; IEA:EnsemblMetazoa.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:EnsemblMetazoa.
DR GO; GO:1903226; P:positive regulation of endodermal cell differentiation; IEA:EnsemblMetazoa.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:EnsemblMetazoa.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:EnsemblMetazoa.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0042661; P:regulation of mesodermal cell fate specification; IEA:EnsemblMetazoa.
DR GO; GO:0044332; P:Wnt signaling pathway involved in dorsal/ventral axis specification; IEA:EnsemblMetazoa.
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 SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; Developmental protein; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..799
FT /note="Armadillo repeat-containing protein wrm-1"
FT /id="PRO_0000342700"
FT REPEAT 454..496
FT /note="ARM"
FT /evidence="ECO:0000255"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 91587 MW; 3B5B2A543962923B CRC64;
MEERGPDIEK YGSQPCTPLS FDPMLPSTSR VATPVRPSST LSARQAPASP FRAQPQNMEP
SISRVHELRE GAAVKRSYTN DWMQGNYIPP NPQQQQYQRP PSMIGSTISN MSNLSHMTKF
SALSVNTQCG QFDNWIYQSQ PALSKVSHSS VENQDPMKRR ERMSIPEIVQ SLASYEMSDQ
VAAIRELEPL AKAEALESTY CQADLGKIIN ALFEVLVPRP QENENVIRKV FEILHRAAVP
KHVRMTEKIF HSLNLELMNT NSSKHSFQVP RPYSIYELVI ERASRLDTAY DQAAMLLLAQ
ICCKPFFMKY VFSEKEQSAG HRRLHEVVMQ FAIKNLQQQE TKRKSKGFCV SIIKNLSRRN
RSIWSIVYEL HVIPIFHDII KDEYSDEDLL WPTMQALTTF CSIERVGEDF VKLGGAQDLC
NLLYHGSTRL LHELLACMQR LSLLQEIGNQ DMEESIRRVI QVVGSDDATI AERATGVLRN
IGQPNKQNKV IMVRNGVTAH AIAVLRTSMR FQSQLREQQN ARTPKNQIDA AKNQILSIYE
NCLSILNNVT KMGKDDILDS AIQACRMISA NPDAAIVLLH FLNAGAPKCR KLAVNVMKRV
IENVPAFAEP FVDLPGTTQE TLPILLLKRA YESLDEWKKA VVEVMRSEPN TQQFRDAIEK
RQDHEDIVWK SVSLLSNLCR NGNPRFFERV KVEMLYTRPT NPFTSLFPEM SDVILYEWLD
FILAICGTEW SLQNCLMYHF LKQANITHEY LLHYRRPNPQ ICDKIKNIID TGMRQQQQHN
QLEQMAMMHA QQQHQQLPM
