MOM2_CAEEL
ID MOM2_CAEEL Reviewed; 362 AA.
AC Q10459; O16146;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein mom-2;
DE Flags: Precursor;
GN Name=mom-2; ORFNames=F38E1.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Bristol N2;
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]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9288749; DOI=10.1016/s0092-8674(00)80530-9;
RA Thorpe C.J., Schlesinger A., Carter J.C., Bowerman B.;
RT "Wnt signaling polarizes an early C. elegans blastomere to distinguish
RT endoderm from mesoderm.";
RL Cell 90:695-705(1997).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15369677; DOI=10.1016/j.cell.2004.09.001;
RA Inoue T., Oz H.S., Wiland D., Gharib S., Deshpande R., Hill R.J.,
RA Katz W.S., Sternberg P.W.;
RT "C. elegans LIN-18 is a Ryk ortholog and functions in parallel to LIN-
RT 17/Frizzled in Wnt signaling.";
RL Cell 118:795-806(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16678095; DOI=10.1016/j.cell.2006.02.049;
RA Baenziger C., Soldini D., Schuett C., Zipperlen P., Hausmann G., Basler K.;
RT "Wntless, a conserved membrane protein dedicated to the secretion of Wnt
RT proteins from signaling cells.";
RL Cell 125:509-522(2006).
RN [6]
RP FUNCTION.
RX PubMed=17942487; DOI=10.1242/dev.005363;
RA Green J.L., Inoue T., Sternberg P.W.;
RT "The C. elegans ROR receptor tyrosine kinase, CAM-1, non-autonomously
RT inhibits the Wnt pathway.";
RL Development 134:4053-4062(2007).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=20711352; DOI=10.1371/journal.pgen.1001056;
RA Song S., Zhang B., Sun H., Li X., Xiang Y., Liu Z., Huang X., Ding M.;
RT "A Wnt-Frz/Ror-Dsh pathway regulates neurite outgrowth in Caenorhabditis
RT elegans.";
RL PLoS Genet. 6:E1001056-E1001056(2010).
RN [8]
RP FUNCTION.
RX PubMed=22022276; DOI=10.1371/journal.pgen.1002308;
RA Yamamoto Y., Takeshita H., Sawa H.;
RT "Multiple Wnts redundantly control polarity orientation in Caenorhabditis
RT elegans epithelial stem cells.";
RL PLoS Genet. 7:E1002308-E1002308(2011).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25344071; DOI=10.1242/dev.113266;
RA Dejima K., Kang S., Mitani S., Cosman P.C., Chisholm A.D.;
RT "Syndecan defines precise spindle orientation by modulating Wnt signaling
RT in C. elegans.";
RL Development 141:4354-4365(2014).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Required in embryonic development for endoderm
CC specification and the correct positioning and orientation of the
CC mitotic spindles and division planes in blastomere cells
CC (PubMed:9288750, PubMed:9288749, PubMed:16678095, PubMed:25344071).
CC Involved in cleavage axis determination (PubMed:9288750). Binds to
CC receptor tyrosine kinase cam-1 (PubMed:17942487). Together with wnt
CC ligand lin-44, plays a role in controlling vulva precursor cell P7.p
CC lineage orientation during vulva development, probably by acting as a
CC ligand for tyrosine kinase receptor lin-18 (PubMed:15369677). May act
CC redundantly with other Wnt ligands such as cwn-1 and cwn-2 to control
CC seam cell polarity (PubMed:22022276). {ECO:0000269|PubMed:15369677,
CC ECO:0000269|PubMed:16678095, ECO:0000269|PubMed:17942487,
CC ECO:0000269|PubMed:22022276, ECO:0000269|PubMed:9288749,
CC ECO:0000269|PubMed:9288750}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Expressed by anchor cell and vulva precursor cell
CC descendants P5.ppa, P5.ppp, P7.paa and P7.pap (PubMed:15369677).
CC Expressed in the tail and weakly expressed in the vulva and body wall
CC muscles (PubMed:20711352). {ECO:0000269|PubMed:15369677,
CC ECO:0000269|PubMed:20711352}.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors. Depalmitoleoylation leads to Wnt signaling pathway
CC inhibition. {ECO:0000250|UniProtKB:P27467,
CC ECO:0000250|UniProtKB:P56704}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal with severely defective
CC embryonic morphogenesis with the formation of unspecified
CC differentiated tissues, no endoderm and excess mesoderm
CC (PubMed:9288749). In addition, embryos have defective mitotic spindle
CC orientation in the 8-cell stage ABar blastomere (PubMed:9288749,
CC PubMed:16678095). RNAi-mediated knockdown results in irregular
CC distribution of the mitotic spindle orientating factor sdn-1 and wnt
CC signaling protein mig-5, with premature accumulation of sdn-1 on the
CC cell surface of the ABar blastomere during the prophase stage of
CC mitosis, and reduced accumulation of mig-5 at cell contact sites
CC between the Abar and C blastomere cells, respectively
CC (PubMed:25344071). {ECO:0000269|PubMed:16678095,
CC ECO:0000269|PubMed:25344071, ECO:0000269|PubMed:9288749}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; AF013952; AAC47749.1; -; mRNA.
DR EMBL; FO080433; CCD63659.1; -; Genomic_DNA.
DR PIR; T34254; T34254.
DR PIR; T42049; T42049.
DR RefSeq; NP_505154.1; NM_072753.5.
DR AlphaFoldDB; Q10459; -.
DR SMR; Q10459; -.
DR BioGRID; 44258; 35.
DR DIP; DIP-26433N; -.
DR IntAct; Q10459; 2.
DR STRING; 6239.F38E1.7; -.
DR EPD; Q10459; -.
DR PaxDb; Q10459; -.
DR EnsemblMetazoa; F38E1.7.1; F38E1.7.1; WBGene00003395.
DR GeneID; 179217; -.
DR KEGG; cel:CELE_F38E1.7; -.
DR UCSC; F38E1.7; c. elegans.
DR CTD; 179217; -.
DR WormBase; F38E1.7; CE17806; WBGene00003395; mom-2.
DR eggNOG; KOG3913; Eukaryota.
DR HOGENOM; CLU_033039_1_3_1; -.
DR InParanoid; Q10459; -.
DR OMA; ALHTCEY; -.
DR OrthoDB; 745245at2759; -.
DR PhylomeDB; Q10459; -.
DR Reactome; R-CEL-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-CEL-4086398; Ca2+ pathway.
DR Reactome; R-CEL-4086400; PCP/CE pathway.
DR SignaLink; Q10459; -.
DR PRO; PR:Q10459; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003395; Expressed in cell and 21 other tissues.
DR GO; GO:0005576; C:extracellular region; ISS:WormBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; ISS:WormBase.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI: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:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:WormBase.
DR GO; GO:0001714; P:endodermal cell fate specification; IMP:WormBase.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:1904936; P:interneuron migration; IGI:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; IMP:UniProtKB.
DR GO; GO:0097475; P:motor neuron migration; IGI:UniProtKB.
DR GO; GO:0097402; P:neuroblast migration; IGI:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IGI:UniProtKB.
DR GO; GO:1905485; P:positive regulation of motor neuron migration; IGI:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:WormBase.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..362
FT /note="Protein mom-2"
FT /id="PRO_0000041475"
FT REGION 263..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 223
FT /note="O-palmitoleoyl serine; by mom-1"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..91
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 129..137
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 139..167
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 217..231
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 219..226
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 304..322
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 313..317
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 321..361
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 337..352
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 339..349
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 344..345
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 362 AA; 40191 MW; ED69435F1F4F40DD CRC64;
MHINTPVLLA IIYFLVFAPK SADAWWLLSK TDTSSANSGS SPILCKNVPG LTPQQKRMCH
ENPNIIKYLI SGLRSALHTC EYTFQREAWN CTLTLPGVGT SPLQIASRES AYVYAISAAG
VSHSLARACS KGLIDDCGCG ETPQGSGSVA VSQASSRSSS DFVWAGCSDN VKFGNTFGRK
FVDQYDRQHA TEPRSQMNLH NNRVGRRLLV NAMNKECKCH GVSGSCVTKT CWKVMPKFDE
FASRLHQKYQ LAKLVTNNDQ KLTVRSSPSA GSSGRSERFA RNMDASSKQM RNELIYLDAS
PNYCAIDVKD RECGENCPNI CCGRGWRTTR EIVDEPCHCQ FVWCCEVKCK TCKKLVERNY
CL
