WNT1_CAEEL
ID WNT1_CAEEL Reviewed; 372 AA.
AC P34888;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein Wnt-1;
DE Flags: Precursor;
GN Name=cwn-1; Synonyms=wnt-1; ORFNames=K10B4.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-335, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=8510930;
RA Shackleford G.M., Shivakumar S., Shiue L., Mason J., Kenyon C.,
RA Varmus H.E.;
RT "Two wnt genes in Caenorhabditis elegans.";
RL Oncogene 8:1857-1864(1993).
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=16109397; DOI=10.1016/j.ydbio.2005.07.014;
RA Zinovyeva A.Y., Forrester W.C.;
RT "The C. elegans Frizzled CFZ-2 is required for cell migration and interacts
RT with multiple Wnt signaling pathways.";
RL Dev. Biol. 285:447-461(2005).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16516839; DOI=10.1016/j.devcel.2006.02.010;
RA Pan C.L., Howell J.E., Clark S.G., Hilliard M., Cordes S., Bargmann C.I.,
RA Garriga G.;
RT "Multiple Wnts and frizzled receptors regulate anteriorly directed cell and
RT growth cone migrations in Caenorhabditis elegans.";
RL Dev. Cell 10:367-377(2006).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=18622031; DOI=10.1534/genetics.108.090290;
RA Zinovyeva A.Y., Yamamoto Y., Sawa H., Forrester W.C.;
RT "Complex network of Wnt signaling regulates neuronal migrations during
RT Caenorhabditis elegans development.";
RL Genetics 179:1357-1371(2008).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19561603; DOI=10.1038/nn.2347;
RA Hayashi Y., Hirotsu T., Iwata R., Kage-Nakadai E., Kunitomo H.,
RA Ishihara T., Iino Y., Kubo T.;
RT "A trophic role for Wnt-Ror kinase signaling during developmental pruning
RT in Caenorhabditis elegans.";
RL Nat. Neurosci. 12:981-987(2009).
RN [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [10]
RP FUNCTION.
RX PubMed=25917219; DOI=10.1016/j.ydbio.2015.04.015;
RA Chien S.C., Gurling M., Kim C., Craft T., Forrester W., Garriga G.;
RT "Autonomous and nonautonomous regulation of Wnt-mediated neuronal polarity
RT by the C. elegans Ror kinase CAM-1.";
RL Dev. Biol. 404:55-65(2015).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Probable developmental protein. May be a
CC signaling molecule which affects the development of discrete regions of
CC tissues. Is likely to signal over only few cell diameters. Binds
CC receptor tyrosine kinase cam-1 (PubMed:17942487). Together with Wnt
CC ligand cwn-2, regulates the migration of CAN, ALM, BDU and HSN neurons
CC during embryogenesis, the migration of QL and QR neuroblast descendants
CC during larval development, and polarity of ALM neurons
CC (PubMed:16109397, PubMed:16516839, PubMed:18622031, PubMed:25917219).
CC Also acts with the Wnt ligand egl-20 to direct HSN neuron migration
CC (PubMed:16516839). Acts through the Wnt receptor cfz-2 to direct ALM
CC migration (PubMed:16109397). Also plays a role in axon growth and
CC guidance in HSN and male CP neurons (PubMed:16109397). In addition,
CC together with Wnt ligand cwn-2, negatively regulates developmental
CC neurite pruning of AIM neurons probably by acting as a ligand for
CC receptor tyrosine kinase cam-1 (PubMed:19561603). Probably by
CC activating the Wnt/Frizzled pathway, may regulate vulva development
CC (PubMed:17942487). May act redundantly with other Wnt ligands such as
CC cwn-2 and mom-2 to control seam cell polarity (PubMed:22022276).
CC {ECO:0000269|PubMed:16109397, ECO:0000269|PubMed:16516839,
CC ECO:0000269|PubMed:17942487, ECO:0000269|PubMed:18622031,
CC ECO:0000269|PubMed:19561603, ECO:0000269|PubMed:22022276,
CC ECO:0000269|PubMed:25917219, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q2LMP1}. Cytoplasm
CC {ECO:0000269|PubMed:22022276}. Cell membrane
CC {ECO:0000269|PubMed:22022276}; Peripheral membrane protein
CC {ECO:0000269|PubMed:22022276}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, some head neurons and
CC ventral nerve cord and pharyngeal neurons (PubMed:19561603). Expressed
CC in the tail and weakly expressed in the vulva and body wall muscles
CC (PubMed:20711352). Expressed highly in posterior dorsal and ventral
CC muscle cells (PubMed:22022276). {ECO:0000269|PubMed:19561603,
CC ECO:0000269|PubMed:20711352, ECO:0000269|PubMed:22022276}.
CC -!- DEVELOPMENTAL STAGE: Detected in all larval forms and adults, but is
CC most abundant in the embryonic stage (PubMed:8510930). First expressed
CC in the embryonic tail at the comma stage of embryogenesis
CC (PubMed:16516839). In newly hatched larvae, it is expressed in four
CC stripes of cells lining the dorsal and ventral posterior quadrants of
CC the body (PubMed:16516839). Expression spreads anteriorly becoming
CC restricted to the ventral side of the body as development progresses
CC (PubMed:16516839). {ECO:0000269|PubMed:16516839,
CC ECO:0000269|PubMed:8510930}.
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: Defective ALM, BDU and QR neuroblast migration
CC and irregular HSN and CP axon growth and guidance (PubMed:16109397).
CC Double knockout with cwn-2 results in ALM and CAN migration defects
CC (PubMed:16109397). Double knockout with either cwn-2 or egl-20 results
CC in HSN migration defects (PubMed:16516839). Triple knockout with cwn-2
CC and cfz-2 results in enhanced neuronal cell migratory defects
CC (PubMed:16109397). {ECO:0000269|PubMed:16109397,
CC ECO:0000269|PubMed:16516839}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; X72941; CAA51446.1; -; mRNA.
DR EMBL; X72942; CAA51447.1; -; Genomic_DNA.
DR EMBL; FO080912; CCD67737.1; -; Genomic_DNA.
DR PIR; S32694; S32694.
DR PIR; T43627; T43627.
DR RefSeq; NP_493668.1; NM_061267.4.
DR AlphaFoldDB; P34888; -.
DR SMR; P34888; -.
DR BioGRID; 38779; 3.
DR DIP; DIP-24702N; -.
DR IntAct; P34888; 1.
DR STRING; 6239.K10B4.6a; -.
DR EPD; P34888; -.
DR PaxDb; P34888; -.
DR EnsemblMetazoa; K10B4.6a.1; K10B4.6a.1; WBGene00000857.
DR GeneID; 173399; -.
DR KEGG; cel:CELE_K10B4.6; -.
DR UCSC; K10B4.6a; c. elegans.
DR CTD; 173399; -.
DR WormBase; K10B4.6a; CE12072; WBGene00000857; cwn-1.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000171022; -.
DR HOGENOM; CLU_033039_1_0_1; -.
DR InParanoid; P34888; -.
DR OMA; FRHIGMA; -.
DR OrthoDB; 745245at2759; -.
DR PhylomeDB; P34888; -.
DR Reactome; R-CEL-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-CEL-4086400; PCP/CE pathway.
DR SignaLink; P34888; -.
DR PRO; PR:P34888; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000857; Expressed in embryo and 22 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; ISS:WormBase.
DR GO; GO:0048018; F:receptor ligand activity; ISS:WormBase.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:WormBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IGI:WormBase.
DR GO; GO:1904936; P:interneuron migration; IMP:UniProtKB.
DR GO; GO:0097475; P:motor neuron migration; IMP:UniProtKB.
DR GO; GO:0097402; P:neuroblast migration; IMP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:1905488; P:positive regulation of anterior/posterior axon guidance; IGI:UniProtKB.
DR GO; GO:1905485; P:positive regulation of motor neuron migration; IGI:UniProtKB.
DR GO; GO:1905491; P:positive regulation of sensory neuron axon guidance; IGI:UniProtKB.
DR GO; GO:0040028; P:regulation of vulval development; IGI:WormBase.
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 Cell membrane; Cytoplasm; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Lipoprotein; Membrane; Neurogenesis;
KW Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..372
FT /note="Protein Wnt-1"
FT /id="PRO_0000041473"
FT LIPID 231
FT /note="O-palmitoleoyl serine; by mom-1"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..88
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 130..138
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 140..158
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 225..239
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 227..234
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 301..332
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 317..327
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 331..371
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 347..362
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 349..359
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 354..355
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 372 AA; 41975 MW; DF1BCE49FEEFBAB3 CRC64;
MLKSTQVILI FILLISIVES LSWLALGLAA NRFDRDKPGT SCKSLKGLTR RQMRFCKKNI
DLMESVRSGS LAAHAECQFQ FHKRRWNCTL IDPVTHEVIP DVFLYENTRE SAFVHAISSA
AVAYKVTRDC ARGISERCGC DYSKNDHSGK SQFQYQGCSD NVKFGIGVSK EFVDSAQRRV
LMMKDDNGTS LLGPSQLSAD GMHMINLHNN QAGRQVLEKS LRRECKCHGM SGSCEMRTCW
DSLPNFRHIG MAIKDKFDGA AEVKVVKEDG IEKPRIVMKN SQFKRHTNAD LVYMTPSPDF
CESDPLRGIL GTKGRQCTLA PNAIDDCSLL CCGRGYEKKV QIVEEKCNCK FIYCCEVRCE
PCQKRIEKYL CL
