ID   LIN44_CAEBR             Reviewed;         341 AA.
AC   A8XEH1;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Abnormal cell lineage protein 44 {ECO:0000303|PubMed:18164284, ECO:0000312|EMBL:CAP31106.2};
DE   AltName: Full=Wnt protein {ECO:0000303|PubMed:18164284};
DE   Flags: Precursor;
GN   Name=lin-44 {ECO:0000312|EMBL:CAP31106.2,
GN   ECO:0000312|WormBase:CBG12066}; ORFNames=CBG12066;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP31106.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP31106.2};
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).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION.
RX   PubMed=18164284; DOI=10.1016/j.ydbio.2007.11.015;
RA   Zhao Z., Boyle T.J., Bao Z., Murray J.I., Mericle B., Waterston R.H.;
RT   "Comparative analysis of embryonic cell lineage between Caenorhabditis
RT   briggsae and Caenorhabditis elegans.";
RL   Dev. Biol. 314:93-99(2008).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors (By similarity). Affects male tail development,
CC       vulval precursor cell specification and egg laying. Involved in
CC       morphogenesis by influencing polarity of asymmetric cell divisions of
CC       the B, U, and F cells in the male, and the T cell in males and
CC       hermaphrodites. Controls spindle orientation in B-gamma cell division
CC       during male copulatory spicule development. Involved in specification
CC       of the P7.p lineage during vulval development. Has a role in providing
CC       polarity and default lin-17 localization in axon development and
CC       positioning of neuromuscular synapses in DA9 regions by negatively
CC       regulating synaptogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:Q27886}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P24383}.
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   -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000255}.
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DR   EMBL; HE601540; CAP31106.2; -; Genomic_DNA.
DR   RefSeq; XP_002646352.1; XM_002646306.1.
DR   AlphaFoldDB; A8XEH1; -.
DR   SMR; A8XEH1; -.
DR   STRING; 6238.A8XEH1; -.
DR   GlyCosmos; A8XEH1; 1 site, No reported glycans.
DR   EnsemblMetazoa; CBG12066.1; CBG12066.1; WBGene00033074.
DR   GeneID; 8588349; -.
DR   WormBase; CBG12066; CBP33782; WBGene00033074; Cbr-lin-44.
DR   eggNOG; KOG3913; Eukaryota.
DR   HOGENOM; CLU_033039_1_0_1; -.
DR   InParanoid; A8XEH1; -.
DR   OMA; ESAYLWA; -.
DR   OrthoDB; 2872881at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
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; IBA:GO_Central.
DR   GO; GO:0008356; P:asymmetric cell division; IEA:EnsemblMetazoa.
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:0060573; P:cell fate specification involved in pattern specification; IEA:EnsemblMetazoa.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:EnsemblMetazoa.
DR   GO; GO:1904936; P:interneuron migration; IEA:EnsemblMetazoa.
DR   GO; GO:0097475; P:motor neuron migration; IEA:EnsemblMetazoa.
DR   GO; GO:0045138; P:nematode male tail tip morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0097402; P:neuroblast migration; IEA:EnsemblMetazoa.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; IEA:EnsemblMetazoa.
DR   GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:1905485; P:positive regulation of motor neuron migration; IEA:EnsemblMetazoa.
DR   GO; GO:0010623; P:programmed cell death involved in cell development; IEA:EnsemblMetazoa.
DR   GO; GO:0046662; P:regulation of egg-laying behavior; IEA:EnsemblMetazoa.
DR   GO; GO:0040028; P:regulation of vulval development; IEA:EnsemblMetazoa.
DR   GO; GO:0040025; P:vulval development; IEA:EnsemblMetazoa.
DR   CDD; cd13113; Wnt; 1.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027:SF115; ABNORMAL CELL LINEAGE PROTEIN 44; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
PE   3: Inferred from homology;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..341
FT                   /note="Abnormal cell lineage protein 44"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000403172"
FT   LIPID           212
FT                   /note="O-palmitoleoyl serine; by mom-1"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        84..95
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        134..142
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        144..158
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        206..220
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        208..215
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        265..292
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        275..287
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        291..331
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        307..322
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        309..319
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        314..315
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   341 AA;  37831 MW;  5E24CD3DB58052C3 CRC64;
     MRALYFRTTT LSTFFILCSL ASNDIPRTGG NKIVQPPKPN ILKQGCPSDL LHSRALRSIQ
     LACRSHPATV ISAFEGIQEG LQNCANRLRF QQWDCSEAGN IMHDPPLLRQ GFRESSLIWA
     LSSASAAWGV ATACAQGWID DCACNNHMGQ NEYEFGGCTH GVQHGITASR KLLTKVGAVN
     SLLRKVEKHN LKAGRLAIKK TLISSCKCHG VSGSCQQKTC WKRTATLEHI TDYLVEKYAR
     AKLYTDDSVV KTTDLIYLEA SPDVCKVKSV AGRVCAWRNE THTQGDCDRL CCGNGFSIRH
     EVVRVKCDCE FVWCCNLVCK DCIQHRWIST CNGTPPKSLI F
//