LIN44_CAEBR
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 25-MAY-2022, entry version 67.
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, ECO:0000312|WormBase:CBG12066};
GN 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 AlphaFoldDB; A8XEH1; -.
DR SMR; A8XEH1; -.
DR STRING; 6238.CBG12066; -.
DR EnsemblMetazoa; CBG12066.1; CBG12066.1; WBGene00033074.
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; 787436at2759; -.
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:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
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 oviposition; IEA:EnsemblMetazoa.
DR GO; GO:0040028; P:regulation of vulval development; IEA:EnsemblMetazoa.
DR GO; GO:0040025; P:vulval development; IEA:EnsemblMetazoa.
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 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
