WNT8C_CHICK
ID WNT8C_CHICK Reviewed; 357 AA.
AC P51030;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein Wnt-8c;
DE AltName: Full=CWnt-8;
DE Flags: Precursor;
GN Name=WNT8C;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn;
RX PubMed=7916678; DOI=10.1242/dev.119.4.1147;
RA Hume C.R., Dodd J.;
RT "Cwnt-8C: a novel Wnt gene with a potential role in primitive streak
RT formation and hindbrain organization.";
RL Development 119:1147-1160(1993).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Probable developmental protein. Is likely to
CC signal over only few cell diameters. May be involved in the regulation
CC of axis formation and in the rhombomere specification.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Cells that form rhombomere 4. Hensen node and the
CC neural plate immediately anterior to it.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors (By similarity). Depalmitoleoylation leads to Wnt signaling
CC pathway inhibition (By similarity). {ECO:0000250|UniProtKB:P28026,
CC ECO:0000250|UniProtKB:P56704}.
CC -!- PTM: Proteolytic processing by tiki1 and tiki2 promotes oxidation and
CC formation of large disulfide-bond oligomers, leading to inactivation of
CC wnt8c. {ECO:0000250|UniProtKB:P28026}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; U02097; AAA18933.1; -; mRNA.
DR PIR; I50690; I50690.
DR RefSeq; NP_990862.1; NM_205531.1.
DR AlphaFoldDB; P51030; -.
DR SMR; P51030; -.
DR STRING; 9031.ENSGALP00000009803; -.
DR PaxDb; P51030; -.
DR GeneID; 396543; -.
DR KEGG; gga:396543; -.
DR CTD; 7478; -.
DR VEuPathDB; HostDB:geneid_396543; -.
DR eggNOG; KOG3913; Eukaryota.
DR InParanoid; P51030; -.
DR OrthoDB; 618621at2759; -.
DR PhylomeDB; P51030; -.
DR PRO; PR:P51030; -.
DR Proteomes; UP000000539; Unplaced.
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:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:AgBase.
DR GO; GO:0060173; P:limb development; TAS:AgBase.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IMP:AgBase.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:AgBase.
DR GO; GO:0090270; P:regulation of fibroblast growth factor production; IMP:AgBase.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR034312; Protein_Wnt-8A/8C.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR013301; Wnt8.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF92; PTHR12027:SF92; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01892; WNT8PROTEIN.
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..357
FT /note="Protein Wnt-8c"
FT /id="PRO_0000041454"
FT LIPID 187
FT /note="O-palmitoleoyl serine"
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..66
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 105..113
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 115..133
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 181..195
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 183..190
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 260..298
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 276..291
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 313..328
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 315..325
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 320..321
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 357 AA; 40042 MW; 58ADD7E835A5B8C4 CRC64;
MRGSTFLLLS IVGIYGAILN AAAWSVNNFL MTGPKAYLTY SSSVAAGAQS GMEECKFQFG
WERWNCPESA LQLSTHNRLR SATRETSFVH AISSAGVMYT LTRNCSLGDF ESCGCDDSRN
GRVGGRGWVW GGCSDNVEFG ERISKLFVDA LETGHDTRAL INLHNNEVGR LAVKATMKRA
CKCHGVSGSC SIQTCWLQLA DFREIGNYLK MKYDQAHKLE MDKRRMRAGN SADSRGATAE
TFHHVHSTEL VFLEDSPDYC TRNASLGHHG TEGRECLQTG KNLSQWERRS CRRLSTECGL
KVEERRTEVV SSCNCKFHWC CTVRCEQCRQ LVAKHFCARR DAAVANHTKR RNKGHRR
