WNT4_CHICK
ID WNT4_CHICK Reviewed; 351 AA.
AC P49337;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein Wnt-4;
DE Flags: Precursor;
GN Name=WNT4; Synonyms=WNT-4;
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 TISSUE=Embryo;
RX PubMed=7945308; DOI=10.1006/bbrc.1994.2367;
RA Yoshioka H., Ohuchi H., Nohno T., Fujiwara A., Tanda N., Kawakami Y.,
RA Noji S.;
RT "Regional expression of the Cwnt-4 gene in developing chick central nervous
RT system in relationship to the diencephalic neuromere D2 and a dorsal domain
RT of the spinal cord.";
RL Biochem. Biophys. Res. Commun. 203:1581-1588(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7579581; DOI=10.3109/10425179509030981;
RA Tanda N., Kawakami Y., Saito T., Noji S., Nohno T.;
RT "Cloning and characterization of Wnt-4 and Wnt-11 cDNAs from chick
RT embryo.";
RL DNA Seq. 5:277-281(1995).
RN [3]
RP INTERACTION WITH CPZ.
RX PubMed=12944424; DOI=10.1242/dev.00686;
RA Moeller C., Swindell E.C., Kispert A., Eichele G.;
RT "Carboxypeptidase Z (CPZ) modulates Wnt signaling and regulates the
RT development of skeletal elements in the chicken.";
RL Development 130:5103-5111(2003).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors (Probable). Plays an important role in
CC embryonic development (By similarity). {ECO:0000250|UniProtKB:P22724,
CC ECO:0000305}.
CC -!- SUBUNIT: Interacts with CPZ. {ECO:0000269|PubMed:12944424}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the diencephalon
CC neuromere D2.
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:0000305}.
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DR EMBL; D31900; BAA06698.1; -; mRNA.
DR PIR; JC2451; JC2451.
DR RefSeq; NP_990114.1; NM_204783.1.
DR AlphaFoldDB; P49337; -.
DR SMR; P49337; -.
DR STRING; 9031.ENSGALP00000007633; -.
DR PaxDb; P49337; -.
DR Ensembl; ENSGALT00000080352; ENSGALP00000046583; ENSGALG00000041708.
DR GeneID; 395561; -.
DR KEGG; gga:395561; -.
DR CTD; 54361; -.
DR VEuPathDB; HostDB:geneid_395561; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000159654; -.
DR HOGENOM; CLU_033039_1_4_1; -.
DR InParanoid; P49337; -.
DR OMA; CWRAMPP; -.
DR OrthoDB; 745245at2759; -.
DR PhylomeDB; P49337; -.
DR TreeFam; TF105310; -.
DR Reactome; R-GGA-3238698; WNT ligand biogenesis and trafficking.
DR PRO; PR:P49337; -.
DR Proteomes; UP000000539; Chromosome 21.
DR Bgee; ENSGALG00000041708; Expressed in liver and 8 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0060993; P:kidney morphogenesis; NAS:AgBase.
DR GO; GO:2000180; P:negative regulation of androgen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0061036; P:positive regulation of cartilage development; TAS:AgBase.
DR GO; GO:0014858; P:positive regulation of skeletal muscle cell proliferation; IMP:AgBase.
DR GO; GO:1902811; P:positive regulation of skeletal muscle fiber differentiation; IMP:AgBase.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR009142; Wnt4.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01844; WNT4PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..351
FT /note="Protein Wnt-4"
FT /id="PRO_0000041425"
FT LIPID 212
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..89
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 128..136
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 138..155
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 280..311
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 296..306
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 310..350
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 326..341
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 328..338
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 333..334
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 351 AA; 38963 MW; D22DC689284A961C CRC64;
MSPEYFLRSL LLIILATFSA NASNWLYLAK LSSVGSISEE ETCEKLKGLI QRQVQMCKRN
LEVMDSVRRG AQLAIEECQY QFRNRRWNCS TLDTLPVFGK VVTQGTREAA FVYAISSAGV
AFAVTRACSS GELDKCGCDR TVQGGSPQGF QWSGCSDNIA YGVAFSQSFV DVRERSKGAS
SNRALMNLHN NEAGRKAILN NMRVECKCHG VSGSCEFKTC WKAMPPFRKV GNVLKEKFDG
ATEVEQSEIG STKVLVPKNS QFKPHTDEDL VYLDSSPDFC DHDLKNGVLG TSGRQCNKTS
KAIDGCELMC CGRGFHTDEV EVVERCSCKF HWCCSVKCKP CHRVVEIHTC R
