WNT4_XENLA
ID WNT4_XENLA Reviewed; 351 AA.
AC P49338; Q5PPW9; Q91927;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein Wnt-4;
DE Short=XWnt-4;
DE Flags: Precursor;
GN Name=wnt4;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Neurula;
RX PubMed=1425335; DOI=10.1242/dev.115.2.463;
RA McGrew L.L., Otte A.P., Moon R.T.;
RT "Analysis of Xwnt-4 in embryos of Xenopus laevis: a Wnt family member
RT expressed in the brain and floor plate.";
RL Development 115:463-473(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 261-351 (ISOFORMS 1/2), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=1991549; DOI=10.1016/0012-1606(91)90073-c;
RA Christian J.L., Gavin B.J., McMahon A.P., Moon R.T.;
RT "Isolation of cDNAs partially encoding four Xenopus Wnt-1/int-1-related
RT proteins and characterization of their transient expression during
RT embryonic development.";
RL Dev. Biol. 143:230-234(1991).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12142017; DOI=10.1006/dbio.2002.0712;
RA Saulnier D.M., Ghanbari H., Brandli A.W.;
RT "Essential function of Wnt-4 for tubulogenesis in the Xenopus pronephric
RT kidney.";
RL Dev. Biol. 248:13-28(2002).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=19793883; DOI=10.1242/dev.042606;
RA Naylor R.W., Jones E.A.;
RT "Notch activates Wnt-4 signalling to control medio-lateral patterning of
RT the pronephros.";
RL Development 136:3585-3595(2009).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19223472; DOI=10.1128/mcb.01503-08;
RA Kim H., Cheong S.M., Ryu J., Jung H.J., Jho E.H., Han J.K.;
RT "Xenopus Wntless and the retromer complex cooperate to regulate XWnt4
RT secretion.";
RL Mol. Cell. Biol. 29:2118-2128(2009).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Plays an important role in embryonic kidney
CC development. Acts downstream of Notch signaling during pronephric
CC kidney development. During early pronephros development, patterns the
CC proximal pronephric anlagen to promote glomus and nephrostome
CC formation. Also required later in pronephros development for
CC tubulogenesis. {ECO:0000269|PubMed:12142017,
CC ECO:0000269|PubMed:19793883}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:19223472}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49338-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49338-2; Sequence=VSP_040030;
CC -!- TISSUE SPECIFICITY: Expressed in the brain and floor plate. In the
CC developing pronephros, expressed in the proximal tubules and
CC nephrostomes but absent from the pronephric duct.
CC {ECO:0000269|PubMed:12142017, ECO:0000269|PubMed:1425335,
CC ECO:0000269|PubMed:1991549}.
CC -!- DEVELOPMENTAL STAGE: Expression during the neurula through tadpole
CC stages of development. {ECO:0000269|PubMed:1425335,
CC ECO:0000269|PubMed:1991549}.
CC -!- INDUCTION: By Notch signaling in the pronephros.
CC {ECO:0000269|PubMed:19793883}.
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; U13183; AAA20879.1; -; mRNA.
DR EMBL; BC087460; AAH87460.1; -; mRNA.
DR EMBL; M55055; AAA69970.1; -; mRNA.
DR PIR; A49146; A49146.
DR RefSeq; NP_001081197.1; NM_001087728.1.
DR RefSeq; NP_001239014.1; NM_001252085.1. [P49338-1]
DR AlphaFoldDB; P49338; -.
DR SMR; P49338; -.
DR DNASU; 397706; -.
DR GeneID; 397706; -.
DR KEGG; xla:397706; -.
DR CTD; 397706; -.
DR Xenbase; XB-GENE-865047; wnt4.L.
DR OrthoDB; 745245at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 397706; Expressed in neurula embryo and 13 other tissues.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
DR GO; GO:0072013; P:glomus development; IMP:UniProtKB.
DR GO; GO:0039018; P:nephrostome development; IMP:UniProtKB.
DR GO; GO:0039020; P:pronephric nephron tubule development; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Lipoprotein; Reference proteome;
KW 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_0000041426"
FT LIPID 212
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
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"
FT VAR_SEQ 1..26
FT /note="MTPEYFLRSLLMMILAVFSANASNWL -> MDCQTAKITFSEGSVSSKEEQL
FT DCQPPCLQVFQIYAFSMKAW (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040030"
FT CONFLICT 49
FT /note="P -> L (in Ref. 2; AAH87460)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="Q -> H (in Ref. 3; AAA69970)"
FT /evidence="ECO:0000305"
FT CONFLICT 335..351
FT /note="FVKCKQCHKVVEMHTCR -> SRVDLQACNLVFYSVT (in Ref. 3;
FT AAA69970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39167 MW; 0F87DF08F904938A CRC64;
MTPEYFLRSL LMMILAVFSA NASNWLYLAK LSSVGSISEE ETCEKLKGPI QRQVQMCKRN
LEVMDSVRRG AQLAIEECQY QFRNRRWNCS TLDTLPVFGK VVTQGTREAA FVYAISSAGV
AFAVTRACSS GDLEKCGCDR TVHGVSPQGF QWSGCSDNIL YGVAFSQSFV DVRERSKGGS
SSRALMNLHN NEAGRKAILN NMRVECKCHG VSGSCEVKTC WKAMPTFRKV GNVLKEKFDG
ATEVEQKKIG STKVLVPKNS QFKPHTDEDL VYLDSSPDFC DHDLKNGVLG TTGRQCNKTS
KAIDGCELMC CGRGFHTEEV EIVERCSCKF HWCCFVKCKQ CHKVVEMHTC R
