WNT5B_XENLA
ID WNT5B_XENLA Reviewed; 360 AA.
AC P33945; Q7T0M2; Q91928;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein Wnt-5b;
DE AltName: Full=Protein Wnt-5c;
DE Short=XWnt-5C;
DE Flags: Precursor;
GN Name=wnt5b; Synonyms=wnt5c;
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], AND DEVELOPMENTAL STAGE.
RC TISSUE=Neurula;
RA Koster J.G., Kuiken G.A., Stegeman B., Peterson J., Eizema K., Stabel L.,
RA Dekker E.J., Destre O.H.J.;
RT "Differential Xwnt-5C expression during early development of Xenopus
RT laevis.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC TISSUE=Embryo;
RX PubMed=8202371; DOI=10.1093/nar/22.9.1675;
RA Kuiken G.A., Bertens P.J.A., Peterson-Maduro J., Veenstra G.J.C.,
RA Koster J.G., Destree O.H.J.;
RT "The promoter of the Xwnt-5C gene contains octamer and AP-2 motifs
RT functional in Xenopus embryos.";
RL Nucleic Acids Res. 22:1675-1680(1994).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Probable developmental protein. May be a
CC signaling molecule which affects the development of discrete regions of
CC tissues. Is likely to signal over only few cell diameters.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- DEVELOPMENTAL STAGE: Expressed from the early gastrula stage onwards.
CC {ECO:0000269|Ref.1}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X73510; CAA51916.1; -; mRNA.
DR EMBL; BC056128; AAH56128.1; -; mRNA.
DR EMBL; X76190; CAA53784.1; -; Genomic_DNA.
DR PIR; S34173; S34173.
DR RefSeq; NP_001080150.1; NM_001086681.1.
DR AlphaFoldDB; P33945; -.
DR SMR; P33945; -.
DR DNASU; 379842; -.
DR GeneID; 379842; -.
DR KEGG; xla:379842; -.
DR CTD; 379842; -.
DR Xenbase; XB-GENE-865372; wnt5b.S.
DR OrthoDB; 695671at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 379842; Expressed in lung and 13 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0042692; P:muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:1904105; P:positive regulation of convergent extension involved in gastrulation; ISS:UniProtKB.
DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; ISS: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; IPR026537; Wnt5b.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF87; PTHR12027:SF87; 1.
DR Pfam; PF00110; wnt; 1.
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..360
FT /note="Protein Wnt-5b"
FT /id="PRO_0000041437"
FT LIPID 224
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
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..162
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 218..232
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 220..227
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 289..320
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 305..315
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 319..359
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 335..350
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 337..347
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 342..343
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CONFLICT 15
FT /note="S -> C (in Ref. 3; CAA53784)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="L -> M (in Ref. 1; CAA51916)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> S (in Ref. 1; CAA51916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 40681 MW; 997A1AA2581CDDBB CRC64;
MTPILRLLLL SSLLSCWKQS VVGANSWWSL ALNPVQRPEM FIIGAQPLCS QLTGLSPGQR
KLCQLYQDHM VHIGEGAKTG IKECQHQFKH RRWNCSTVDN NSVFGRVMQI GSREAAFTYA
ISSAGVVNAI SRACREGELS TCGCSRTPRP KDLPRDWLWG GCGDNVEYGY RFAKEFVDAR
EREKNFPKGS EEQARSLMNL QNNEAGRRAV YKLADVACKC HGVSGSCSLK TCWLQLADFR
KVGEYIKEKY DSAASMRLNK RNKLEQVNQR FNPPTGEDLV YLDPSPDYCL YNETTGSLGT
HGRQCNKTSE GMDGCELMCC GRGYDQFKTV QVERCHCKFQ WCCFVKCKKC TEIVDQFVCK
