ID   WNT5A_XENLA             Reviewed;         380 AA.
AC   P31286;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Protein Wnt-5a;
DE            Short=XWnt-5a;
DE   Flags: Precursor;
GN   Name=wnt5a;
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], TISSUE SPECIFICITY, AND FUNCTION.
RC   TISSUE=Oocyte;
RX   PubMed=8275867; DOI=10.1242/dev.119.1.97;
RA   Moon R.T., Campbell R.M., Christian J.L., McGrew L.L., Shih J., Fraser S.;
RT   "Xwnt-5A: a maternal Wnt that affects morphogenetic movements after
RT   overexpression in embryos of Xenopus laevis.";
RL   Development 119:97-111(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 238-363, 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).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors. Can activate or inhibit canonical Wnt
CC       signaling, depending on receptor context (By similarity). Plays a role
CC       in normal embryonic development (PubMed:8275867).
CC       {ECO:0000250|UniProtKB:P22725, ECO:0000269|PubMed:8275867}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P41221}. Secreted
CC       {ECO:0000250|UniProtKB:P41221}.
CC   -!- TISSUE SPECIFICITY: Found primarily in ectoderm with lower levels of
CC       expression in mesoderm. Detected in the head and tail with lower
CC       expression in the middle of the embryo. No expression was found in the
CC       notochord. {ECO:0000269|PubMed:8275867}.
CC   -!- DEVELOPMENTAL STAGE: Present in oocytes. Levels decrease during early
CC       embryo development and then increase considerably in neurula and
CC       tadpole stages. {ECO:0000269|PubMed:1991549}.
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; L19716; AAA16628.1; -; mRNA.
DR   EMBL; M55056; AAA50011.1; -; mRNA.
DR   PIR; B49764; B49764.
DR   RefSeq; NP_001079345.1; NM_001085876.1.
DR   AlphaFoldDB; P31286; -.
DR   SMR; P31286; -.
DR   BioGRID; 97270; 1.
DR   GeneID; 378689; -.
DR   KEGG; xla:378689; -.
DR   CTD; 378689; -.
DR   Xenbase; XB-GENE-6252367; wnt5a.S.
DR   OrthoDB; 695671at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 378689; Expressed in internal ear and 15 other tissues.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR   GO; GO:0005109; F:frizzled binding; NAS:BHF-UCL.
DR   GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR   GO; GO:0008595; P:anterior/posterior axis specification, embryo; IDA:BHF-UCL.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0042074; P:cell migration involved in gastrulation; TAS:BHF-UCL.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IGI:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:DFLAT.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR   GO; GO:0060061; P:Spemann organizer formation; IDA:BHF-UCL.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR026538; Wnt5a.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   PANTHER; PTHR12027:SF33; PTHR12027:SF33; 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..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..380
FT                   /note="Protein Wnt-5a"
FT                   /id="PRO_0000041431"
FT   LIPID           244
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        104..115
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        154..162
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        164..182
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        238..252
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        240..247
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        309..340
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        325..335
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        339..379
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        355..370
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        357..367
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        362..363
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   CONFLICT        261
FT                   /note="Missing (in Ref. 2; AAA50011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265
FT                   /note="H -> L (in Ref. 2; AAA50011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        274
FT                   /note="G -> A (in Ref. 2; AAA50011)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  42520 MW;  822E2259739E815D CRC64;
     MRKNLWTFQF GGEASGLVGS AMVSQHFVVL LMSLYCLTQS VVESSSWWSL GMNPVQMPEV
     YIIGAQPLCS QLSGLSQGQK KLCQLYQDHM QFIGDGAKTG IKECQYQFRH RRWNCSTVDN
     TSVFGRVMQI GSRETAFTYA ISAAGVVNAV SRACREGELS TCGCSRAARP KDLPRDWLWG
     GCGDNLDYGY RFAKEFVDAR EREKIHQKGS YESSRIMMNL HNNEAGRRAV STLADVACKC
     HGVSGSCSLK TCWLQLADFR KVGDHLKEKY DSAGAMKLNT RGKLVQVNNK FNSPTMNDLV
     YIDPSPDYCV HNESTGSLGT QGRLCNKTSE GMDGCELMCC GRGYDQFKTV QTERCHCKFH
     WCCYVKCKKC TEVVDQFACK