ID   WNT5B_ORYLA             Reviewed;         371 AA.
AC   O42122;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Protein Wnt-5b;
DE   Flags: Precursor;
GN   Name=wnt5b;
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yokoi H., Nishimatsu A., Ozato K., Yoda K.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
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; AB006579; BAA22143.1; -; mRNA.
DR   RefSeq; NP_001098129.1; NM_001104659.1.
DR   RefSeq; XP_011489304.1; XM_011491002.1.
DR   AlphaFoldDB; O42122; -.
DR   SMR; O42122; -.
DR   STRING; 8090.ENSORLP00000017197; -.
DR   Ensembl; ENSORLT00000032686; ENSORLP00000030767; ENSORLG00000013709.
DR   GeneID; 100049184; -.
DR   KEGG; ola:100049184; -.
DR   CTD; 81029; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000157617; -.
DR   HOGENOM; CLU_033039_0_1_1; -.
DR   InParanoid; O42122; -.
DR   OMA; EHARMLM; -.
DR   OrthoDB; 695671at2759; -.
DR   TreeFam; TF105310; -.
DR   Proteomes; UP000001038; Chromosome 23.
DR   Proteomes; UP000265180; Unplaced.
DR   Proteomes; UP000265200; Unplaced.
DR   Bgee; ENSORLG00000013709; Expressed in heart and 11 other tissues.
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:0048513; P:animal organ development; IEA:UniProt.
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:0042692; P:muscle cell differentiation; ISS:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
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   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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..371
FT                   /note="Protein Wnt-5b"
FT                   /id="PRO_0000041436"
FT   LIPID           235
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..106
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        145..153
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        155..173
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        229..243
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        231..238
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        300..331
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        316..326
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        330..370
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        346..361
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        348..358
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        353..354
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   371 AA;  42280 MW;  E9864E1FA342E82D CRC64;
     MDNRSVQRRR TGDVRHLLLA AAFLTCNSQL LLVDANSWWS LGLTPIQRPE MYIIGAQPLC
     SQLSGLSQGQ RKLCQLYQDH MTYIGDGAKT GIKECQYQFR QRRWNCSTVD NTSVFGRVMQ
     IGSRETAFTY AISAAGVVNA ISRACREGEL STCGCSRTAR PRDLPRDWLW GGCGDNVYYG
     KRFAQEFVDA REREKNYPRG SREHARTLMN LHNNEAGRQA VYNLADVACK CHGVSGSCSL
     KTCWLQLADF RRVGEFLKEK YDSAAAMRIG RKGRLELLDK RFNPPTPEDL VYIDLSPDYC
     HRNETTGSLG TQGRFCNKTS EGMDGCELMC CGRGYDQFRV YKHERCHCKF HWCCYVKCKR
     CSTLVDQFVC K