ID   WNT5B_PONAB             Reviewed;         359 AA.
AC   Q5NVK2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Protein Wnt-5b;
DE   Flags: Precursor;
GN   Name=WNT5B;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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   -!- SUBUNIT: Interacts with PORCN. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
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; CR926024; CAI29661.1; -; mRNA.
DR   RefSeq; NP_001127098.1; NM_001133626.1.
DR   AlphaFoldDB; Q5NVK2; -.
DR   SMR; Q5NVK2; -.
DR   STRING; 9601.ENSPPYP00000004719; -.
DR   Ensembl; ENSPPYT00000004905; ENSPPYP00000004719; ENSPPYG00000004141.
DR   GeneID; 100174132; -.
DR   KEGG; pon:100174132; -.
DR   CTD; 81029; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000157617; -.
DR   HOGENOM; CLU_033039_0_1_1; -.
DR   InParanoid; Q5NVK2; -.
DR   OMA; EHARMLM; -.
DR   OrthoDB; 695671at2759; -.
DR   TreeFam; TF105310; -.
DR   Proteomes; UP000001595; Chromosome 12.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0042692; P:muscle cell differentiation; ISS:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; 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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..359
FT                   /note="Protein Wnt-5b"
FT                   /id="PRO_0000229769"
FT   LIPID           223
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..94
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        133..141
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        143..161
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        217..231
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        219..226
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        288..319
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        304..314
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        318..358
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        334..349
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        336..346
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        341..342
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   359 AA;  40349 MW;  B932E2CC374B8805 CRC64;
     MPSLLLLFTA ALLSSWAQLL TDANSWWSLA LNPVQRPEMF IIGAQPVCSQ LPGLSPGQRK
     LCQLYQEHMA YIGEGAKTGI KECQHQFRQR RWNCSTVDNA SVFGRVMQIG SRETAFTYAV
     SAAGVVNAIS RACREGELST CGCSRTARPK DLPRDWLWGG CGDNVEYGYR FAKEFVDARE
     REKNFAKGSE EQGRVLMNLQ NNEAGRRAVY KMADVACKCH GVSGSCSLKT CWLQLAEFRK
     VGDRLKEKYD SAAAMRVTRK GRLELVNSRF TQPTPEDLVY VDPSPDYCLR NESTGSLGTQ
     GRLCNKTSEG MDGCELMCCG RGYNQFKSVQ VERCHCKFHW CCFVKCKKCT EIVDQYICK