ID   WNT5B_AMBME             Reviewed;         357 AA.
AC   Q06443;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Protein Wnt-5b;
DE   Flags: Precursor;
GN   Name=WNT-5B;
OS   Ambystoma mexicanum (Axolotl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Caudata; Salamandroidea; Ambystomatidae; Ambystoma.
OX   NCBI_TaxID=8296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8443107; DOI=10.1016/0925-4773(93)90088-f;
RA   Busse U., Seguin C.;
RT   "Isolation of cDNAs for two closely related members of the axolotl Wnt
RT   family, Awnt-5A and Awnt-5B, and analysis of their expression during
RT   development.";
RL   Mech. Dev. 40:63-72(1993).
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   -!- TISSUE SPECIFICITY: Predominantly in neuroectodermal tissues.
CC   -!- DEVELOPMENTAL STAGE: Undetectable in the blastula. Appears with
CC       gastrulation, is present throughout neurulation and organogenesis, and
CC       decrease to barely detectable levels in hatched larvae.
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; Z14048; CAA78416.1; -; mRNA.
DR   PIR; B56549; B56549.
DR   AlphaFoldDB; Q06443; -.
DR   SMR; Q06443; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
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; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..357
FT                   /note="Protein Wnt-5b"
FT                   /id="PRO_0000041433"
FT   LIPID           221
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        81..92
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        131..139
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        141..159
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        215..229
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        217..224
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        286..317
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        302..312
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        316..356
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        332..347
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        334..344
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        339..340
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   357 AA;  40086 MW;  3AAD6E8807BF7DB4 CRC64;
     MPGIRLLLAA ALLCCPPPAG ATSWWSLAQN PVQRPEMYII GAQPVCSQLS SLSPGQKKLC
     QLYQDHMMYI GEGAKTGIKE CQYQFKQRRW NCSTVDNTSV FGRVMQIGSR ETAFTYAVSA
     AGVVNAISRA CREGELSTCG CSRTTRPKDL HRDWLWGGCG DNVDYGYRFA KEFVDARERE
     KNYPKGSEEQ ARTLMNLQNN EAGRRAVYKL ADAACKCHGV SGSCSLKTCW LQLADFRKVG
     DHLKEKYDSA AAMRINRKGK LELVNNRFNL PTVEDLVYTD QSPDYCLRNE STGSLGTLGR
     LCNKTSEGMD GCELMCCGRG YDQFKTVQVE RCHCKFHWCC FVKCKKCTEI VDQYVCK