ID   WNT5A_AMBME             Reviewed;         359 AA.
AC   Q06442;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Protein Wnt-5a;
DE   Flags: Precursor;
GN   Name=WNT-5A;
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. Can activate or inhibit canonical Wnt
CC       signaling, depending on receptor context. Required during embryogenesis
CC       for extension of the primary anterior-posterior axis.
CC       {ECO:0000250|UniProtKB:P22725}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P41221}. Secreted
CC       {ECO:0000250|UniProtKB:P41221}.
CC   -!- TISSUE SPECIFICITY: Neuroectodermal and non-neuroectodermal tissues.
CC   -!- DEVELOPMENTAL STAGE: Abundant in the blastula until gastrulation,
CC       barely detectable during gastrulation, and increase again during
CC       neurulation. Detected throughout the remaining development and in
CC       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; Z14047; CAA78415.1; -; mRNA.
DR   PIR; A56549; A56549.
DR   AlphaFoldDB; Q06442; -.
DR   SMR; Q06442; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..359
FT                   /note="Protein Wnt-5a"
FT                   /id="PRO_0000041432"
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;  40117 MW;  533FFB0414DAAA14 CRC64;
     MATTHLTAAL ALLCALLQVD IEASSWWSLA MNPVQIPEAY IVGAQPLCSQ LPGLSPGQKK
     LCQLYQDHMP YIGEGAKTGI KECQYQFRHR RWNCSTVDNA SVFGRVMQIG SRETAFTYSI
     SAAGVVNAVS RACREGELST CGCSRAARPK DLQRDWLWGG CGDNLEYGYR FAKEFVDARE
     REKIHTKGSY ESSRTLMNIH NNEAGRRTVY NLADAACKCH GVSGSCSLKT CWLQLADFRK
     VGDFLKEKYD SAASMRLNAR GKLVQVNSRF NPPTTNDLVY VDTSPDYCVR NESTGSLGTQ
     GRLCNKTSEG MDGCELMCCG RGYDQFKTVQ TERCHCKFHW CCYVKCKKCT EIVDQFVCK