ID   WN10A_DANRE             Reviewed;         442 AA.
AC   P43446;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Protein Wnt-10a;
DE   Flags: Precursor;
GN   Name=wnt10a; Synonyms=wnt-10a;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=8330668; DOI=10.1006/dbio.1993.1172;
RA   Kelly G.M., Lai C.-J., Moon R.T.;
RT   "Expression of wnt10a in the central nervous system of developing
RT   zebrafish.";
RL   Dev. Biol. 158:113-121(1993).
RN   [2]
RP   FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   GLY-248 AND THR-382.
RX   PubMed=29178643; DOI=10.1002/mgg3.332;
RA   Yuan Q., Zhao M., Tandon B., Maili L., Liu X., Zhang A., Baugh E.H.,
RA   Tran T., Silva R.M., Hecht J.T., Swindell E.C., Wagner D.S., Letra A.;
RT   "Role of WNT10A in failure of tooth development in humans and zebrafish.";
RL   Mol. Genet. Genomic Med. 5:730-741(2017).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors (Probable). Required for normal tooth
CC       development (PubMed:29178643). Regulates the expression of genes
CC       involved in tooth development (PubMed:29178643).
CC       {ECO:0000269|PubMed:29178643, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q9GZT5}. Secreted
CC       {ECO:0000250|UniProtKB:Q9GZT5}.
CC   -!- DEVELOPMENTAL STAGE: Detected in embryos (at protein level)
CC       (PubMed:29178643). First detected during the segmentation period of
CC       embryogenesis (PubMed:8330668). Detected in the developing brain and
CC       spinal cord (PubMed:8330668). Detected at constant levels in embryonic
CC       head throughout embryonic development, from 18 hpf to 5 dpf
CC       (PubMed:29178643). Widely expressed in embryos at 56 hpf
CC       (PubMed:29178643). {ECO:0000269|PubMed:29178643,
CC       ECO:0000269|PubMed:8330668}.
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   -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes arrest
CC       of tooth development. Otherwise, mutant embryos appear grossly normal,
CC       excepting some cartilage abnormalities. {ECO:0000269|PubMed:29178643}.
CC   -!- MISCELLANEOUS: Wnt10a overexpression in embryos results in loss of
CC       anterior neural identity, causing a phenotype with small or no eyes.
CC       {ECO:0000269|PubMed:29178643}.
CC   -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR   EMBL; U02544; AAA03431.1; -; mRNA.
DR   PIR; I50110; I50110.
DR   AlphaFoldDB; P43446; -.
DR   SMR; P43446; -.
DR   STRING; 7955.ENSDARP00000005680; -.
DR   PaxDb; P43446; -.
DR   ZFIN; ZDB-GENE-990415-278; wnt10a.
DR   eggNOG; KOG3913; Eukaryota.
DR   InParanoid; P43446; -.
DR   PhylomeDB; P43446; -.
DR   Reactome; R-DRE-3238698; WNT ligand biogenesis and trafficking.
DR   PRO; PR:P43446; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0042476; P:odontogenesis; IMP:ZFIN.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR013302; Wnt10.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01893; WNT10PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..442
FT                   /note="Protein Wnt-10a"
FT                   /id="PRO_0000041462"
FT   LIPID           303
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        133..144
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        186..194
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        196..249
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        297..311
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        299..306
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        371..402
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        387..397
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        401..441
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        417..432
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        419..429
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        424..425
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   MUTAGEN         248
FT                   /note="G->S: Strongly decreases the ability to induce the
FT                   expression of genes involved in tooth development."
FT                   /evidence="ECO:0000269|PubMed:29178643"
FT   MUTAGEN         382
FT                   /note="T->I: No significant effect on the ability to induce
FT                   the expression of genes involved in tooth development."
FT                   /evidence="ECO:0000269|PubMed:29178643"
SQ   SEQUENCE   442 AA;  50047 MW;  B764B8D344B22E57 CRC64;
     MSSHDISWHS PASVYFSSDL DVKRIAGKLR GCWTDLLLRQ ESCCERVLQK SSSSMDYFLF
     RLFCSLALAS LLVQRADSNE ILGLKIPFDP ILNANTVCLT LPGLTKKQLD VCMRNPDVTA
     SAIQGIQIAI HECQHQFRGH RWNCSSLETR NKIPYESVVF SRGFRESAFA YAIAAAGVVH
     AVSNACAMGK LKACGCDEKR RGDEEALRIK LNRLQLEAIN RGKGMVHGVM EHFPAEALGP
     QDSWEWGGCS PNVEYGERFS KDFLDSRETY RDIHSRMRLH NNRVGRQVVV DHMRRKCKCH
     GTSGSCQLKT CWQVTPEFRT VGSLLKERLN VATLIKAHNR NTGQVENAHH THRRRANIND
     LVYFEKSPDF CERDLGSDSA GTQGRICNKT SQGMDNCESL CCGRGHNILQ QTRSERCNCK
     FHWCCYVVCE ECRITEWVSV CK