WN10B_DANRE
ID WN10B_DANRE Reviewed; 427 AA.
AC Q801F7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein Wnt-10b;
DE Flags: Precursor;
GN Name=wnt10b {ECO:0000312|ZFIN:ZDB-GENE-980526-524};
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] {ECO:0000305, ECO:0000312|EMBL:AAO24132.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:12591239};
RX PubMed=12591239; DOI=10.1016/s0012-1606(02)00044-1;
RA Lekven A.C., Buckles G.R., Kostakis N., Moon R.T.;
RT "Wnt1 and wnt10b function redundantly at the zebrafish midbrain-hindbrain
RT boundary.";
RL Dev. Biol. 254:172-187(2003).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15366005; DOI=10.1002/dvdy.20133;
RA Riley B.B., Chiang M.-Y., Storch E.M., Heck R., Buckles G.R., Lekven A.C.;
RT "Rhombomere boundaries are Wnt signaling centers that regulate metameric
RT patterning in the zebrafish hindbrain.";
RL Dev. Dyn. 231:278-291(2004).
CC -!- FUNCTION: Member of the Wnt ligand gene family that encodes for
CC secreted proteins, which activate the Wnt signaling cascade. Involved
CC in neurogenesis. Performs a partially redundant function with wnt1 in
CC the formation of the midbrain-hindbrain boundary (MHB) organizer.
CC {ECO:0000269|PubMed:12591239}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:O00744}. Secreted
CC {ECO:0000250|UniProtKB:O00744}.
CC -!- TISSUE SPECIFICITY: In the embryo, expressed in the developing central
CC nervous system (CNS), with an expression pattern very similar to that
CC of wnt1. {ECO:0000269|PubMed:12591239, ECO:0000269|PubMed:15366005}.
CC -!- DEVELOPMENTAL STAGE: First detected at around 8 hours post-
CC fertilization (hpf) within the prospective midbrain-hindbrain boundary
CC (MHB). By 10 hpf, expressed in two stripes that converge at the dorsal
CC midline. During somitogenesis, this expression domain extends to the
CC prospective epiphysis and the dorsal midline of the hindbrain; unlike
CC wnt1, wnt10b is detected in the prospective cerebellum. The hindbrain
CC domain bifurcates along the midline to form two dorsolateral columns
CC with transverse bands of up-regulation at rhombomere boundaries; these
CC are refined into stripes which are maintained at least until at least
CC 48 hpf. At 30 hpf, expressed in the epiphysis, the dorsal midline of
CC the optic tectum, the anterior half of the MHB constriction and in the
CC hindbrain walls. {ECO:0000269|PubMed:12591239,
CC ECO:0000269|PubMed:15366005}.
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:0000255}.
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DR EMBL; AY182171; AAO24132.1; -; mRNA.
DR RefSeq; NP_835737.1; NM_178219.2.
DR AlphaFoldDB; Q801F7; -.
DR SMR; Q801F7; -.
DR STRING; 7955.ENSDARP00000059973; -.
DR PaxDb; Q801F7; -.
DR GeneID; 30308; -.
DR KEGG; dre:30308; -.
DR CTD; 7480; -.
DR ZFIN; ZDB-GENE-980526-524; wnt10b.
DR eggNOG; KOG3913; Eukaryota.
DR InParanoid; Q801F7; -.
DR OrthoDB; 1241694at2759; -.
DR PhylomeDB; Q801F7; -.
DR Reactome; R-DRE-3238698; WNT ligand biogenesis and trafficking.
DR PRO; PR:Q801F7; -.
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:0030917; P:midbrain-hindbrain boundary development; IGI:ZFIN.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 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..427
FT /note="Protein Wnt-10b"
FT /evidence="ECO:0000255"
FT /id="PRO_0000250604"
FT LIPID 279
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 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..94
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 136..144
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 146..225
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 273..287
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 275..282
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 356..387
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 372..382
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 386..426
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 402..417
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 404..414
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 409..410
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 427 AA; 47407 MW; 6C7D2F1D58E3211E CRC64;
MELPHRQCLG RVLIVTAALL SPAFTVLGND ILGLKVAGEP VLTPNAVCLR LAGLTKKQMR
LCVRSPDVTA SALQGIQVAI HECQHQLRDQ RWNCSSLENH GKLPHQSAIL NRGFRESAFS
LSLLAAGVVH SVASACSLGK LRGCGCEAKR RLDDDKIRLK LTQLQLQTFQ RSGVSLAGAG
ENTPELSSLH GSLPANLHSS HPMSLLKPLP DEVTMLQDTW EWGGCSHDIR FGVRFSRDWL
DSRGSPRDIH ARTRIHNNRV GRQVVTDNMR RKCKCHGTSG SCQFKTCWYV SPEFRLVGSL
LREKFLTAIF INSQNKNNGV FNSRTGGSTG SDPLRGQRRR SISRELVYFE KSPDFCDREP
AVDSLGTQGR ICNKSSPGMD GCGSLCCGRG HNILKQARSE RCHCRFHWCC YVLCEECKVT
EWVNVCK
