WNT1_DANRE
ID WNT1_DANRE Reviewed; 370 AA.
AC P24257;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein Wnt-1;
DE Flags: Precursor;
GN Name=wnt1; Synonyms=int-1, wnt-1;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=2009859; DOI=10.1002/j.1460-2075.1991.tb08012.x;
RA Molven A., Njolstad P.R., Fjose A.;
RT "Genomic structure and restricted neural expression of the zebrafish wnt-1
RT (int-1) gene.";
RL EMBO J. 10:799-807(1991).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [3]
RP FUNCTION, 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).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15659486; DOI=10.1242/dev.01616;
RA Amoyel M., Cheng Y.-C., Jiang Y.-J., Wilkinson D.G.;
RT "Wnt1 regulates neurogenesis and mediates lateral inhibition of boundary
RT cell specification in the zebrafish hindbrain.";
RL Development 132:775-785(2005).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Acts in the canonical Wnt signaling pathway by
CC promoting beta-catenin-dependent transcriptional activation (By
CC similarity). Involved in neurogenesis. Performs a partially redundant
CC function with wnt10b in the formation of the midbrain-hindbrain
CC boundary (MHB) organizer. In the hindbrain, mediates lateral inhibition
CC of boundary cell specification, probably via up-regulation of proneural
CC and Delta gene expression in non-boundary cells; localized expression
CC of wnt1 in boundary cells is maintained via rfng-mediated modulation of
CC Notch activity. {ECO:0000250|UniProtKB:P04628,
CC ECO:0000269|PubMed:12591239, ECO:0000269|PubMed:15366005,
CC ECO:0000269|PubMed:15659486}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P04628}. Secreted
CC {ECO:0000250|UniProtKB:P04628}.
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 wnt10b. During somitogenesis, expressed strongly in hindbrain
CC boundary and roof plate cells. {ECO:0000269|PubMed:12591239,
CC ECO:0000269|PubMed:15659486, ECO:0000269|PubMed:2009859}.
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 wnt10b, wnt1 is not detected in the prospective cerebellum. The
CC hindbrain domain bifurcates along the midline to form two dorsolateral
CC columns with transverse bands of up-regulation at rhombomere
CC boundaries; these are refined into stripes which are maintained at
CC least until at least 48 hpf. At 30 hpf, expressed in the epiphysis, the
CC dorsal midline of the optic tectum, the anterior half of the MHB
CC constriction and in the hindbrain walls. Not detected in adults.
CC {ECO:0000269|PubMed:12591239, ECO:0000269|PubMed:15366005,
CC ECO:0000269|PubMed:2009859}.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors. Palmitoleoylation is necessary for proper trafficking to
CC cell surface (By similarity). Depalmitoleoylated by NOTUM, leading to
CC inhibit Wnt signaling pathway (By similarity).
CC {ECO:0000250|UniProtKB:P56704, ECO:0000250|UniProtKB:Q91029}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown results in broadening of
CC hindbrain boundary marker expression. {ECO:0000269|PubMed:15659486}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; X58880; CAA41687.1; -; Genomic_DNA.
DR EMBL; X58881; CAA41687.1; JOINED; Genomic_DNA.
DR EMBL; X58882; CAA41687.1; JOINED; Genomic_DNA.
DR EMBL; X58883; CAA41687.1; JOINED; Genomic_DNA.
DR PIR; S15013; S15013.
DR RefSeq; NP_001188327.1; NM_001201398.1.
DR AlphaFoldDB; P24257; -.
DR SMR; P24257; -.
DR STRING; 7955.ENSDARP00000110057; -.
DR PaxDb; P24257; -.
DR Ensembl; ENSDART00000077931; ENSDARP00000072397; ENSDARG00000055554.
DR GeneID; 30128; -.
DR KEGG; dre:30128; -.
DR CTD; 7471; -.
DR ZFIN; ZDB-GENE-980526-526; wnt1.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000160329; -.
DR HOGENOM; CLU_033039_1_1_1; -.
DR InParanoid; P24257; -.
DR PhylomeDB; P24257; -.
DR TreeFam; TF105310; -.
DR Reactome; R-DRE-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-DRE-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-DRE-4086400; PCP/CE pathway.
DR Reactome; R-DRE-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR PRO; PR:P24257; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000055554; Expressed in midbrain-hindbrain boundary and 57 other tissues.
DR ExpressionAtlas; P24257; baseline.
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:0035284; P:brain segmentation; IMP:ZFIN.
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:0021587; P:cerebellum morphogenesis; IMP:ZFIN.
DR GO; GO:0021592; P:fourth ventricle development; IMP:ZFIN.
DR GO; GO:0030902; P:hindbrain development; IMP:ZFIN.
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; IPR009139; Wnt1.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01841; WNT1PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Lipoprotein; Neurogenesis;
KW Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..370
FT /note="Protein Wnt-1"
FT /id="PRO_0000041408"
FT REGION 261..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 223
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:Q91029"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..103
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 142..150
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 152..169
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 299..330
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 315..325
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 329..369
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 345..360
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 347..357
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 352..353
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 370 AA; 41011 MW; F2AB0A82DB031D3E CRC64;
MRVLALLLAV KAACVLLVSS LTGTGAVNNS GRWWGIVNVA SSGNLLTNSK NVQLVLDPSL
ALLSRRQRKL IRQNPGILHA IAAGLHTAIK ECKWQFRNRR WNCPTTHSPN VFGKIVNRGC
RETAFVFAIT SAGVTHAVAR SCSEGAIESC TCDYRRRGPG GPDWHWGGCS DNVEFGRMFG
REFVDSSERG RDLRYLTNLH NNEAGRMTVA SEMQQECKCH GMSGSCTVRT CWMRLPSFRL
VGDYLKDRFD GASRVVYANK GSNRASHRAD PRHLEPENPA HKLPSSRDLV YFEKSPNFCS
YNGKTGTHGT SGRTCNSSSP ALDGCELLCC GRGYKTRMEQ VTERCHCTFH WCCHVSCLNC
TSTQTVHQCL
