WNT5B_DANRE
ID WNT5B_DANRE Reviewed; 363 AA.
AC Q92050; A5WVR7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein Wnt-5b;
DE Flags: Precursor;
GN Name=wnt5b; Synonyms=wnt-5, wnt5, wnt5a; ORFNames=si:ch73-211c7.1;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RA Blader P., Straehle U., Ingham P.W.;
RT "Three Wnt genes expressed in a wide variety of tissues during development
RT of the zebrafish, Danio rerio: developmental and evolutionary
RT perspectives.";
RL Dev. Genes Evol. 206:3-13(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=22406073; DOI=10.1016/j.bbamcr.2012.02.013;
RA Lou Q., He J., Hu L., Yin Z.;
RT "Role of lbx2 in the noncanonical Wnt signaling pathway for convergence and
RT extension movements and hypaxial myogenesis in zebrafish.";
RL Biochim. Biophys. Acta 1823:1024-1032(2012).
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. Regulates
CC convergent extension movements and hypaxial myogenesis during
CC gastrulation via activation of non-canonical Wnt signaling
CC (PubMed:22406073). {ECO:0000250|UniProtKB:P22725,
CC ECO:0000269|PubMed:22406073}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P41221}. Secreted
CC {ECO:0000250|UniProtKB:P41221}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically (Ref.1).
CC Expressed in the germ ring at the blastoderm margin during the shield
CC stage of gastrulation, expression is higher dorsally than ventrally
CC (PubMed:22406073). Expressed at the posterior dorsal midline at the
CC four-somite stage and in the pectoral fin bud 48 hours post-
CC fertilization (PubMed:22406073). Zygotic expression begins during
CC somitogenesis and is confined to the mesenchyme of the developing
CC tailbud, the posterior 4-5 somites and the ventrolateral mesenchyme of
CC the head (Ref.1). In later stages, expressed in the pharyngeal arch
CC mesenchyme and pectoral finbuds (Ref.1). Not detected in mature
CC chondrocytes (Ref.1). {ECO:0000269|PubMed:22406073, ECO:0000269|Ref.1}.
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 results in convergent
CC extension movement defects during gastrulation and an absence of myod1
CC expression in the majority of hypaxial muscle precursor cells.
CC {ECO:0000269|PubMed:22406073}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; U51268; AAA96519.1; -; mRNA.
DR EMBL; CT025936; CAN88522.1; -; Genomic_DNA.
DR RefSeq; NP_571012.1; NM_130937.1.
DR RefSeq; XP_005164595.1; XM_005164538.3.
DR RefSeq; XP_005164596.1; XM_005164539.3.
DR AlphaFoldDB; Q92050; -.
DR SMR; Q92050; -.
DR BioGRID; 78343; 6.
DR STRING; 7955.ENSDARP00000106303; -.
DR PaxDb; Q92050; -.
DR Ensembl; ENSDART00000162065; ENSDARP00000134193; ENSDARG00000102464.
DR Ensembl; ENSDART00000165181; ENSDARP00000131042; ENSDARG00000102464.
DR Ensembl; ENSDART00000186829; ENSDARP00000152177; ENSDARG00000102464.
DR GeneID; 30105; -.
DR KEGG; dre:30105; -.
DR CTD; 81029; -.
DR ZFIN; ZDB-GENE-980526-87; wnt5b.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000157617; -.
DR HOGENOM; CLU_033039_0_1_1; -.
DR InParanoid; Q92050; -.
DR OMA; EHARMLM; -.
DR PhylomeDB; Q92050; -.
DR Reactome; R-DRE-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-DRE-4086400; PCP/CE pathway.
DR PRO; PR:Q92050; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000102464; Expressed in pharyngeal gill and 39 other tissues.
DR ExpressionAtlas; Q92050; 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:0005102; F:signaling receptor binding; IPI:ZFIN.
DR GO; GO:0001667; P:ameboidal-type cell migration; IMP:ZFIN.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0060536; P:cartilage morphogenesis; IMP:ZFIN.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:ZFIN.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:ZFIN.
DR GO; GO:0060026; P:convergent extension; IGI:ZFIN.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IMP:ZFIN.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:ZFIN.
DR GO; GO:0060030; P:dorsal convergence; IMP:ZFIN.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:ZFIN.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:ZFIN.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:ZFIN.
DR GO; GO:0001958; P:endochondral ossification; IMP:ZFIN.
DR GO; GO:0031018; P:endocrine pancreas development; IMP:ZFIN.
DR GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR GO; GO:0001946; P:lymphangiogenesis; IMP:ZFIN.
DR GO; GO:0021555; P:midbrain-hindbrain boundary morphogenesis; IMP:ZFIN.
DR GO; GO:0042692; P:muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0048884; P:neuromast development; IMP:ZFIN.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IMP:ZFIN.
DR GO; GO:0048840; P:otolith development; IMP:ZFIN.
DR GO; GO:1904105; P:positive regulation of convergent extension involved in gastrulation; IMP:UniProtKB.
DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:ZFIN.
DR GO; GO:0008591; P:regulation of Wnt signaling pathway, calcium modulating pathway; IMP:ZFIN.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:ZFIN.
DR GO; GO:0001501; P:skeletal system development; IMP:ZFIN.
DR GO; GO:0061053; P:somite development; IGI:ZFIN.
DR GO; GO:0002574; P:thrombocyte differentiation; IMP:ZFIN.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:ZFIN.
DR GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; IDA:ZFIN.
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; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..363
FT /note="Protein Wnt-5b"
FT /id="PRO_0000041438"
FT LIPID 227
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..98
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 137..145
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 147..165
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 221..235
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 223..230
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 292..323
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 308..318
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 322..362
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 338..353
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 340..350
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 345..346
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 363 AA; 41137 MW; 86AC06DE20DCBBA3 CRC64;
MDVRMNQGHL LLAVTLIVCN SQLLVVANSW WSLAMNPIQR PEMYIIGAQP LCSQLTGLSQ
GQRKLCQLYQ DHMVYIGEGA KTGIKECQYQ FRQRRWNCST VDNTSVFGRV MHIGSRETAF
TYAVSAAGVV NAVSRACREG ELSTCGCSRA ARPRDLPRDW LWGGCGDNVN YGYRFAREFV
DAREREKNYP RGSVEHARTL MNLQNNEAGR MAVYNLANVA CKCHGVSGSC SLKTCWLQLA
DFRRVGEFLK EKYDSAAAMR INRRGKLELV NNRFNPPTGE DLVYIDPSPD YCLRNETTGS
LGTQGRLCNK TSEGMDGCEL MCCGRGYDQF KTYKHERCHC KFHWCCYVKC KRCTSLVDQF
VCK
