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Protein

Wnt inhibitor of Dorsal protein

Gene

wntD

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds as a ligand to a family of frizzled seven-transmembrane receptors and acts through a cascade of genes on the nucleus.Curated

GO - Molecular functioni

  1. frizzled binding Source: UniProtKB

GO - Biological processi

  1. cell fate commitment Source: GO_Central
  2. defense response to Gram-positive bacterium Source: FlyBase
  3. neuron differentiation Source: GO_Central
  4. pole cell migration Source: FlyBase
  5. regulation of embryonic development Source: FlyBase
  6. ventral furrow formation Source: FlyBase
  7. Wnt signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_314967. WNT ligand biogenesis and trafficking.
REACT_322963. TCF dependent signaling in response to WNT.
REACT_343579. disassembly of the destruction complex and recruitment of AXIN to the membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Wnt inhibitor of Dorsal protein
Alternative name(s):
Protein Wnt-8
dWnt-8
Gene namesi
Name:wntD
Synonyms:Wnt8
ORF Names:CG8458
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0038134. wntD.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: FlyBase
  2. extracellular space Source: GO_Central
  3. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 309293Wnt inhibitor of Dorsal proteinPRO_0000041480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 621 Publication
Disulfide bondi102 ↔ 1101 Publication
Disulfide bondi112 ↔ 1211 Publication
Disulfide bondi162 ↔ 1791 Publication
Disulfide bondi164 ↔ 1741 Publication
Disulfide bondi232 ↔ 269By similarity
Disulfide bondi248 ↔ 262By similarity
Disulfide bondi266 ↔ 308By similarity
Disulfide bondi284 ↔ 299By similarity
Disulfide bondi286 ↔ 296By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Gene expression databases

BgeeiQ9VFX1.

Interactioni

Protein-protein interaction databases

BioGridi66717. 8 interactions.
IntActiQ9VFX1. 2 interactions.
MINTiMINT-767524.
STRINGi7227.FBpp0082243.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 5419Combined sources
Beta strandi58 – 603Combined sources
Helixi64 – 729Combined sources
Helixi81 – 10323Combined sources
Helixi125 – 13511Combined sources
Helixi141 – 15515Combined sources
Beta strandi158 – 1669Combined sources
Turni171 – 1733Combined sources
Beta strandi177 – 1837Combined sources
Helixi186 – 19813Combined sources
Beta strandi208 – 2103Combined sources
Turni214 – 2163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KRRX-ray2.12A31-240[»]
ProteinModelPortaliQ9VFX1.
SMRiQ9VFX1. Positions 33-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Wnt family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG258743.
GeneTreeiENSGT00690000101857.
InParanoidiQ9VFX1.
KOiK00714.
OMAiERRCNCK.
OrthoDBiEOG7SFHZX.
PhylomeDBiQ9VFX1.

Family and domain databases

InterProiIPR005817. Wnt.
IPR026540. WntD.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PTHR12027:SF79. PTHR12027:SF79. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01349. WNTPROTEIN.
SMARTiSM00097. WNT1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9VFX1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIFAITFFMG ITSTLAAVLE PMSYYQYTQF QAPLSWEDIT GKGLKQALDS
60 70 80 90 100
CQQSFQWQRW NCPSQDFVQK NSKPEENSPN REDVYVAAIS MAAIVHTLTK
110 120 130 140 150
DCANGVIAGC GCTENALNVP CAHEPTKALE QYEKHFGSGS GAIGHNRRVV
160 170 180 190 200
GALLQRSLEQ ECRCKQPGAV QGECQEEECV AVLKPFEAIA QDLLQMYDDA
210 220 230 240 250
IQLEGASSNL KIMWQNIPLD SLVFMQDSPN YCERDATGLW KGTRGRQCSK
260 270 280 290 300
DGSGSLEERL SCQQLCRVCG YRVRSQHVRT ERRCNCKLVW GFRLQCDVCV

QLERQYSCY
Length:309
Mass (Da):34,777
Last modified:March 1, 2001 - v2
Checksum:iBA6AC2F3198B4DAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF54924.2.
AY071538 mRNA. Translation: AAL49160.1.
RefSeqiNP_650272.1. NM_142015.2.
UniGeneiDm.5874.

Genome annotation databases

EnsemblMetazoaiFBtr0082775; FBpp0082243; FBgn0038134.
GeneIDi41633.
KEGGidme:Dmel_CG8458.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF54924.2.
AY071538 mRNA. Translation: AAL49160.1.
RefSeqiNP_650272.1. NM_142015.2.
UniGeneiDm.5874.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KRRX-ray2.12A31-240[»]
ProteinModelPortaliQ9VFX1.
SMRiQ9VFX1. Positions 33-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66717. 8 interactions.
IntActiQ9VFX1. 2 interactions.
MINTiMINT-767524.
STRINGi7227.FBpp0082243.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082775; FBpp0082243; FBgn0038134.
GeneIDi41633.
KEGGidme:Dmel_CG8458.

Organism-specific databases

CTDi41633.
FlyBaseiFBgn0038134. wntD.

Phylogenomic databases

eggNOGiNOG258743.
GeneTreeiENSGT00690000101857.
InParanoidiQ9VFX1.
KOiK00714.
OMAiERRCNCK.
OrthoDBiEOG7SFHZX.
PhylomeDBiQ9VFX1.

Enzyme and pathway databases

ReactomeiREACT_314967. WNT ligand biogenesis and trafficking.
REACT_322963. TCF dependent signaling in response to WNT.
REACT_343579. disassembly of the destruction complex and recruitment of AXIN to the membrane.

Miscellaneous databases

GenomeRNAii41633.
NextBioi824739.
PROiQ9VFX1.

Gene expression databases

BgeeiQ9VFX1.

Family and domain databases

InterProiIPR005817. Wnt.
IPR026540. WntD.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PTHR12027:SF79. PTHR12027:SF79. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01349. WNTPROTEIN.
SMARTiSM00097. WNT1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  4. "Wnt proteins are lipid-modified and can act as stem cell growth factors."
    Willert K., Brown J.D., Danenberg E., Duncan A.W., Weissman I.L., Reya T., Yates J.R. III, Nusse R.
    Nature 423:448-452(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PALMITOYLATION.
  5. "Lipid-independent secretion of a Drosophila Wnt protein."
    Ching W., Hang H.C., Nusse R.
    J. Biol. Chem. 283:17092-17098(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF PALMITOYLATION.
  6. "structural Studies of Wnts and identification of an LRP6 binding site."
    Chu M.L., Ahn V.E., Choi H.J., Daniels D.L., Nusse R., Weis W.I.
    Structure 21:1235-1242(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 31-240, DISULFIDE BONDS.

Entry informationi

Entry nameiWNT8_DROME
AccessioniPrimary (citable) accession number: Q9VFX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

In contrast to other members of the family, it is not lipidated.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.