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UniProtKB - O00755 (WNT7A_HUMAN)

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Protein

Protein Wnt-7a

Gene

WNT7A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development (PubMed:16826533). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes. Required for normal neural stem cell proliferation in the hippocampus dentate gyrus. Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation. Promotes formation of synapses via its interaction with FZD5 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • cytokine activity Source: BHF-UCL
  • frizzled binding Source: GO_Central
  • receptor ligand activity Source: BHF-UCL
  • signaling receptor binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • angiogenesis Source: Ensembl
  • asymmetric protein localization involved in cell fate determination Source: Ensembl
  • axonogenesis Source: ParkinsonsUK-UCL
  • canonical Wnt signaling pathway Source: BHF-UCL
  • cartilage condensation Source: AgBase
  • cell fate commitment Source: GO_Central
  • cell proliferation in forebrain Source: BHF-UCL
  • cellular response to transforming growth factor beta stimulus Source: UniProtKB
  • central nervous system vasculogenesis Source: Ensembl
  • cerebellar granule cell differentiation Source: Ensembl
  • chondrocyte differentiation Source: AgBase
  • dendritic spine morphogenesis Source: ParkinsonsUK-UCL
  • dorsal/ventral pattern formation Source: Ensembl
  • embryonic axis specification Source: BHF-UCL
  • embryonic digit morphogenesis Source: BHF-UCL
  • embryonic forelimb morphogenesis Source: BHF-UCL
  • embryonic hindlimb morphogenesis Source: BHF-UCL
  • establishment of cell polarity Source: Ensembl
  • excitatory synapse assembly Source: ParkinsonsUK-UCL
  • lens fiber cell development Source: BHF-UCL
  • negative regulation of apoptotic process Source: Ensembl
  • negative regulation of neurogenesis Source: BHF-UCL
  • neurotransmitter secretion Source: Ensembl
  • non-canonical Wnt signaling pathway Source: Ensembl
  • oviduct development Source: Ensembl
  • positive regulation of canonical Wnt signaling pathway Source: ARUK-UCL
  • positive regulation of cellular protein metabolic process Source: ARUK-UCL
  • positive regulation of endothelial cell migration Source: Ensembl
  • positive regulation of epithelial cell proliferation involved in wound healing Source: BHF-UCL
  • positive regulation of excitatory postsynaptic potential Source: ParkinsonsUK-UCL
  • positive regulation of excitatory synapse assembly Source: ParkinsonsUK-UCL
  • positive regulation of JNK cascade Source: Ensembl
  • positive regulation of protein localization to presynapse Source: ParkinsonsUK-UCL
  • positive regulation of synapse assembly Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • positive regulation of transcription by RNA polymerase II Source: BHF-UCL
  • postsynapse assembly Source: ParkinsonsUK-UCL
  • presynapse assembly Source: ParkinsonsUK-UCL
  • regulation of axon diameter Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to estrogen Source: Ensembl
  • secondary palate development Source: BHF-UCL
  • sex differentiation Source: ProtInc
  • skeletal muscle satellite cell activation Source: Ensembl
  • skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration Source: Ensembl
  • somatic stem cell division Source: Ensembl
  • somatic stem cell population maintenance Source: Ensembl
  • stem cell development Source: BHF-UCL
  • synaptic vesicle recycling Source: ParkinsonsUK-UCL
  • uterus morphogenesis Source: Ensembl
  • Wnt signaling pathway Source: Reactome
  • Wnt signaling pathway involved in wound healing, spreading of epidermal cells Source: BHF-UCL
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDevelopmental protein
Biological processWnt signaling pathway

Enzyme and pathway databases

ReactomeiR-HSA-3238698 WNT ligand biogenesis and trafficking
R-HSA-373080 Class B/2 (Secretin family receptors)
SignaLinkiO00755
SIGNORiO00755

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Wnt-7a
Gene namesi
Name:WNT7A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000154764.5
HGNCiHGNC:12786 WNT7A
MIMi601570 gene
neXtProtiNX_O00755

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Limb pelvis hypoplasia aplasia syndrome (LPHAS)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome of severe deficiency of the extremities due to hypo- or aplasia of one or more long bones of one or more limbs. Pelvic manifestations include hip dislocation, hypoplastic iliac bone and aplastic pubic bones. Thoracic deformity, unusual facies and genitourinary anomalies can be present.
See also OMIM:276820
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06576572E → K in LPHAS. 1 PublicationCorresponds to variant dbSNP:rs397514666EnsemblClinVar.1
Natural variantiVAR_077340102R → W in LPHAS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs879255548EnsemblClinVar.1
Natural variantiVAR_064480222R → W in LPHAS. 1 PublicationCorresponds to variant dbSNP:rs397514643EnsemblClinVar.1
Natural variantiVAR_030674292R → C in LPHAS; results in a loss of function mutation with some residual activity. 2 PublicationsCorresponds to variant dbSNP:rs104893835EnsemblClinVar.1
Fuhrmann syndrome (FUHRS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionDistinct limb-malformation disorder characterized also by various degrees of limb aplasia/hypoplasia and joint dysplasia.
See also OMIM:228930
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030673109A → T in FUHRS; retains activity that is significant but not comparable to wild-type activity. 1 PublicationCorresponds to variant dbSNP:rs104893832EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi7476
MalaCardsiWNT7A
MIMi228930 phenotype
276820 phenotype
OpenTargetsiENSG00000154764
Orphaneti2854 Fuhrmann syndrome
2879 Phocomelia, Schinzel type
PharmGKBiPA37387

Polymorphism and mutation databases

BioMutaiWNT7A

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000004144232 – 349Protein Wnt-7aAdd BLAST318

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi73 ↔ 84By similarity
Glycosylationi83N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi123 ↔ 131By similarity
Glycosylationi127N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi133 ↔ 152By similarity
Disulfide bondi200 ↔ 214By similarity
Disulfide bondi202 ↔ 209By similarity
Lipidationi206O-palmitoleoyl serine; by PORCNBy similarity1
Disulfide bondi294 ↔ 309By similarity
Glycosylationi295N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi324 ↔ 339By similarity
Disulfide bondi326 ↔ 336By similarity
Disulfide bondi331 ↔ 332By similarity

Post-translational modificationi

Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein

Proteomic databases

MaxQBiO00755
PaxDbiO00755
PeptideAtlasiO00755
PRIDEiO00755
ProteomicsDBi48019
TopDownProteomicsiO00755

PTM databases

iPTMnetiO00755
PhosphoSitePlusiO00755

Expressioni

Tissue specificityi

Expression is restricted to placenta, kidney, testis, uterus, fetal lung, and fetal and adult brain.

Gene expression databases

BgeeiENSG00000154764
CleanExiHS_WNT7A
GenevisibleiO00755 HS

Organism-specific databases

HPAiCAB025894
HPA015719

Interactioni

Subunit structurei

Forms a soluble 1:1 complex with AFM; this prevents oligomerization and is required for prolonged biological activity (PubMed:26902720). The complex with AFM may represent the physiological form in body fluids (PubMed:26902720). Interacts with FZD5. Interacts with PORCN (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
WIF1Q9Y5W53EBI-727198,EBI-3922719

GO - Molecular functioni

  • cytokine activity Source: BHF-UCL
  • frizzled binding Source: GO_Central
  • receptor ligand activity Source: BHF-UCL
  • signaling receptor binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi113313, 31 interactors
DIPiDIP-61511N
IntActiO00755, 3 interactors
MINTiO00755
STRINGi9606.ENSP00000285018

Structurei

3D structure databases

ProteinModelPortaliO00755
SMRiO00755
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Wnt family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3913 Eukaryota
ENOG410XQZ1 LUCA
GeneTreeiENSGT00760000118943
HOGENOMiHOG000039528
HOVERGENiHBG001595
InParanoidiO00755
KOiK00572
OMAiYIDKSPN
OrthoDBiEOG091G0OFF
PhylomeDBiO00755
TreeFamiTF105310

Family and domain databases

InterProiView protein in InterPro
IPR005817 Wnt
IPR013300 Wnt7
IPR018161 Wnt_CS
PANTHERiPTHR12027 PTHR12027, 1 hit
PfamiView protein in Pfam
PF00110 wnt, 1 hit
PRINTSiPR01891 WNT7PROTEIN
PR01349 WNTPROTEIN
SMARTiView protein in SMART
SM00097 WNT1, 1 hit
PROSITEiView protein in PROSITE
PS00246 WNT1, 1 hit

Sequencei

Sequence statusi: Complete.

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

O00755-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRKARRCLG HLFLSLGMVY LRIGGFSSVV ALGASIICNK IPGLAPRQRA 
        60         70         80         90        100
ICQSRPDAII VIGEGSQMGL DECQFQFRNG RWNCSALGER TVFGKELKVG 
       110        120        130        140        150
SREAAFTYAI IAAGVAHAIT AACTQGNLSD CGCDKEKQGQ YHRDEGWKWG 
       160        170        180        190        200
GCSADIRYGI GFAKVFVDAR EIKQNARTLM NLHNNEAGRK ILEENMKLEC 
       210        220        230        240        250
KCHGVSGSCT TKTCWTTLPQ FRELGYVLKD KYNEAVHVEP VRASRNKRPT 
       260        270        280        290        300
FLKIKKPLSY RKPMDTDLVY IEKSPNYCEE DPVTGSVGTQ GRACNKTAPQ 
       310        320        330        340 
ASGCDLMCCG RGYNTHQYAR VWQCNCKFHW CCYVKCNTCS ERTEMYTCK
Length:349
Mass (Da):39,005
Last modified:April 17, 2007 - v2
Checksum:i259EF506CFCD7AB0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6R → L in AAC51319 (PubMed:9161407).Curated1
Sequence conflicti14L → F in BAA82509 (PubMed:8893824).Curated1
Sequence conflicti20Y → C in AAC51319 (PubMed:9161407).Curated1
Sequence conflicti35S → T in AAC51319 (PubMed:9161407).Curated1
Sequence conflicti103 – 104EA → DG in AAC51319 (PubMed:9161407).Curated2
Sequence conflicti125Q → H in AAC51319 (PubMed:9161407).Curated1
Sequence conflicti280E → G no nucleotide entry (PubMed:8168088).Curated1
Sequence conflicti329H → Q in BAA82509 (PubMed:8893824).Curated1
Sequence conflicti338T → K in BAA82509 (PubMed:8893824).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06576572E → K in LPHAS. 1 PublicationCorresponds to variant dbSNP:rs397514666EnsemblClinVar.1
Natural variantiVAR_077340102R → W in LPHAS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs879255548EnsemblClinVar.1
Natural variantiVAR_030673109A → T in FUHRS; retains activity that is significant but not comparable to wild-type activity. 1 PublicationCorresponds to variant dbSNP:rs104893832EnsemblClinVar.1
Natural variantiVAR_064480222R → W in LPHAS. 1 PublicationCorresponds to variant dbSNP:rs397514643EnsemblClinVar.1
Natural variantiVAR_030674292R → C in LPHAS; results in a loss of function mutation with some residual activity. 2 PublicationsCorresponds to variant dbSNP:rs104893835EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53476 mRNA Translation: AAC51319.1
D83175 mRNA Translation: BAA82509.1
CH471055 Genomic DNA Translation: EAW64173.1
BC008811 mRNA Translation: AAH08811.1
CCDSiCCDS2616.1
RefSeqiNP_004616.2, NM_004625.3
UniGeneiHs.72290

Genome annotation databases

EnsembliENST00000285018; ENSP00000285018; ENSG00000154764
GeneIDi7476
KEGGihsa:7476
UCSCiuc003bye.2 human

Similar proteinsi

Entry informationi

Entry nameiWNT7A_HUMAN
AccessioniPrimary (citable) accession number: O00755
Secondary accession number(s): Q96H90, Q9Y560
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 17, 2007
Last modified: July 18, 2018
This is version 164 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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