WNT3A

Protein Wnt-3a is a protein that in humans is encoded by the WNT3A gene.[5][6]

WNT3A
Identifiers
Aliases	WNT3A, Wnt family member 3A
External IDs	OMIM: 606359 MGI: 98956 HomoloGene: 22528 GeneCards: WNT3A
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q42.13 Start 228,006,998 bp[1] End 228,061,271 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 B1.3|11 37.17 cM Start 59,248,033 bp[2] End 59,290,752 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein domain specific binding • receptor binding • co-receptor binding • GO:0005110 frizzled binding • GO:0001948 protein binding • GO:0001105 transcription coactivator activity • receptor ligand activity Cellular component • endocytic vesicle membrane • endoplasmic reticulum lumen • extracellular region • cell surface • extracellular exosome • Wnt-Frizzled-LRP5/6 complex • early endosome membrane • cell membrane • Golgi lumen • presynapse • extracellular • synapse • glutamatergic synapse Biological process • somitogenesis • cellular response to retinoic acid • haematopoiesis • positive regulation of protein phosphorylation • Wnt signaling pathway involved in forebrain neuroblast division • positive regulation of skeletal muscle tissue development • positive regulation of receptor internalization • axis elongation involved in somitogenesis • positive regulation of collateral sprouting in absence of injury • mammary gland development • platelet activation • heart looping • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process • positive regulation of protein localization to plasma membrane • cardiac muscle cell fate commitment • mesoderm development • cell proliferation in forebrain • positive regulation of mesodermal cell fate specification • negative regulation of fat cell differentiation • canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment • regulation of microtubule cytoskeleton organization • negative regulation of dopaminergic neuron differentiation • cell proliferation in midbrain • in utero embryonic development • negative regulation of axon extension involved in axon guidance • positive regulation of peptidyl-serine phosphorylation • positive regulation of transcription, DNA-templated • regulation of axonogenesis • positive regulation of B cell proliferation • post-anal tail morphogenesis • positive regulation of cardiac muscle cell differentiation • negative regulation of neuron projection development • paraxial mesodermal cell fate commitment • negative regulation of neurogenesis • positive regulation of protein tyrosine kinase activity • positive regulation of sequence-specific DNA binding transcription factor activity • extracellular matrix organization • positive regulation of neural precursor cell proliferation • synaptic vesicle recycling • osteoblast differentiation • skeletal muscle cell differentiation • COP9 signalosome assembly • dorsal/ventral neural tube patterning • positive regulation of protein binding • platelet aggregation • midbrain development • positive regulation of protein kinase activity • positive regulation of cell-cell adhesion mediated by cadherin • positive regulation of hepatocyte proliferation • neurogenesis • spinal cord association neuron differentiation • axonogenesis • positive regulation of cytokine production • positive regulation of dermatome development • somatic stem cell division • positive regulation of canonical Wnt signaling pathway involved in controlling type B pancreatic cell proliferation • axon guidance • multicellular organism development • cellular protein localization • determination of left/right symmetry • inner ear morphogenesis • positive regulation of cell proliferation • regulation of cell differentiation • hippocampus development • negative regulation of heart induction by canonical Wnt signaling pathway • positive regulation of transcription from RNA polymerase II promoter • anterior/posterior pattern specification • Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation • beta-catenin destruction complex disassembly • neuron differentiation • Wnt signaling pathway • positive regulation of canonical Wnt signaling pathway • positive regulation of gene expression • calcium ion transmembrane transport via low voltage-gated calcium channel • presynapse assembly • negative regulation of neuron death • positive regulation of core promoter binding • regulation of RNA biosynthetic process • regulation of receptor activity • cellular proliferation • canonical Wnt signaling pathway • secondary palate development • cell fate commitment • modulation of chemical synaptic transmission • regulation of synapse organization • postsynapse to nucleus signaling pathway • regulation of presynapse assembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	89780	22416
Ensembl	ENSG00000154342	ENSMUSG00000009900
UniProt	P56704	P27467
RefSeq (mRNA)	NM_033131	NM_009522
RefSeq (protein)	NP_149122	NP_033548
Location (UCSC)	Chr 1: 228.01 – 228.06 Mb	Chr 11: 59.25 – 59.29 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The WNT gene family consists of structurally related genes that encode secreted signaling proteins. These proteins have been implicated in oncogenesis, adipogenesis etc[7] and in several other developmental processes, including regulation of cell fate and patterning during embryogenesis. This gene is a member of the WNT gene family. It encodes a protein showing 96% amino acid identity to mouse Wnt3A protein, and 84% to human WNT3 protein, another WNT gene product. This gene is clustered with WNT14 gene, another family member, in chromosome 1q42 region.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000154342 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000009900 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Saitoh T, Hirai M, Katoh M (Jun 2001). "Molecular cloning and characterization of WNT3A and WNT14 clustered in human chromosome 1q42 region". Biochem Biophys Res Commun. 284 (5): 1168–75. doi:10.1006/bbrc.2001.5105. PMID 11414706.
6. "Entrez Gene: WNT3A wingless-type MMTV integration site family, member 3A".
7. Kennell, Jennifer A.; MacDougald, Ormond A. (24 June 2005). "Wnt Signaling Inhibits Adipogenesis through β-Catenin-dependent and -independent Mechanisms". Journal of Biological Chemistry. 280 (25): 24004–24010. doi:10.1074/jbc.M501080200. PMID 15849360.

Further reading

• Smolich BD, McMahon JA, McMahon AP, Papkoff J (1994). "Wnt family proteins are secreted and associated with the cell surface". Mol. Biol. Cell. 4 (12): 1267–75. doi:10.1091/mbc.4.12.1267. PMC 275763. PMID 8167409.
• Huguet EL, McMahon JA, McMahon AP, et al. (1994). "Differential expression of human Wnt genes 2, 3, 4, and 7B in human breast cell lines and normal and disease states of human breast tissue". Cancer Res. 54 (10): 2615–21. PMID 8168088.
• Gazit A, Yaniv A, Bafico A, et al. (1999). "Human frizzled 1 interacts with transforming Wnts to transduce a TCF dependent transcriptional response". Oncogene. 18 (44): 5959–66. doi:10.1038/sj.onc.1202985. PMID 10557084.
• Tanaka K, Okabayashi K, Asashima M, et al. (2000). "The evolutionarily conserved porcupine gene family is involved in the processing of the Wnt family". Eur. J. Biochem. 267 (13): 4300–11. doi:10.1046/j.1432-1033.2000.01478.x. PMID 10866835.
• Katoh M (2002). "Regulation of WNT3 and WNT3A mRNAs in human cancer cell lines NT2, MCF-7, and MKN45". Int. J. Oncol. 20 (2): 373–7. doi:10.3892/ijo.20.2.373. PMID 11788904.
• Katoh M (2002). "Molecular cloning and expression of mouse Wnt14, and structural comparison between mouse Wnt14-Wnt3a gene cluster and human WNT14-WNT3A gene cluster". Int. J. Mol. Med. 9 (3): 221–7. doi:10.3892/ijmm.9.3.221. PMID 11836627.
• Filali M, Cheng N, Abbott D, et al. (2002). "Wnt-3A/beta-catenin signaling induces transcription from the LEF-1 promoter". J. Biol. Chem. 277 (36): 33398–410. doi:10.1074/jbc.M107977200. PMID 12052822.
• Hering H, Sheng M (2002). "Direct interaction of Frizzled-1, -2, -4, and -7 with PDZ domains of PSD-95". FEBS Lett. 521 (1–3): 185–9. doi:10.1016/S0014-5793(02)02831-4. PMID 12067714.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Hino S, Michiue T, Asashima M, Kikuchi A (2003). "Casein kinase I epsilon enhances the binding of Dvl-1 to Frat-1 and is essential for Wnt-3a-induced accumulation of beta-catenin". J. Biol. Chem. 278 (16): 14066–73. doi:10.1074/jbc.M213265200. PMID 12556519.
• Qiang YW, Endo Y, Rubin JS, Rudikoff S (2003). "Wnt signaling in B-cell neoplasia". Oncogene. 22 (10): 1536–45. doi:10.1038/sj.onc.1206239. PMID 12629517.
• Hocevar BA, Mou F, Rennolds JL, et al. (2003). "Regulation of the Wnt signaling pathway by disabled-2 (Dab2)". EMBO J. 22 (12): 3084–94. doi:10.1093/emboj/cdg286. PMC 162138. PMID 12805222.
• Liu G, Bafico A, Harris VK, Aaronson SA (2003). "A novel mechanism for Wnt activation of canonical signaling through the LRP6 receptor". Mol. Cell. Biol. 23 (16): 5825–35. doi:10.1128/MCB.23.16.5825-5835.2003. PMC 166321. PMID 12897152.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Swiatek W, Tsai IC, Klimowski L, et al. (2004). "Regulation of casein kinase I epsilon activity by Wnt signaling". J. Biol. Chem. 279 (13): 13011–7. doi:10.1074/jbc.M304682200. PMID 14722104.
• Zilberberg A, Yaniv A, Gazit A (2004). "The low density lipoprotein receptor-1, LRP1, interacts with the human frizzled-1 (HFz1) and down-regulates the canonical Wnt signaling pathway". J. Biol. Chem. 279 (17): 17535–42. doi:10.1074/jbc.M311292200. PMID 14739301.
• Lu W, Yamamoto V, Ortega B, Baltimore D (2004). "Mammalian Ryk is a Wnt coreceptor required for stimulation of neurite outgrowth". Cell. 119 (1): 97–108. doi:10.1016/j.cell.2004.09.019. PMID 15454084.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Capurro MI, Shi W, Sandal S, Filmus J (2006). "Processing by convertases is not required for glypican-3-induced stimulation of hepatocellular carcinoma growth". J. Biol. Chem. 280 (50): 41201–6. doi:10.1074/jbc.M507004200. PMID 16227623.
• Thrasivoulou C, Millar M, Ahmed A (2013). "Activation of intracellular calcium by multiple Wnt ligands and translocation of ß-catenin into the nucleus: a convergent model of Wnt/Ca2+ and Wnt/ß-catenin pathways". J. Biol. Chem. 288 (50): 35651–35659. doi:10.1074/jbc.M112.437913. PMC 3861617. PMID 24158438.