R-spondin 3

RSPO3
Identifiers
Aliases	RSPO3, CRISTIN1, PWTSR, THSD2, R-spondin 3
External IDs	OMIM: 610574; MGI: 1920030; HomoloGene: 12484; GeneCards: RSPO3; OMA:RSPO3 - orthologs
Gene location (Human)
Chr.	Chromosome 6 (human)
End	127,199,481 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	29,411,863 bp
RNA expression pattern
	Top expressed in
	gastric mucosa; ; tail of epididymis; ; caput epididymis; ; smooth muscle tissue; ; corpus epididymis; ; vastus lateralis muscle; ; superficial temporal artery; ; buccal mucosa cell; ; placenta; ; body of uterus;
	Top expressed in
	vas deferens; ; otolith organ; ; tail of embryo; ; utricle; ; vestibular sensory epithelium; ; primitive streak; ; stria vascularis; ; stroma of bone marrow; ; adventitia of seminal vesicle; ; gastrula;
	More reference expression data
	n/a
Gene ontology
Molecular function	heparin binding; signaling receptor binding; frizzled binding;
Cellular component	extracellular region; extracellular space;
Biological process	positive regulation of canonical Wnt signaling pathway; positive regulation of Wnt signaling pathway; positive regulation of Wnt signaling pathway, planar cell polarity pathway; Wnt signaling pathway; branching involved in labyrinthine layer morphogenesis; angiogenesis; response to stimulus; blood vessel remodeling; positive regulation of non-canonical Wnt signaling pathway; sprouting angiogenesis; regulation of Wnt signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	84870
	72780
	ENSG00000146374
	ENSMUSG00000019880
	Q9BXY4
	Q2TJ95
	NM_032784
	NM_028351
	NP_116173
	NP_082627
	Wikidata
View/Edit Human	View/Edit Mouse

R-spondin-3 is a protein that in humans is encoded by the RSPO3 gene.^[5]^[6]^[7]

Function

This gene encodes a member of the thrombospondin type 1 repeat supergene family. In addition, the protein contains a furin-like cysteine-rich region. Furin-like repeat domains have been found in a variety of eukaryotic proteins involved in the mechanism of signal transduction by receptor tyrosine kinases.^[7]

During embryonic development, RSPO3 is expressed in the tail bud and the posterior presomitic mesoderm of the embryo. In tissue engineering, R-spondin 3 has been used to differentiate pluripotent stem cells into paraxial mesoderm progenitors^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000146374 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000019880 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Adams JC, Tucker RP (Jun 2000). "The thrombospondin type 1 repeat (TSR) superfamily: diverse proteins with related roles in neuronal development". Developmental Dynamics. 218 (2): 280–99. doi:10.1002/(SICI)1097-0177(200006)218:2<280::AID-DVDY4>3.0.CO;2-0. PMID 10842357.
^ Kazanskaya O, Glinka A, del Barco Barrantes I, Stannek P, Niehrs C, Wu W (Oct 2004). "R-Spondin2 is a secreted activator of Wnt/beta-catenin signaling and is required for Xenopus myogenesis". Developmental Cell. 7 (4): 525–34. doi:10.1016/j.devcel.2004.07.019. PMID 15469841.
^ ^a ^b "Entrez Gene: RSPO3 R-spondin 3 homolog (Xenopus laevis)".
^ Chal J, Oginuma M, Al Tanoury Z, Gobert B, Sumara O, Hick A, Bousson F, Zidouni Y, Mursch C, Moncuquet P, Tassy O, Vincent S, Miyanari A, Bera A, Garnier JM, Guevara G, Hestin M, Kennedy L, Hayashi S, Drayton B, Cherrier T, Gayraud-Morel B, Gussoni E, Relaix F, Tajbakhsh S, Pourquié O (Sep 2015). "Differentiation of pluripotent stem cells to muscle fiber to model Duchenne muscular dystrophy". Nature Biotechnology. 33 (9): 962–9. doi:10.1038/nbt.3297. PMID 26237517.

Kim KA, Zhao J, Andarmani S, Kakitani M, Oshima T, Binnerts ME, Abo A, Tomizuka K, Funk WD (Jan 2006). "R-Spondin proteins: a novel link to beta-catenin activation". Cell Cycle. 5 (1): 23–6. doi:10.4161/cc.5.1.2305. PMID 16357527.
Hannah BL, Misenheimer TM, Annis DS, Mosher DF (Mar 2003). "A polymorphism in thrombospondin-1 associated with familial premature coronary heart disease causes a local change in conformation of the Ca2+-binding repeats". The Journal of Biological Chemistry. 278 (11): 8929–34. doi:10.1074/jbc.M211185200. PMID 12643280.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Chen JZ, Wang S, Tang R, Yang QS, Zhao E, Chao Y, Ying K, Xie Y, Mao YM (Sep 2002). "Cloning and identification of a cDNA that encodes a novel human protein with thrombospondin type I repeat domain, hPWTSR". Molecular Biology Reports. 29 (3): 287–92. doi:10.1023/A:1020479301379. PMID 12463421.

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000146374 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000019880 – 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.

[pmid10842357-5] Adams JC, Tucker RP (Jun 2000). "The thrombospondin type 1 repeat (TSR) superfamily: diverse proteins with related roles in neuronal development". Developmental Dynamics. 218 (2): 280–99. doi:10.1002/(SICI)1097-0177(200006)218:2<280::AID-DVDY4>3.0.CO;2-0. PMID 10842357.

[pmid15469841-6] Kazanskaya O, Glinka A, del Barco Barrantes I, Stannek P, Niehrs C, Wu W (Oct 2004). "R-Spondin2 is a secreted activator of Wnt/beta-catenin signaling and is required for Xenopus myogenesis". Developmental Cell. 7 (4): 525–34. doi:10.1016/j.devcel.2004.07.019. PMID 15469841.

[entrez-7] "Entrez Gene: RSPO3 R-spondin 3 homolog (Xenopus laevis)".

[pmid26237517-8] Chal J, Oginuma M, Al Tanoury Z, Gobert B, Sumara O, Hick A, Bousson F, Zidouni Y, Mursch C, Moncuquet P, Tassy O, Vincent S, Miyanari A, Bera A, Garnier JM, Guevara G, Hestin M, Kennedy L, Hayashi S, Drayton B, Cherrier T, Gayraud-Morel B, Gussoni E, Relaix F, Tajbakhsh S, Pourquié O (Sep 2015). "Differentiation of pluripotent stem cells to muscle fiber to model Duchenne muscular dystrophy". Nature Biotechnology. 33 (9): 962–9. doi:10.1038/nbt.3297. PMID 26237517.

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Function

References

Further reading