RSPO3

R-spondin 3
Identifiers
Symbols	RSPO3 ; CRISTIN1; PWTSR; THSD2
External IDs	OMIM: 610574 MGI: 1920030 HomoloGene: 12484 GeneCards: RSPO3 Gene
Gene ontology Molecular function • G-protein coupled receptor binding • receptor binding • frizzled binding • heparin binding Cellular component • extracellular region • extracellular space Biological process • angiogenesis • Wnt signaling pathway • branching involved in labyrinthine layer morphogenesis • positive regulation of canonical Wnt signaling pathway Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	84870	72780
Ensembl	ENSG00000146374	ENSMUSG00000019880
UniProt	Q9BXY4	Q2TJ95
RefSeq (mRNA)	NM_032784	NM_028351
RefSeq (protein)	NP_116173	NP_082627
Location (UCSC)	Chr 6: 127.12 – 127.2 Mb	Chr 10: 29.45 – 29.54 Mb
PubMed search

R-spondin-3 is a protein that in humans is encoded by the RSPO3 gene.^[1][2][3]

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.^[3]

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^[4]

References

1. 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.
2. 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.
3. "Entrez Gene: RSPO3 R-spondin 3 homolog (Xenopus laevis)".
4. 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.

Further reading

• 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.
• 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.