MRVI1

MRVI1
Identifiers
Aliases MRVI1, IRAG, JAW1L, murine retrovirus integration site 1 homolog
External IDs MGI: 1338023 HomoloGene: 4425 GeneCards: MRVI1
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

10335

17540

Ensembl

ENSG00000072952

ENSMUSG00000005611

UniProt

Q9Y6F6

Q9WUX5

RefSeq (mRNA)

NM_010826
NM_194464

RefSeq (protein)

XP_006507478.1
XP_006507479.1

Location (UCSC) Chr 11: 10.57 – 10.69 Mb Chr 7: 110.87 – 110.98 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Protein MRVI1 is a protein that in humans is encoded by the MRVI1 gene.[3][4]

Function

This gene is similar to a mouse putative tumor suppressor gene that is frequently disrupted by mouse AIDS-related virus (MRV). The encoded protein, which is found in the membrane of the endoplasmic reticulum, is similar to Jaw1, a lymphoid-restricted protein whose expression is downregulated during myeloid differentiation. Therefore, this gene may be a myeloid leukemia tumor suppressor gene. Several alternatively spliced transcripts have been found for this gene, however, the full-length nature of some variants has not been determined. Of the two characterized variants which encode different isoforms, one initiates translation at a non-AUG start site.[4]

Interactions

MRVI1 has been shown to interact with ITPR1[5] and PRKG1.[5][6]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ Shaughnessy JD, Largaespada DA, Tian E, Fletcher CF, Cho BC, Vyas P, Jenkins NA, Copeland NG (June 1999). "Mrvi1, a common MRV integration site in BXH2 myeloid leukemias, encodes a protein with homology to a lymphoid-restricted membrane protein Jaw1". Oncogene. 18 (12): 2069–84. doi:10.1038/sj.onc.1202419. PMID 10321731.
  4. 1 2 "Entrez Gene: MRVI1 murine retrovirus integration site 1 homolog".
  5. 1 2 Schlossmann J, Ammendola A, Ashman K, Zong X, Huber A, Neubauer G, Wang GX, Allescher HD, Korth M, Wilm M, Hofmann F, Ruth P (March 2000). "Regulation of intracellular calcium by a signalling complex of IRAG, IP3 receptor and cGMP kinase Ibeta". Nature. 404 (6774): 197–201. doi:10.1038/35004606. PMID 10724174.
  6. ↑ Ammendola A, Geiselhöringer A, Hofmann F, Schlossmann J (June 2001). "Molecular determinants of the interaction between the inositol 1,4,5-trisphosphate receptor-associated cGMP kinase substrate (IRAG) and cGMP kinase Ibeta". J. Biol. Chem. 276 (26): 24153–9. doi:10.1074/jbc.M101530200. PMID 11309393.

Further reading

  • Adams MD, Dubnick M, Kerlavage AR, Moreno R, Kelley JM, Utterback TR, Nagle JW, Fields C, Venter JC (1992). "Sequence identification of 2,375 human brain genes". Nature. 355 (6361): 632–4. doi:10.1038/355632a0. PMID 1538749. 
  • Baltensperger K, Chiesi M, Carafoli E (1990). "Substrates of cGMP kinase in vascular smooth muscle and their role in the relaxation process". Biochemistry. 29 (41): 9753–60. doi:10.1021/bi00493a035. PMID 2271613. 
  • Schlossmann J, Ammendola A, Ashman K, Zong X, Huber A, Neubauer G, Wang GX, Allescher HD, Korth M, Wilm M, Hofmann F, Ruth P (2000). "Regulation of intracellular calcium by a signalling complex of IRAG, IP3 receptor and cGMP kinase Ibeta". Nature. 404 (6774): 197–201. doi:10.1038/35004606. PMID 10724174. 
  • Ammendola A, Geiselhöringer A, Hofmann F, Schlossmann J (2001). "Molecular determinants of the interaction between the inositol 1,4,5-trisphosphate receptor-associated cGMP kinase substrate (IRAG) and cGMP kinase Ibeta". J. Biol. Chem. 276 (26): 24153–9. doi:10.1074/jbc.M101530200. PMID 11309393. 
  • Koller A, Schlossmann J, Ashman K, Uttenweiler-Joseph S, Ruth P, Hofmann F (2003). "Association of phospholamban with a cGMP kinase signaling complex". Biochem. Biophys. Res. Commun. 300 (1): 155–60. doi:10.1016/S0006-291X(02)02799-7. PMID 12480535. 
  • Fritsch RM, Saur D, Kurjak M, Oesterle D, Schlossmann J, Geiselhöringer A, Hofmann F, Allescher HD (2004). "InsP3R-associated cGMP kinase substrate (IRAG) is essential for nitric oxide-induced inhibition of calcium signaling in human colonic smooth muscle". J. Biol. Chem. 279 (13): 12551–9. doi:10.1074/jbc.M313365200. PMID 14729908. 
  • Casteel DE, Boss GR, Pilz RB (2005). "Identification of the interface between cGMP-dependent protein kinase Ibeta and its interaction partners TFII-I and IRAG reveals a common interaction motif". J. Biol. Chem. 280 (46): 38211–8. doi:10.1074/jbc.M507021200. PMID 16166082. 
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129Freely accessible. PMID 16344560. 
  • Antl M, von Brühl ML, Eiglsperger C, Werner M, Konrad I, Kocher T, Wilm M, Hofmann F, Massberg S, Schlossmann J (2007). "IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation". Blood. 109 (2): 552–9. doi:10.1182/blood-2005-10-026294. PMID 16990611. 
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