MOCS2

MOCS2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4AP8
Identifiers
Aliases	MOCS2, MCBPE, MOCO1, MOCODB, MPTS, molybdenum cofactor synthesis 2
External IDs	OMIM: 603708; MGI: 1336894; HomoloGene: 32193; GeneCards: MOCS2; OMA:MOCS2 - orthologs
Gene location (Human)
Chr.	Chromosome 5 (human)
End	53,110,063 bp
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)
End	114,968,811 bp
RNA expression pattern
	Top expressed in
	anterior cingulate cortex; ; right adrenal gland; ; prefrontal cortex; ; right adrenal cortex; ; left adrenal gland; ; left adrenal cortex; ; caudate nucleus; ; right frontal lobe; ; right auricle; ; nucleus accumbens;
	Top expressed in
	lens; ; epithelium of lens; ; Paneth cell; ; transitional epithelium of urinary bladder; ; left lobe of liver; ; facial motor nucleus; ; supraoptic nucleus; ; jejunum; ; aortic valve; ; ascending aorta;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; molybdopterin synthase activity; nucleotide binding;
Cellular component	molybdopterin synthase complex; cytosol; nucleus; cytoplasm; nuclear speck;
Biological process	Mo-molybdopterin cofactor biosynthetic process; molybdopterin cofactor biosynthetic process;
	Sources:Amigo / QuickGO
Orthologs
	4338
	17434
	ENSG00000164172
	ENSMUSG00000015536
	O96007; O96033
	Q9Z223; Q9Z224
	NM_176806; NM_004531
	NM_001113374; NM_001113375; NM_013826
	NP_004522; NP_789776; NP_789776.1
	NP_001106845; NP_001106846; NP_038854
	Wikidata
View/Edit Human	View/Edit Mouse

Molybdenum cofactor synthesis protein 2A and molybdenum cofactor synthesis protein 2B are a pair of proteins that in humans are encoded from the same MOCS2 gene.^[5]^[6]^[7] These two proteins dimerize to form molybdopterin synthase.

Function

Eukaryotic molybdoenzymes use a unique molybdenum cofactor (MoCo) consisting of a pterin and the catalytically active metal molybdenum. MoCo is synthesized from cyclic pyranopterin monophosphate (precursor Z) by the heterodimeric enzyme molybdopterin synthase.^[7]

Gene

The large and small subunits of molybdopterin synthase are both encoded from the MOCS2 gene by overlapping open reading frames. The proteins were initially thought to be encoded from a bicistronic transcript. They are now thought to be encoded from monocistronic transcripts. Alternatively spliced transcripts have been found for this locus that encode the large and small subunits.^[7]

The MOCS2 gene contains 7 exons. Exons 1 to 3 encode MOCS2A (the small subunit), and exons 3 to 7 encode MOCS2B (large subunit).^[5]

Genetic disease

Defects in both copies of MOCS2 cause the molybdenum cofactor deficiency disease in babies.^[8]

Protein structure

MOCS2A and MOCS2B subunits form dimers in solution. These dimers in turn dimerize to form the tetrameric molybdopterin synthase complex.^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000164172 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000015536 – 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.
^ ^a ^b Reiss J, Dorche C, Stallmeyer B, Mendel RR, Cohen N, Zabot MT (March 1999). "Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B". American Journal of Human Genetics. 64 (3): 706–11. doi:10.1086/302296. PMC 1377787. PMID 10053004.
^ Sloan J, Kinghorn JR, Unkles SE (February 1999). "The two subunits of human molybdopterin synthase: evidence for a bicistronic messenger RNA with overlapping reading frames". Nucleic Acids Research. 27 (3): 854–8. doi:10.1093/nar/27.3.854. PMC 148257. PMID 9889283.
^ ^a ^b ^c EntrezGene 4338: MOCS2 molybdenum cofactor synthesis 2
^ Ichida K, Aydin HI, Hosoyamada M, et al. (2006). "A Turkish case with molybdenum cofactor deficiency". Nucleosides, Nucleotides & Nucleic Acids. 25 (9–11): 1087–91. doi:10.1080/15257770600894022. PMID 17065069. S2CID 40601679.
^ Leimkuhler S, Freuer A, Araujo JA, Rajagopalan KV, Mendel RR (July 2003). "Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency". The Journal of Biological Chemistry. 278 (28): 26127–34. doi:10.1074/jbc.M303092200. PMID 12732628.

Reiss J, Johnson JL (June 2003). "Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH". Human Mutation. 21 (6): 569–76. doi:10.1002/humu.10223. PMID 12754701. S2CID 41013043.
Krawczak M, Reiss J, Cooper DN (1992). "The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: causes and consequences". Human Genetics. 90 (1–2): 41–54. doi:10.1007/bf00210743. PMID 1427786. S2CID 12544333.
Reiss J, Cohen N, Dorche C, et al. (September 1998). "Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency". Nature Genetics. 20 (1): 51–3. doi:10.1038/1706. PMID 9731530. S2CID 23833158.
Feng G, Tintrup H, Kirsch J, et al. (November 1998). "Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity". Science. 282 (5392): 1321–4. Bibcode:1998Sci...282.1321F. doi:10.1126/science.282.5392.1321. PMID 9812897.
Stallmeyer B, Drugeon G, Reiss J, Haenni AL, Mendel RR (March 1999). "Human molybdopterin synthase gene: identification of a bicistronic transcript with overlapping reading frames". American Journal of Human Genetics. 64 (3): 698–705. doi:10.1086/302295. PMC 1377786. PMID 10053003.
Johnson JL, Coyne KE, Rajagopalan KV, et al. (November 2001). "Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency". American Journal of Medical Genetics. 104 (2): 169–73. doi:10.1002/1096-8628(20011122)104:2<169::AID-AJMG1603>3.0.CO;2-8. PMID 11746050.
Strausberg RL, Feingold EA, Grouse LH, et al. (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S (April 2004). "Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans". Proceedings of the National Academy of Sciences of the United States of America. 101 (16): 5946–51. Bibcode:2004PNAS..101.5946M. doi:10.1073/pnas.0308191101. PMC 395903. PMID 15073332.
Gerhard DS, Wagner L, Feingold EA, et al. (October 2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Research. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Leimkühler S, Charcosset M, Latour P, et al. (October 2005). "Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase". Human Genetics. 117 (6): 565–70. doi:10.1007/s00439-005-1341-9. PMID 16021469. S2CID 1267356.
Hahnewald R, Leimkühler S, Vilaseca A, Acquaviva-Bourdain C, Lenz U, Reiss J (November 2006). "A novel MOCS2 mutation reveals coordinated expression of the small and large subunit of molybdopterin synthase". Molecular Genetics and Metabolism. 89 (3): 210–3. doi:10.1016/j.ymgme.2006.04.008. PMID 16737835.
Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
Per H, Gümüş H, Ichida K, Cağlayan O, Kumandaş S (July 2007). "Molybdenum cofactor deficiency: clinical features in a Turkish patient". Brain & Development. 29 (6): 365–8. doi:10.1016/j.braindev.2006.10.007. PMID 17158010. S2CID 46531501.

This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000164172 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000015536 – 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.

[pmid10053004-5] Reiss J, Dorche C, Stallmeyer B, Mendel RR, Cohen N, Zabot MT (March 1999). "Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B". American Journal of Human Genetics. 64 (3): 706–11. doi:10.1086/302296. PMC 1377787. PMID 10053004.

[pmid9889283-6] Sloan J, Kinghorn JR, Unkles SE (February 1999). "The two subunits of human molybdopterin synthase: evidence for a bicistronic messenger RNA with overlapping reading frames". Nucleic Acids Research. 27 (3): 854–8. doi:10.1093/nar/27.3.854. PMC 148257. PMID 9889283.

[entrez-7] EntrezGene 4338: MOCS2 molybdenum cofactor synthesis 2

[8] Ichida K, Aydin HI, Hosoyamada M, et al. (2006). "A Turkish case with molybdenum cofactor deficiency". Nucleosides, Nucleotides & Nucleic Acids. 25 (9–11): 1087–91. doi:10.1080/15257770600894022. PMID 17065069. S2CID 40601679.

[pmid12732628-9] Leimkuhler S, Freuer A, Araujo JA, Rajagopalan KV, Mendel RR (July 2003). "Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency". The Journal of Biological Chemistry. 278 (28): 26127–34. doi:10.1074/jbc.M303092200. PMID 12732628.

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