MOCS3

Protein-coding gene in the species Homo sapiens

MOCS3

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
3I2V

Identifiers

Aliases

MOCS3, UBA4, molybdenum cofactor synthesis 3

External IDs

OMIM: 609277 MGI: 1916622 HomoloGene: 6108 GeneCards: MOCS3

Gene location (Human)

Chr.	Chromosome 20 (human)^[1]

Band	20q13.13	Start	50,958,818 bp^[1]
Band	20q13.13	End	50,963,929 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)^[2]

Band	2\|2 H3	Start	168,072,542 bp^[2]
Band	2\|2 H3	End	168,074,514 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

sperm

stromal cell of endometrium

ganglionic eminence

islet of Langerhans

gastrocnemius muscle

prefrontal cortex

bronchial epithelial cell

left adrenal gland

right lobe of liver

right coronary artery

Top expressed in

seminiferous tubule

spermatid

spermatocyte

proximal tubule

hair follicle

superior frontal gyrus

primitive streak

yolk sac

medial ganglionic eminence

epithelium of stomach

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity nucleotide binding thiosulfate sulfurtransferase activity molybdopterin-synthase sulfurtransferase activity metal ion binding URM1 activating enzyme activity protein binding catalytic activity ubiquitin-like modifier activating enzyme activity ATP binding molybdopterin-synthase adenylyltransferase activity nucleotidyltransferase activity sulfurtransferase activity
Cellular component	cytoplasm cytosol
Biological process	molybdopterin cofactor biosynthetic process tRNA processing Mo-molybdopterin cofactor biosynthetic process metabolism tRNA wobble uridine modification tRNA thio-modification tRNA wobble position uridine thiolation protein urmylation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


27304


69372

Ensembl


ENSG00000124217


ENSMUSG00000074576

UniProt


O95396


A2BDX3

RefSeq (mRNA)


NM_014484


NM_001160330

RefSeq (protein)


NP_055299


NP_001153802

Location (UCSC)

Chr 20: 50.96 – 50.96 Mb

Chr 2: 168.07 – 168.07 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Adenylyltransferase and sulfurtransferase MOCS3 is an enzyme that in humans is encoded by the MOCS3 gene.^[5]^[6]

Molybdenum cofactor (MoCo) is necessary for the function of all molybdoenzymes. One of the enzymes required for the biosynthesis of MoCo is molybdopterin synthase (MPT synthase, encoded by MOCS2/Mocs2 in mammals). The protein encoded by this gene adenylates and activates MPT synthase. This gene contains no introns. A pseudogene of this gene is present on chromosome 14.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000124217 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000074576 – 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.
^ Matthies A, Nimtz M, Leimkuhler S (May 2005). "Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry". Biochemistry. 44 (21): 7912–20. doi:10.1021/bi0503448. PMID 15910006.
^ ^a ^b "Entrez Gene: MOCS3 molybdenum cofactor synthesis 3".

Reiss J, Johnson JL (2003). "Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH". Hum. Mutat. 21 (6): 569–76. doi:10.1002/humu.10223. PMID 12754701. S2CID 41013043.
Johnson JL, Coyne KE, Rajagopalan KV, et al. (2002). "Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency". Am. J. Med. Genet. 104 (2): 169–73. doi:10.1002/1096-8628(20011122)104:2<169::AID-AJMG1603>3.0.CO;2-8. PMID 11746050.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.
Cortese MS, Caplan AB, Crawford RL (2003). "Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid)". BMC Evol. Biol. 2: 8. doi:10.1186/1471-2148-2-8. PMC 115864. PMID 11972321.
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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S (2004). "Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 5946–51. Bibcode:2004PNAS..101.5946M. doi:10.1073/pnas.0308191101. PMC 395903. PMID 15073332.
Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
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.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Krepinsky K, Leimkühler S (2007). "Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologs". FEBS J. 274 (11): 2778–87. doi:10.1111/j.1742-4658.2007.05811.x. PMID 17459099. S2CID 82541137.

Metabolism of vitamins, coenzymes, and cofactors

Fat soluble vitamins

Vitamin A	Retinol binding protein
Vitamin E	Alpha-tocopherol transfer protein
Vitamin D	liver (Sterol 27-hydroxylase or CYP27A1) renal (25-Hydroxyvitamin D₃ 1-alpha-hydroxylase or CYP27B1) degradation (1,25-Dihydroxyvitamin D₃ 24-hydroxylase or CYP24A1)
Vitamin K	Vitamin K epoxide reductase