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MTHFD2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1ZN4
Identifiers
Aliases	MTHFD2, NMDMC, methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase
External IDs	OMIM: 604887; MGI: 1338850; HomoloGene: 21321; GeneCards: MTHFD2; OMA:MTHFD2 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2p13.1 Start 74,186,172 bp End 74,217,565 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6 C3|6 35.94 cM Start 83,282,673 bp End 83,302,890 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cartilage tissue Descending thoracic aorta popliteal artery tibial arteries ascending aorta gonad left coronary artery right coronary artery stromal cell of endometrium tibia Top expressed in lacrimal gland seminal vesicula Ileal epithelium zygote calvaria secondary oocyte primary oocyte primitive streak Paneth cell salivary gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function oxidoreductase activity catalytic activity hydrolase activity methenyltetrahydrofolate cyclohydrolase activity magnesium ion binding methylenetetrahydrofolate dehydrogenase (NAD+) activity methylenetetrahydrofolate dehydrogenase (NADP+) activity phosphate ion binding Cellular component mitochondrion cytosol mitochondrial matrix extracellular space Biological process metabolism one-carbon metabolic process tetrahydrofolate metabolic process folic acid metabolic process tetrahydrofolate interconversion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10797 17768 Ensembl ENSG00000065911 ENSMUSG00000005667 UniProt P13995 P18155 RefSeq (mRNA) NM_001040409 NM_006636 NM_008638 RefSeq (protein) NP_006627 NP_032664 Location (UCSC) Chr 2: 74.19 – 74.22 Mb Chr 6: 83.28 – 83.3 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial is an enzyme that in humans is encoded by the MTHFD2 gene.

This gene encodes a nuclear-encoded mitochondrial bifunctional enzyme with methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities. The enzyme functions as a homodimer and is unique in its absolute requirement for magnesium and inorganic phosphate. Formation of the enzyme-magnesium complex allows binding of NAD. Alternative splicing results in multiple transcripts encoding different isoforms. This gene has a pseudogene on chromosome 7.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000065911 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000005667 – 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.
5. Peri KG, Belanger C, Mackenzie RE (Dec 1989). "Nucleotide sequence of the human NAD-dependent methylene tetrahydrofolate dehydrogenase-cyclohydrolase". Nucleic Acids Res. 17 (21): 8853. doi:10.1093/nar/17.21.8853. PMC 335047. PMID 2587219.
6. Yang XM, MacKenzie RE (Nov 1993). "NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the mammalian homolog of the mitochondrial enzyme encoded by the yeast MIS1 gene". Biochemistry. 32 (41): 11118–23. doi:10.1021/bi00092a022. PMID 8218174.
7. ^ "Entrez Gene: MTHFD2 methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase".

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Kokame K, Kato H, Miyata T (1997). "Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis. GRP78/BiP and novel genes". J. Biol. Chem. 271 (47): 29659–65. doi:10.1074/jbc.271.47.29659. PMID 8939898.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Pawelek PD, MacKenzie RE (1998). "Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes". Biochemistry. 37 (4): 1109–15. doi:10.1021/bi971906t. PMID 9454603.
• 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.
• 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.
• Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMID 15815621.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (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 1356129. PMID 16344560.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

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