ALDH1L1

Protein-coding gene in the species Homo sapiens

ALDH1L1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2BW0, 2CFI, 2CQ8

Identifiers
AliasesALDH1L1, 10-FTHFDH, 10-fTHF, FDH, FTHFD, aldehyde dehydrogenase 1 family member L1
External IDsOMIM: 600249; MGI: 1340024; HomoloGene: 122031; GeneCards: ALDH1L1; OMA:ALDH1L1 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for ALDH1L1
Genomic location for ALDH1L1
Band3q21.3Start126,103,562 bp[1]
End126,197,994 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for ALDH1L1
Genomic location for ALDH1L1
Band6|6 D1Start90,463,409 bp[2]
End90,577,185 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of liver

  • olfactory zone of nasal mucosa

  • human kidney

  • muscle of thigh

  • parotid gland

  • gastrocnemius muscle

  • optic nerve

  • glutes

  • gastric mucosa

  • caudate nucleus
Top expressed in
  • left lobe of liver

  • right kidney

  • human kidney

  • proximal tubule

  • left colon

  • intestinal villus

  • jejunum

  • adrenal gland

  • white adipose tissue

  • optic nerve
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • formyltetrahydrofolate dehydrogenase activity
  • oxidoreductase activity
  • hydroxymethyl-, formyl- and related transferase activity
  • catalytic activity
  • aldehyde dehydrogenase (NAD+) activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Cellular component
  • extracellular exosome
  • mitochondrion
  • cytoplasm
  • cytosol
Biological process
  • metabolism
  • one-carbon metabolic process
  • biosynthesis
  • 10-formyltetrahydrofolate catabolic process
  • folic acid metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10840

107747

Ensembl

ENSG00000144908

ENSMUSG00000030088

UniProt

O75891

Q8R0Y6

RefSeq (mRNA)

NM_001270364
NM_001270365
NM_012190
NM_144776

NM_027406
NM_001356412

RefSeq (protein)

NP_001257293
NP_001257294
NP_036322

NP_081682
NP_001343341

Location (UCSC)Chr 3: 126.1 – 126.2 MbChr 6: 90.46 – 90.58 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

10-formyltetrahydrofolate dehydrogenase is an enzyme that in humans is encoded by the ALDH1L1 gene.[5]

The protein encoded by this gene catalyzes the conversion of 10-formyltetrahydrofolate, nicotinamide adenine dinucleotide phosphate (NADP), and water to tetrahydrofolate, NADPH, and carbon dioxide. The encoded protein belongs to the aldehyde dehydrogenase family and is responsible for formate oxidation in vivo. Deficiencies in this gene can result in an accumulation of formate and subsequent methanol poisoning.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000144908 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030088 – 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. ^ a b "Entrez Gene: ALDH1L1 aldehyde dehydrogenase 1 family, member L1".

Further reading

  • Lee KM, Lan Q, Kricker A, et al. (2007). "One-carbon metabolism gene polymorphisms and risk of non-Hodgkin lymphoma in Australia". Hum. Genet. 122 (5): 525–33. doi:10.1007/s00439-007-0431-2. PMID 17891500. S2CID 21487646.
  • Stevens VL, McCullough ML, Pavluck AL, et al. (2007). "Association of polymorphisms in one-carbon metabolism genes and postmenopausal breast cancer incidence". Cancer Epidemiol. Biomarkers Prev. 16 (6): 1140–7. doi:10.1158/1055-9965.EPI-06-1037. PMID 17548676. S2CID 25945965.
  • Lim U, Wang SS, Hartge P, et al. (2007). "Gene-nutrient interactions among determinants of folate and one-carbon metabolism on the risk of non-Hodgkin lymphoma: NCI-SEER case-control study". Blood. 109 (7): 3050–9. doi:10.1182/blood-2006-07-034330. PMC 1852210. PMID 17119116.
  • Oleinik NV, Krupenko SA (2004). "Ectopic expression of 10-formyltetrahydrofolate dehydrogenase in A549 cells induces G1 cell cycle arrest and apoptosis". Mol. Cancer Res. 1 (8): 577–88. PMID 12805405.
  • 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.
  • Krupenko SA, Oleinik NV (2002). "10-formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells". Cell Growth Differ. 13 (5): 227–36. PMID 12065246.
  • Hong M, Lee Y, Kim JW, et al. (1999). "Isolation and characterization of cDNA clone for human liver 10-formyltetrahydrofolate dehydrogenase". Biochem. Mol. Biol. Int. 47 (3): 407–15. doi:10.1080/15216549900201433. PMID 10204077. S2CID 10950424.
  • 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.
  • 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.
  • Champion KM, Cook RJ, Tollaksen SL, Giometti CS (1994). "Identification of a heritable deficiency of the folate-dependent enzyme 10-formyltetrahydrofolate dehydrogenase in mice". Proc. Natl. Acad. Sci. U.S.A. 91 (24): 11338–42. Bibcode:1994PNAS...9111338C. doi:10.1073/pnas.91.24.11338. PMC 45226. PMID 7972060.
  • Johlin FC, Swain E, Smith C, Tephly TR (1989). "Studies on the mechanism of methanol poisoning: purification and comparison of rat and human liver 10-formyltetrahydrofolate dehydrogenase". Mol. Pharmacol. 35 (6): 745–50. PMID 2733692.
  • v
  • t
  • e
  • 1s3i: Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase
    1s3i: Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase
  • 2bw0: CRYSTAL STRUCTURE OF THE HYDROLASE DOMAIN OF HUMAN 10-FORMYLTETRAHYDROFOLATE 2 DEHYDROGENASE
    2bw0: CRYSTAL STRUCTURE OF THE HYDROLASE DOMAIN OF HUMAN 10-FORMYLTETRAHYDROFOLATE 2 DEHYDROGENASE
  • 2cfi: THE HYDROLASE DOMAIN OF HUMAN 10-FTHFD IN COMPLEX WITH 6-FORMYLTETRAHYDROPTERIN
    2cfi: THE HYDROLASE DOMAIN OF HUMAN 10-FTHFD IN COMPLEX WITH 6-FORMYLTETRAHYDROPTERIN
  • 2cq8: Solution structure of RSGI RUH-033, a pp-binding domain of 10-FTHFDH from human cDNA
    2cq8: Solution structure of RSGI RUH-033, a pp-binding domain of 10-FTHFDH from human cDNA
  • 2o2p: Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase
    2o2p: Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase
  • 2o2q: Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADP
    2o2q: Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADP
  • 2o2r: Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH
    2o2r: Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH


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