Gene
mthfd2l
- ID
- ZDB-GENE-030131-5707
- Name
- methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2 like
- Symbol
- mthfd2l Nomenclature History
- Previous Names
-
- wu:fi14c12
- zgc:63479
- Type
- protein_coding_gene
- Location
- Chr: 8 Mapping Details/Browsers
- Description
- Predicted to enable methenyltetrahydrofolate cyclohydrolase activity and methylenetetrahydrofolate dehydrogenase (NADP+) activity. Predicted to be involved in tetrahydrofolate interconversion. Predicted to act upstream of or within one-carbon metabolic process. Predicted to be active in mitochondrion. Is expressed in anterior neural tube and optic cup. Orthologous to human MTHFD2L (methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2 like).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 1 figure from Lee et al., 2012
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
- No data available
Wild Type Expression Summary
- All Phenotype Data
- No data available
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
No data available
No data available
Human Disease
Domain, Family, and Site Summary
| Type | InterPro ID | Name |
|---|---|---|
| Conserved_site | IPR020867 | Tetrahydrofolate dehydrogenase/cyclohydrolase, conserved site |
| Domain | IPR020630 | Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain |
| Domain | IPR020631 | Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain |
| Family | IPR000672 | Tetrahydrofolate dehydrogenase/cyclohydrolase |
| Homologous_superfamily | IPR036291 | NAD(P)-binding domain superfamily |
| Homologous_superfamily | IPR046346 | Aminoacid dehydrogenase-like, N-terminal domain superfamily |
Domain Details Per Protein
| Protein | Additional Resources | Length | Aminoacid dehydrogenase-like, N-terminal domain superfamily | NAD(P)-binding domain superfamily | Tetrahydrofolate dehydrogenase/cyclohydrolase | Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain | Tetrahydrofolate dehydrogenase/cyclohydrolase, conserved site | Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain |
|---|---|---|---|---|---|---|---|---|
| UniProtKB:A0A8M2BEG5 | InterPro | 348 | ||||||
| UniProtKB:Q7SY55 | InterPro | 334 | ||||||
| UniProtKB:A0AB32TWJ8 | InterPro | 306 | ||||||
| UniProtKB:A0AB32TYC2 | InterPro | 238 |
| Type | Name | Annotation Method | Has Havana Data | Length (nt) | Analysis |
|---|---|---|---|---|---|
| mRNA |
mthfd2l-201
(1)
|
Ensembl | 1,788 nt | ||
| mRNA |
mthfd2l-202
(1)
|
Ensembl | 922 nt |
Interactions and Pathways
No data available
Plasmids
No data available
No data available
| Relationship | Marker Type | Marker | Accession Numbers | Citations |
|---|---|---|---|---|
| Contained in | BAC | DKEY-27J13 | ZFIN Curated Data | |
| Encodes | EST | fi14c12 | ||
| Encodes | cDNA | MGC:63479 | ZFIN Curated Data |
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| Type | Accession # | Sequence | Length (nt/aa) | Analysis |
|---|---|---|---|---|
| RNA | RefSeq:NM_199813 (1) | 1790 nt | ||
| Genomic | GenBank:BX545917 (1) | 139530 nt | ||
| Polypeptide | UniProtKB:A0A8M2BEG5 (1) | 348 aa |
- Briolat, V., Jouneau, L., Carvalho, R., Palha, N., Langevin, C., Herbomel, P., Schwartz, O., Spaink, H.P., Levraud, J.P., Boudinot, P. (2014) Contrasted Innate Responses to Two Viruses in Zebrafish: Insights into the Ancestral Repertoire of Vertebrate IFN-Stimulated Genes. Journal of immunology (Baltimore, Md. : 1950). 192:4328-41
- Lee, M.S., Bonner, J.R., Bernard, D.J., Sanchez, E.L., Sause, E.T., Prentice, R.R., Burgess, S.M., and Brody, L.C. (2012) Disruption of the folate pathway in zebrafish causes developmental defects. BMC Developmental Biology. 12(1):12
- Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G., Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D., Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K., Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F., Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L., Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L., Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S., Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J., Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J., McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S., Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W., Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A., Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y., Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M., Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E., Schnerch,A., Schein,J.E., Jones,S.J., and Marra,M.A. (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
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