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UniProtKB/Swiss-Prot entry P18155


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MTDC_MOUSE
Primary accession number P18155
Secondary accession number Q3TMN4
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on November 1, 1990 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 79)
Name and origin of the protein
Protein name Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial [Precursor]
Synonyms None
Includes NAD-dependent methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.15)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Gene name
Name: Mthfd2
Synonyms: Nmdmc
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 36-55.
PubMed=2647744 [NCBI, ExPASy, EBI, Israel, Japan]
Belanger C., Mackenzie R.E.;
"Isolation and characterization of cDNA clones encoding the murine NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase.";
J. Biol. Chem. 264:4837-4843(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(91)90064-I; PubMed=1999293 [NCBI, ExPASy, EBI, Israel, Japan]
Belanger C., Mackenzie R.E.;
"Structural organization of the murine gene encoding NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase.";
Gene 97:283-288(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Salivary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
DOI=10.1093/nar/19.16.4341; PubMed=1843253 [NCBI, ExPASy, EBI, Israel, Japan]
Belanger C., Peri K.G., Mackenzie R.E.;
"Analysis of the promoter region of the gene encoding NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase.";
Nucleic Acids Res. 19:4341-4345(1991).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J04627; AAA39827.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63445; AAA39828.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63415; AAA39828.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63439; AAA39828.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63440; AAA39828.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63441; AAA39828.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63442; AAA39828.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63443; AAA39828.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63444; AAA39828.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK076019; BAC36124.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK159680; BAE35283.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK165840; BAE38407.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019511; AAH19511.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S52980; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR A33267; A33267.
RefSeq NP_032664.1; -.
UniGene Mm.443
3D structure databases
HSSP P11586; 1A4I. [HSSP ENTRY / PDB]
ModBase P18155.
PTM databases
PhosphoSite P18155; -.
Organism-specific databases
MGI MGI:1338850; Mthfd2.
Gene expression databases
ArrayExpress P18155; -.
GermOnline ENSMUSG00000005667; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.
Pfam PF00763; THF_DHG_CYH; 1.
PF02882; THF_DHG_CYH_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00085; THFDHDRGNASE.
ProDom PD002300; THFDhg/Cyc_hydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00766; THF_DHG_CYH_1; 1.
PS00767; THF_DHG_CYH_2; 1.
BLOCKS P18155.
Genome annotation databases
Ensembl ENSMUSG00000005667; Mus musculus. [Contig view]
GeneID 17768; -.
KEGG mmu:17768; -.
NMPDR fig|10090.3.peg.14707; -.
Phylogenomic databases
HOGENOM P18155; -.
HOVERGEN P18155; -.
Other
LinkHub P18155; -.
SOURCE Mthfd2; Mus musculus.
ProtoNet P18155.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Hydrolase; Magnesium; Mitochondrion; Multifunctional enzyme; NAD; One-carbon metabolism; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
TRANSIT   1    35  35     Mitochondrion. 
CHAIN   36   350  315     Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial. PRO_0000034050
Sequence information
Length: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 37863 Da [This is the MW of the unprocessed precursor] CRC64: 896AD40D9154E9D7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASVSLLSAL AVRLLRPTHG CHPRLQPFHL AAVRNEAVVI SGRKLAQQIK QEVQQEVEEW 

        70         80         90        100        110        120 
VASGNKRPHL SVILVGDNPA SHSYVLNKTR AAAEVGINSE TIVKPASVSE EELLNSIRKL 

       130        140        150        160        170        180 
NNDENVDGLL VQLPLPEHID ERKVCNAVSP DKDVDGFHVI NVGRMCLDQY SMLPATPWGV 

       190        200        210        220        230        240 
WEIIKRTGIP TLGKNVVVAG RSKNVGMPIA MLLHTDGAHE RPGGDATVTI SHRYTPKEQL 

       250        260        270        280        290        300 
KKHTILADIV ISAAGIPNLI TADMIKEGAA VIDVGINRVQ DPVTAKPKLV GDVDFEGVKK 

       310        320        330        340        350 
KAGYITPVPG GVGPMTVAML MKNTIIAAKK VLRPEELEVF KSKQRGVATN 

P18155 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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