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Protein

Methylenetetrahydrofolate reductase

Gene

Mthfr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co-substrate for homocysteine remethylation to methionine.

Catalytic activityi

5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H.

Cofactori

FADBy similarity

Enzyme regulationi

Allosterically regulated by S-adenosylmethionine.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei62 – 621Proton donor/acceptorBy similarity
Binding sitei126 – 1261FADBy similarity
Binding sitei158 – 1581SubstrateBy similarity
Binding sitei196 – 1961FADBy similarity
Binding sitei209 – 2091FADBy similarity
Binding sitei216 – 2161FADBy similarity
Binding sitei227 – 2271SubstrateBy similarity
Binding sitei320 – 3201SubstrateBy similarity
Binding sitei324 – 3241SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi62 – 676NADBy similarity
Nucleotide bindingi93 – 942NAD and FADBy similarity
Nucleotide bindingi156 – 1583FADBy similarity
Nucleotide bindingi173 – 1742FADBy similarity
Nucleotide bindingi200 – 2034FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.5.1.15. 3474.
1.5.1.20. 3474.
ReactomeiREACT_300004. Metabolism of folate and pterines.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylenetetrahydrofolate reductase (EC:1.5.1.20)
Gene namesi
Name:Mthfr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:106639. Mthfr.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654Methylenetetrahydrofolate reductasePRO_0000190247Add
BLAST

Proteomic databases

MaxQBiQ9WU20.
PaxDbiQ9WU20.
PRIDEiQ9WU20.

PTM databases

PhosphoSiteiQ9WU20.

Expressioni

Gene expression databases

BgeeiQ9WU20.
CleanExiMM_MTHFR.
ExpressionAtlasiQ9WU20. baseline and differential.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9WU20.
SMRiQ9WU20. Positions 59-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0685.
GeneTreeiENSGT00390000012490.
HOGENOMiHOG000246234.
HOVERGENiHBG006414.
InParanoidiQ9WU20.
KOiK00297.
OrthoDBiEOG7TF7B4.

Family and domain databases

Gene3Di3.20.20.220. 1 hit.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR004621. Fadh2_euk.
IPR003171. Mehydrof_redctse.
[Graphical view]
PfamiPF02219. MTHFR. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 1 hit.
TIGRFAMsiTIGR00677. fadh2_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9WU20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNEARGSGS PNPRSEGSSS GSESSKDSSR CSTPSLDPER HERLREKMRR
60 70 80 90 100
RMDSGDKWFS LEFFPPRTAE GAVNLISRFD RMAAGGPLFV DVTWHPAGDP
110 120 130 140 150
GSDKETSSMM IASTAVNYCG LETILHMTCC QQRPEEITGH LHRAKQLGLK
160 170 180 190 200
NIMALRGDPV GDHWEAEEGG FSYATDLVKH IRTEFADYFD ICVAGYPRGH
210 220 230 240 250
PDAESFEDDL KHLKEKVSAG ADFIITQLFF EASTFFSFVK ACTEIGISCP
260 270 280 290 300
ILPGIFPIQG YTSLRQLVKL SKLEVPQKIK DVIEPIKDND AAIRNYGIEL
310 320 330 340 350
AVSLCRELLD SGLVPGLHFY TLNREVATME VLKQLGMWTE DPRRPLPWAL
360 370 380 390 400
SAHPKRREED VRPIFWASRP KSYIYRTQDW DEFPNGRWGN SSSPAFGELK
410 420 430 440 450
DYYLFYLKSK SPREELLKMW GEELTSEESV FEVFEHYLSG EPNRHGYRVT
460 470 480 490 500
CLPWNDEPLA AETSLMKEEL LRVNRLGILT INSQPNINAK PSSDPVVGWG
510 520 530 540 550
PSGGYVFQKA YLEFFTSRET VEALLQVLKT YELRVNYHIV DVKGENITNA
560 570 580 590 600
PELQPNAVTW GIFPGREIIQ PTVVDPISFM FWKDEAFALW IEQWGKLYEE
610 620 630 640 650
ESPSRMIIQY IHDNYFLVNL VDNEFPLDSC LWQVVEDTFE LLNRHPTERE

TQAP
Length:654
Mass (Da):74,580
Last modified:July 27, 2011 - v2
Checksum:i96E625014D8F4838
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti303 – 3031S → R in AAD20313 (PubMed:9680386).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF105998
, AF105988, AF105989, AF105990, AF105991, AF105992, AF105993, AF105994, AF105995, AF105996, AF105997 Genomic DNA. Translation: AAD20313.1.
AK030192 mRNA. Translation: BAC26832.1.
AL606929 Genomic DNA. Translation: CAM14896.1.
CH466594 Genomic DNA. Translation: EDL14794.1.
CH466594 Genomic DNA. Translation: EDL14796.1.
CH466594 Genomic DNA. Translation: EDL14797.1.
BC051017 mRNA. Translation: AAH51017.1.
BC052466 mRNA. Translation: AAH52466.1.
CCDSiCCDS18929.1.
RefSeqiNP_034970.2. NM_010840.3.
UniGeneiMm.89959.

Genome annotation databases

EnsembliENSMUST00000097788; ENSMUSP00000095395; ENSMUSG00000029009.
GeneIDi17769.
KEGGimmu:17769.
UCSCiuc008vtu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF105998
, AF105988, AF105989, AF105990, AF105991, AF105992, AF105993, AF105994, AF105995, AF105996, AF105997 Genomic DNA. Translation: AAD20313.1.
AK030192 mRNA. Translation: BAC26832.1.
AL606929 Genomic DNA. Translation: CAM14896.1.
CH466594 Genomic DNA. Translation: EDL14794.1.
CH466594 Genomic DNA. Translation: EDL14796.1.
CH466594 Genomic DNA. Translation: EDL14797.1.
BC051017 mRNA. Translation: AAH51017.1.
BC052466 mRNA. Translation: AAH52466.1.
CCDSiCCDS18929.1.
RefSeqiNP_034970.2. NM_010840.3.
UniGeneiMm.89959.

3D structure databases

ProteinModelPortaliQ9WU20.
SMRiQ9WU20. Positions 59-337.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9WU20.

Proteomic databases

MaxQBiQ9WU20.
PaxDbiQ9WU20.
PRIDEiQ9WU20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000097788; ENSMUSP00000095395; ENSMUSG00000029009.
GeneIDi17769.
KEGGimmu:17769.
UCSCiuc008vtu.2. mouse.

Organism-specific databases

CTDi4524.
MGIiMGI:106639. Mthfr.

Phylogenomic databases

eggNOGiCOG0685.
GeneTreeiENSGT00390000012490.
HOGENOMiHOG000246234.
HOVERGENiHBG006414.
InParanoidiQ9WU20.
KOiK00297.
OrthoDBiEOG7TF7B4.

Enzyme and pathway databases

UniPathwayiUPA00193.
BRENDAi1.5.1.15. 3474.
1.5.1.20. 3474.
ReactomeiREACT_300004. Metabolism of folate and pterines.

Miscellaneous databases

ChiTaRSiMthfr. mouse.
NextBioi292481.
PROiQ9WU20.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WU20.
CleanExiMM_MTHFR.
ExpressionAtlasiQ9WU20. baseline and differential.

Family and domain databases

Gene3Di3.20.20.220. 1 hit.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR004621. Fadh2_euk.
IPR003171. Mehydrof_redctse.
[Graphical view]
PfamiPF02219. MTHFR. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 1 hit.
TIGRFAMsiTIGR00677. fadh2_euk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene structure of human and mouse methylenetetrahydrofolate reductase (MTHFR)."
    Goyette P., Pai A., Milos R., Frosst P., Tran P., Chen Z., Chan M., Rozen R.
    Mamm. Genome 9:652-656(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain and Olfactory epithelium.

Entry informationi

Entry nameiMTHR_MOUSE
AccessioniPrimary (citable) accession number: Q9WU20
Secondary accession number(s): Q8CDE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: May 27, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.