SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9WU20

- MTHR_MOUSE

UniProt

Q9WU20 - MTHR_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Methylenetetrahydrofolate reductase
Gene
Mthfr
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

FAD By similarity.

Enzyme regulationi

Allosterically regulated by S-adenosylmethionine By similarity.

Pathwayi

Sites

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

Regions

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

GO - Molecular functioni

  1. methylenetetrahydrofolate reductase (NAD(P)H) activity Source: MGI
Complete GO annotation...

GO - Biological processi

  1. methionine biosynthetic process Source: MGI
  2. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.5.1.15. 3474.
ReactomeiREACT_220137. 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: Chromosome 4

Organism-specific databases

MGIiMGI:106639. Mthfr.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654Methylenetetrahydrofolate reductase
PRO_0000190247Add
BLAST

Proteomic databases

PaxDbiQ9WU20.
PRIDEiQ9WU20.

PTM databases

PhosphoSiteiQ9WU20.

Expressioni

Gene expression databases

ArrayExpressiQ9WU20.
BgeeiQ9WU20.
CleanExiMM_MTHFR.

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9WU20.
SMRiQ9WU20. Positions 59-337.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0685.
GeneTreeiENSGT00390000012490.
HOGENOMiHOG000246234.
HOVERGENiHBG006414.
InParanoidiQ8CDE4.
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

MVNEARGSGS PNPRSEGSSS GSESSKDSSR CSTPSLDPER HERLREKMRR    50
RMDSGDKWFS LEFFPPRTAE GAVNLISRFD RMAAGGPLFV DVTWHPAGDP 100
GSDKETSSMM IASTAVNYCG LETILHMTCC QQRPEEITGH LHRAKQLGLK 150
NIMALRGDPV GDHWEAEEGG FSYATDLVKH IRTEFADYFD ICVAGYPRGH 200
PDAESFEDDL KHLKEKVSAG ADFIITQLFF EASTFFSFVK ACTEIGISCP 250
ILPGIFPIQG YTSLRQLVKL SKLEVPQKIK DVIEPIKDND AAIRNYGIEL 300
AVSLCRELLD SGLVPGLHFY TLNREVATME VLKQLGMWTE DPRRPLPWAL 350
SAHPKRREED VRPIFWASRP KSYIYRTQDW DEFPNGRWGN SSSPAFGELK 400
DYYLFYLKSK SPREELLKMW GEELTSEESV FEVFEHYLSG EPNRHGYRVT 450
CLPWNDEPLA AETSLMKEEL LRVNRLGILT INSQPNINAK PSSDPVVGWG 500
PSGGYVFQKA YLEFFTSRET VEALLQVLKT YELRVNYHIV DVKGENITNA 550
PELQPNAVTW GIFPGREIIQ PTVVDPISFM FWKDEAFALW IEQWGKLYEE 600
ESPSRMIIQY IHDNYFLVNL VDNEFPLDSC LWQVVEDTFE LLNRHPTERE 650
TQAP 654
Length:654
Mass (Da):74,580
Last modified:July 27, 2011 - v2
Checksum:i96E625014D8F4838
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti303 – 3031S → R in AAD20313. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18929.1.
RefSeqi NP_034970.2. NM_010840.3.
UniGenei Mm.89959.

3D structure databases

ProteinModelPortali Q9WU20.
SMRi Q9WU20. Positions 59-337.
ModBasei Search...

PTM databases

PhosphoSitei Q9WU20.

Proteomic databases

PaxDbi Q9WU20.
PRIDEi Q9WU20.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000097788 ; ENSMUSP00000095395 ; ENSMUSG00000029009 .
GeneIDi 17769.
KEGGi mmu:17769.
UCSCi uc008vtu.2. mouse.

Organism-specific databases

CTDi 4524.
MGIi MGI:106639. Mthfr.

Phylogenomic databases

eggNOGi COG0685.
GeneTreei ENSGT00390000012490.
HOGENOMi HOG000246234.
HOVERGENi HBG006414.
InParanoidi Q8CDE4.
KOi K00297.
OrthoDBi EOG7TF7B4.

Enzyme and pathway databases

UniPathwayi UPA00193 .
BRENDAi 1.5.1.15. 3474.
Reactomei REACT_220137. Metabolism of folate and pterines.

Miscellaneous databases

NextBioi 292481.
PROi Q9WU20.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9WU20.
Bgeei Q9WU20.
CleanExi MM_MTHFR.

Family and domain databases

Gene3Di 3.20.20.220. 1 hit.
InterProi IPR029041. FAD-linked_oxidoreductase-like.
IPR004621. Fadh2_euk.
IPR003171. Mehydrof_redctse.
[Graphical view ]
Pfami PF02219. MTHFR. 1 hit.
[Graphical view ]
SUPFAMi SSF51730. SSF51730. 1 hit.
TIGRFAMsi TIGR00677. fadh2_euk. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 98 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