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Q3V3R1

- C1TM_MOUSE

UniProt

Q3V3R1 - C1TM_MOUSE

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Protein

Monofunctional C1-tetrahydrofolate synthase, mitochondrial

Gene
Mthfd1l, Fthfsdc1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2.1 Publication

Catalytic activityi

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.UniRule annotation

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi422 – 4298ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. formate-tetrahydrofolate ligase activity Source: MGI
  3. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: InterPro

GO - Biological processi

  1. 10-formyltetrahydrofolate biosynthetic process Source: MGI
  2. formate metabolic process Source: Ensembl
  3. one-carbon metabolic process Source: RefGenome
  4. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Monofunctional C1-tetrahydrofolate synthase, mitochondrial (EC:6.3.4.3)
Alternative name(s):
Formyltetrahydrofolate synthetase
Gene namesi
Name:Mthfd1l
Synonyms:Fthfsdc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1924836. Mthfd1l.

Subcellular locationi

Mitochondrion By similarity UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3131Mitochondrion Reviewed predictionAdd
BLAST
Chaini32 – 977946Monofunctional C1-tetrahydrofolate synthase, mitochondrialUniRule annotationPRO_0000343178Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881N6-acetyllysine; alternate By similarity
Modified residuei188 – 1881N6-succinyllysine; alternate1 Publication
Modified residuei595 – 5951N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ3V3R1.
PaxDbiQ3V3R1.
PRIDEiQ3V3R1.

2D gel databases

REPRODUCTION-2DPAGEQ3V3R1.

PTM databases

PhosphoSiteiQ3V3R1.

Expressioni

Gene expression databases

BgeeiQ3V3R1.
GenevestigatoriQ3V3R1.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi234813. 2 interactions.
IntActiQ3V3R1. 4 interactions.
MINTiMINT-4114903.
STRINGi10090.ENSMUSP00000101210.

Structurei

Secondary structure

1
977
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi514 – 5218
Beta strandi525 – 5284
Helixi533 – 54210
Turni549 – 5513
Helixi554 – 5629

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EO2NMR-A510-573[»]
ProteinModelPortaliQ3V3R1.
SMRiQ3V3R1. Positions 82-290, 358-977.

Miscellaneous databases

EvolutionaryTraceiQ3V3R1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 347316Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseUniRule annotationAdd
BLAST
Regioni348 – 977630Formyltetrahydrofolate synthetaseUniRule annotationAdd
BLAST

Domaini

This monofunctional enzyme consists of two major domains: an N-terminal inactive methylene-THF dehydrogenase and cyclohydrolase domain and an active larger formyl-THF synthetase C-terminal domain.UniRule annotation

Sequence similaritiesi

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0190.
GeneTreeiENSGT00750000117401.
HOGENOMiHOG000040280.
HOVERGENiHBG004916.
InParanoidiQ3V3R1.
KOiK13402.
OMAiVNGVREF.
OrthoDBiEOG76T9QN.
PhylomeDBiQ3V3R1.
TreeFamiTF300623.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.720. 2 hits.
HAMAPiMF_01543. FTHFS.
InterProiIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3V3R1-1 [UniParc]FASTAAdd to Basket

« Hide

MSVRLPLLLR QLGRQQLPSG PACRLRELCR SGSRSSSSGG GDPEGLRGRR    50
LQDGQTFSSH GPGNPEAPGM DSIVRDVIHN SKEVLSLLQE KNPAFKPVLV 100
VIQAGDDNLM KDMNQNLAKE AGLDITHICL PPDSGEDEII DEILKINEDP 150
RVHGLTLQIS EDSLSNKVLN ALKPEKDVDG VTDINLGKLV RGDAPECFVS 200
PLAKAAVELV EKSGITLDGK KVLVVGAHGP LEAALQWLFQ RKGSMTMSCP 250
WATPQLPDKL READIVVLGS PKPEEIPAVW IPSGTTILNC FHDFLSGKLS 300
GGSPGVPVDK LIAEESVSLL AAALRIQNMV SSGRRWLREQ QHRRWRLHCL 350
KLQPLSPVPS DIEISRGQTP KAVDVLAKEI GLLADEIEIY GKSKAKVQLS 400
LLERLKDQTD GKYVLVAGIT PTPLGEGKST VTIGLVQALT AHLKVNSFAC 450
LRQPSQGPTF GVKGGAAGGG YAQVIPMEEF NLHLTGDIHA ITAANNLLAA 500
AIDTRILHES TQTDKALYNR LVPLVNGVRE FSEIQLSRLK KLGIHKTDPS 550
TLTEEEVRKF ARLNIDPATI TWQRVLDTND RFLRKITIGQ GSTEKGYSRQ 600
AQFDIAVASE IMAVLALTDS LTDMKERLGR MVVASDKDGQ PVTAEDLGVT 650
GALTVLMKDA IKPNLMQTLE GTPVFVHAGP FANIAHGNSS VLADKIALKL 700
VGEEGFVVTE AGFGADIGME KFFNIKCRAS GLVPNVVVLV ATVRALKMHG 750
GGPSVTAGVP LKKEYTEENI QLVADGCCNL QKQIQIAQLF GVPVVVALNV 800
FKTDTRAEID LVCELAKRAG AFDAVPCYHW SAGGKGSVDL ARAVREAANK 850
RSRFQFLYDV QLPIVEKIRV IAQTVYGAKD IELSPEAQSK IDRYTQQGFG 900
NLPICMAKTH LSLSHEPDKK GVPRDFTLPI SDVRASIGAG FIYPLVGTMS 950
TMPGLPTRPC FYDIDLDTET EQVKGLF 977
Length:977
Mass (Da):105,729
Last modified:July 1, 2008 - v2
Checksum:i7275EF6F9A4292D6
GO

Sequence cautioni

The sequence AAH30437.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371D → N in BAE35568. 1 Publication
Sequence conflicti279 – 2791V → A in BAE35568. 1 Publication
Sequence conflicti279 – 2791V → A in AAH30437. 1 Publication
Sequence conflicti279 – 2791V → A in AAH49936. 1 Publication
Sequence conflicti353 – 3531Q → H in BAE35568. 1 Publication
Sequence conflicti369 – 3691T → N in BAE20500. 1 Publication
Sequence conflicti419 – 4191I → V in BAC30053. 1 Publication
Sequence conflicti422 – 4221T → S in BAE35568. 1 Publication
Sequence conflicti632 – 6321V → A in BAE35568. 1 Publication
Sequence conflicti963 – 9631D → G in BAE20438. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK038579 mRNA. Translation: BAC30053.1.
AK028211 mRNA. Translation: BAE20438.1.
AK036284 mRNA. Translation: BAE20500.1.
AK160025 mRNA. Translation: BAE35568.1.
BC030437 mRNA. Translation: AAH30437.1. Different initiation.
BC049936 mRNA. Translation: AAH49936.1.
CCDSiCCDS56672.1.
RefSeqiNP_001164256.1. NM_001170785.1.
NP_001164257.1. NM_001170786.1.
NP_758512.3. NM_172308.4.
UniGeneiMm.184752.

Genome annotation databases

EnsembliENSMUST00000043735; ENSMUSP00000036178; ENSMUSG00000040675.
ENSMUST00000117291; ENSMUSP00000112870; ENSMUSG00000040675.
ENSMUST00000120585; ENSMUSP00000112897; ENSMUSG00000040675.
GeneIDi270685.
KEGGimmu:270685.
UCSCiuc007ehj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK038579 mRNA. Translation: BAC30053.1 .
AK028211 mRNA. Translation: BAE20438.1 .
AK036284 mRNA. Translation: BAE20500.1 .
AK160025 mRNA. Translation: BAE35568.1 .
BC030437 mRNA. Translation: AAH30437.1 . Different initiation.
BC049936 mRNA. Translation: AAH49936.1 .
CCDSi CCDS56672.1.
RefSeqi NP_001164256.1. NM_001170785.1.
NP_001164257.1. NM_001170786.1.
NP_758512.3. NM_172308.4.
UniGenei Mm.184752.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EO2 NMR - A 510-573 [» ]
ProteinModelPortali Q3V3R1.
SMRi Q3V3R1. Positions 82-290, 358-977.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 234813. 2 interactions.
IntActi Q3V3R1. 4 interactions.
MINTi MINT-4114903.
STRINGi 10090.ENSMUSP00000101210.

PTM databases

PhosphoSitei Q3V3R1.

2D gel databases

REPRODUCTION-2DPAGE Q3V3R1.

Proteomic databases

MaxQBi Q3V3R1.
PaxDbi Q3V3R1.
PRIDEi Q3V3R1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000043735 ; ENSMUSP00000036178 ; ENSMUSG00000040675 .
ENSMUST00000117291 ; ENSMUSP00000112870 ; ENSMUSG00000040675 .
ENSMUST00000120585 ; ENSMUSP00000112897 ; ENSMUSG00000040675 .
GeneIDi 270685.
KEGGi mmu:270685.
UCSCi uc007ehj.2. mouse.

Organism-specific databases

CTDi 25902.
MGIi MGI:1924836. Mthfd1l.

Phylogenomic databases

eggNOGi COG0190.
GeneTreei ENSGT00750000117401.
HOGENOMi HOG000040280.
HOVERGENi HBG004916.
InParanoidi Q3V3R1.
KOi K13402.
OMAi VNGVREF.
OrthoDBi EOG76T9QN.
PhylomeDBi Q3V3R1.
TreeFami TF300623.

Enzyme and pathway databases

UniPathwayi UPA00193 .

Miscellaneous databases

ChiTaRSi MTHFD1L. mouse.
EvolutionaryTracei Q3V3R1.
NextBioi 393373.
PROi Q3V3R1.
SOURCEi Search...

Gene expression databases

Bgeei Q3V3R1.
Genevestigatori Q3V3R1.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
3.40.50.720. 2 hits.
HAMAPi MF_01543. FTHFS.
InterProi IPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view ]
Pfami PF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view ]
PRINTSi PR00085. THFDHDRGNASE.
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: Cerebellum and Hypothalamus.
  2. "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] OF 167-977.
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  3. "Disruption of the mthfd1 gene reveals a monofunctional 10-formyltetrahydrofolate synthetase in mammalian mitochondria."
    Christensen K.E., Patel H., Kuzmanov U., Mejia N.R., MacKenzie R.E.
    J. Biol. Chem. 280:7597-7602(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-188 AND LYS-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  5. "Solution structure of the insertion region (510-573) of FTHFS domain from mouse methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1-like protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 510-573.

Entry informationi

Entry nameiC1TM_MOUSE
AccessioniPrimary (citable) accession number: Q3V3R1
Secondary accession number(s): Q3TVQ0
, Q3V402, Q80V98, Q8CAL0, Q8K2N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: July 9, 2014
This is version 76 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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