C1TC_MOUSE
ID C1TC_MOUSE Reviewed; 935 AA.
AC Q922D8; Q8R013;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic {ECO:0000305|PubMed:15611115};
DE Short=C1-THF synthase;
DE Includes:
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000305|PubMed:15611115};
DE EC=1.5.1.5 {ECO:0000269|PubMed:15611115};
DE Includes:
DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000250|UniProtKB:P11586};
DE EC=3.5.4.9 {ECO:0000250|UniProtKB:P11586};
DE Includes:
DE RecName: Full=Formyltetrahydrofolate synthetase {ECO:0000305|PubMed:15611115};
DE EC=6.3.4.3 {ECO:0000269|PubMed:15611115};
DE Contains:
DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processed;
GN Name=Mthfd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ;
RX PubMed=12061812; DOI=10.1016/s0003-9861(02)00203-5;
RA Patel H., Christensen K.E., Mejia N., MacKenzie R.E.;
RT "Mammalian mitochondrial methylenetetrahydrofolate dehydrogenase-
RT cyclohydrolase derived from a trifunctional methylenetetrahydrofolate
RT dehydrogenase-cyclohydrolase-synthetase.";
RL Arch. Biochem. Biophys. 403:145-148(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-17; 27-56; 59-66; 75-83; 123-134; 138-173; 176-198;
RP 205-223; 251-262; 314-324; 330-352; 355-362; 371-402; 464-473; 488-495;
RP 505-517; 521-532; 543-553; 658-679; 687-702; 706-733; 747-772; 776-784;
RP 805-819; 833-848 AND 855-889, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=15611115; DOI=10.1074/jbc.m409380200;
RA Christensen K.E., Patel H., Kuzmanov U., Mejia N.R., MacKenzie R.E.;
RT "Disruption of the mthfd1 gene reveals a monofunctional 10-
RT formyltetrahydrofolate synthetase in mammalian mitochondria.";
RL J. Biol. Chem. 280:7597-7602(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Trifunctional enzyme that catalyzes the interconversion of
CC three forms of one-carbon-substituted tetrahydrofolate: (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate, 5,10-methenyltetrahydrofolate and
CC (6S)-10-formyltetrahydrofolate. These derivatives of tetrahydrofolate
CC are differentially required in nucleotide and amino acid biosynthesis,
CC (6S)-10-formyltetrahydrofolate being required for purine biosynthesis
CC while (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate is used for serine
CC and methionine biosynthesis for instance.
CC {ECO:0000269|PubMed:15611115}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-
CC methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.5;
CC Evidence={ECO:0000269|PubMed:15611115};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methenyltetrahydrofolate + H2O = (6S)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:57455; EC=3.5.4.9;
CC Evidence={ECO:0000250|UniProtKB:P11586};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-
CC formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC Evidence={ECO:0000269|PubMed:15611115};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000269|PubMed:15611115}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15611115}.
CC -!- DOMAIN: The N-terminal methylenetetrahydrofolate dehydrogenase and
CC methenyltetrahydrofolate cyclohydrolase (D/C) domain carries both the
CC methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate
CC cyclohydrolase activities. {ECO:0000250|UniProtKB:P11586}.
CC -!- DOMAIN: The larger C-terminal formyltetrahydrofolate synthetase domain
CC carries a third formyltetrahydrofolate synthetase activity.
CC {ECO:0000250|UniProtKB:P11586}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the formate--
CC tetrahydrofolate ligase family. {ECO:0000305}.
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DR EMBL; AF364579; AAL99692.1; -; mRNA.
DR EMBL; AF364591; AAL99693.1; -; Genomic_DNA.
DR EMBL; AF364580; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AF364581; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AF364582; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AF364583; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AF364584; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AF364585; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AF364586; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AF364587; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AF364588; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AF364589; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AF364590; AAL99693.1; JOINED; Genomic_DNA.
DR EMBL; AK088700; BAC40513.1; -; mRNA.
DR EMBL; BC008523; AAH08523.1; -; mRNA.
DR CCDS; CCDS25990.1; -.
DR RefSeq; NP_620084.2; NM_138745.2.
DR AlphaFoldDB; Q922D8; -.
DR SMR; Q922D8; -.
DR BioGRID; 223871; 20.
DR IntAct; Q922D8; 3.
DR MINT; Q922D8; -.
DR STRING; 10090.ENSMUSP00000021443; -.
DR ChEMBL; CHEMBL3137; -.
DR iPTMnet; Q922D8; -.
DR PhosphoSitePlus; Q922D8; -.
DR SwissPalm; Q922D8; -.
DR REPRODUCTION-2DPAGE; Q922D8; -.
DR EPD; Q922D8; -.
DR jPOST; Q922D8; -.
DR MaxQB; Q922D8; -.
DR PaxDb; Q922D8; -.
DR PeptideAtlas; Q922D8; -.
DR PRIDE; Q922D8; -.
DR ProteomicsDB; 273855; -.
DR Antibodypedia; 52; 181 antibodies from 30 providers.
DR DNASU; 108156; -.
DR Ensembl; ENSMUST00000021443; ENSMUSP00000021443; ENSMUSG00000021048.
DR GeneID; 108156; -.
DR KEGG; mmu:108156; -.
DR UCSC; uc007nxz.2; mouse.
DR CTD; 4522; -.
DR MGI; MGI:1342005; Mthfd1.
DR VEuPathDB; HostDB:ENSMUSG00000021048; -.
DR eggNOG; KOG4230; Eukaryota.
DR GeneTree; ENSGT00940000154746; -.
DR HOGENOM; CLU_003601_2_0_1; -.
DR InParanoid; Q922D8; -.
DR OMA; KVDTYTK; -.
DR OrthoDB; 690393at2759; -.
DR PhylomeDB; Q922D8; -.
DR TreeFam; TF300623; -.
DR BRENDA; 6.3.4.3; 3474.
DR Reactome; R-MMU-196757; Metabolism of folate and pterines.
DR UniPathway; UPA00193; -.
DR BioGRID-ORCS; 108156; 23 hits in 75 CRISPR screens.
DR ChiTaRS; Mthfd1; mouse.
DR PRO; PR:Q922D8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q922D8; protein.
DR Bgee; ENSMUSG00000021048; Expressed in paneth cell and 283 other tissues.
DR ExpressionAtlas; Q922D8; baseline and differential.
DR Genevisible; Q922D8; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IMP:UniProtKB.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; ISS:UniProtKB.
DR GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; IDA:BHF-UCL.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IMP:UniProtKB.
DR GO; GO:0004486; F:methylenetetrahydrofolate dehydrogenase [NAD(P)+] activity; ISO:MGI.
DR GO; GO:0009257; P:10-formyltetrahydrofolate biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0007507; P:heart development; IMP:BHF-UCL.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; ISO:MGI.
DR GO; GO:0006555; P:methionine metabolic process; IMP:BHF-UCL.
DR GO; GO:0001843; P:neural tube closure; IMP:BHF-UCL.
DR GO; GO:0001780; P:neutrophil homeostasis; IMP:BHF-UCL.
DR GO; GO:0006730; P:one-carbon metabolic process; ISO:MGI.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0009152; P:purine ribonucleotide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009070; P:serine family amino acid biosynthetic process; ISO:MGI.
DR GO; GO:0009069; P:serine family amino acid metabolic process; IMP:BHF-UCL.
DR GO; GO:0061053; P:somite development; IMP:BHF-UCL.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IMP:BHF-UCL.
DR GO; GO:0019346; P:transsulfuration; IMP:BHF-UCL.
DR CDD; cd00477; FTHFS; 1.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01543; FTHFS; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR000559; Formate_THF_ligase.
DR InterPro; IPR020628; Formate_THF_ligase_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR Pfam; PF01268; FTHFS; 1.
DR Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00721; FTHFS_1; 1.
DR PROSITE; PS00722; FTHFS_2; 1.
DR PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Histidine biosynthesis; Hydrolase; Ligase;
KW Methionine biosynthesis; Multifunctional enzyme; NADP; Nucleotide-binding;
KW One-carbon metabolism; Oxidoreductase; Phosphoprotein; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..935
FT /note="C-1-tetrahydrofolate synthase, cytoplasmic"
FT /id="PRO_0000199322"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT CHAIN 2..935
FT /note="C-1-tetrahydrofolate synthase, cytoplasmic, N-
FT terminally processed"
FT /id="PRO_0000423281"
FT REGION 2..291
FT /note="Methylenetetrahydrofolate dehydrogenase and
FT methenyltetrahydrofolate cyclohydrolase (D/C) domain"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT REGION 310..935
FT /note="Formyltetrahydrofolate synthetase domain"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT ACT_SITE 56
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT BINDING 52..56
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT BINDING 99..101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT BINDING 172..174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT BINDING 197
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT BINDING 272..276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT BINDING 380..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11586"
FT CONFLICT 365
FT /note="H -> Y (in Ref. 3; AAH08523)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="A -> T (in Ref. 3; AAH08523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 935 AA; 101200 MW; 0EB92D58C78DDEB5 CRC64;
MAPAGILNGK LVSAQIRDRL KNQVTRMQEQ VPGFTPGLAI LQVGDRDDSN LYINVKLKAA
EEIGIKATHI KLPRTSTESE VLKYVISLNE DASVHGFIVQ LPLDSENSIN TEAVINAIAP
EKDVDGLTSV SAGKLARGDL NDCFIPCTPK GCLELIKEAG VQIAGRHAVV VGRSKIVGAP
MHDLLLWNNA TVTTCHSKTA NLDKEVNKGD ILVVATGQPE MVKGEWIKPG AVVIDCGINY
VPDDTKPNGR KVVGDVAYDE AKERASFITP VPGGVGPMTV AMLMQSTVES AQRFLQKFKP
GKWTIQYNKL NLKTPVPSDI AISRSCKPKL IGNLAREIGL LTEEVELYGE TKAKVLLSAL
DRLKHQPDGK YVVVTGITPT PLGEGKSTTT IGLVQALGAH LRQNVFACVR QPSQGPTFGI
KGGAAGGGYS QVIPMEEFNL HLTGDIHAIT AANNLVAAAI DARIFHELTQ TDKALFNRLV
PSVNGIRKFS DIQIRRLRRL GIEKTDPTTL TDDEINRFAR LDIDPETITW QRVLDTNDRF
LRKITIGQSP TEKGHTRTAQ FDISVASEIM AVLALTSSLE DMRERLGRMV VASSKKGEPI
SCEDLGVSGA LTVLMKDAIK PNLMQTLEGT PVFVHAGPFA NIAHGNSSII ADRIALKLVG
PEGFVVTEAG FGADIGMEKF FNIKCRYSGL QPHVVVLVAT VRALKMHGGG PTVTAGLPLP
KAYTEEDLDL VEKGFSNLRK QIENARMFGV PVVVAVNVFK TDTDAELDLV SRLSREHGAF
DAVKCTHWAE GGQGALALAQ AVQRASQAPS SFQLLYDLKL SIEDKIRIIA QRIYGADDIE
LLPEAQNKAE IYTKQGFGNL PICMAKTHLS LSHNPEQKGV PTGFVLPIRD IRASVGAGFL
YPLVGTMSTM PGLPTRPCFY DIDLDPETEQ VNGLF
