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Q3V3R1

- C1TM_MOUSE

UniProt

Q3V3R1 - C1TM_MOUSE

Protein

Monofunctional C1-tetrahydrofolate synthase, mitochondrial

Gene

Mthfd1l

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (01 Jul 2008)
      Previous versions | rss
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    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.

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi422 – 4298ATPBy 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

    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

    GO - Cellular componenti

    1. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3131MitochondrionSequence AnalysisAdd
    BLAST
    Chaini32 – 977946Monofunctional C1-tetrahydrofolate synthase, mitochondrialPRO_0000343178Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei188 – 1881N6-acetyllysine; alternateBy 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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ3V3R1.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni32 – 347316Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd
    BLAST
    Regioni348 – 977630Formyltetrahydrofolate synthetaseAdd
    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.

    Sequence similaritiesi

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

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371D → N in BAE35568. (PubMed:16141072)Curated
    Sequence conflicti279 – 2791V → A in BAE35568. (PubMed:16141072)Curated
    Sequence conflicti279 – 2791V → A in AAH30437. (PubMed:15489334)Curated
    Sequence conflicti279 – 2791V → A in AAH49936. (PubMed:15489334)Curated
    Sequence conflicti353 – 3531Q → H in BAE35568. (PubMed:16141072)Curated
    Sequence conflicti369 – 3691T → N in BAE20500. (PubMed:16141072)Curated
    Sequence conflicti419 – 4191I → V in BAC30053. (PubMed:16141072)Curated
    Sequence conflicti422 – 4221T → S in BAE35568. (PubMed:16141072)Curated
    Sequence conflicti632 – 6321V → A in BAE35568. (PubMed:16141072)Curated
    Sequence conflicti963 – 9631D → G in BAE20438. (PubMed:16141072)Curated

    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

    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: October 1, 2014
    This is version 77 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