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Q8R123

- FAD1_MOUSE

UniProt

Q8R123 - FAD1_MOUSE

Protein

FAD synthase

Gene

Flad1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.By similarity

    Catalytic activityi

    ATP + FMN = diphosphate + FAD.

    Cofactori

    Magnesium.By similarity

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. FMN adenylyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. FAD biosynthetic process Source: UniProtKB-UniPathway
    2. Mo-molybdopterin cofactor biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_216155. Vitamin B2 (riboflavin) metabolism.
    UniPathwayiUPA00277; UER00407.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FAD synthase (EC:2.7.7.2)
    Alternative name(s):
    FAD pyrophosphorylase
    FMN adenylyltransferase
    Flavin adenine dinucleotide synthase
    Including the following 2 domains:
    Molybdenum cofactor biosynthesis protein-like region
    FAD synthase region
    Gene namesi
    Name:Flad1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:2443030. Flad1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 492492FAD synthasePRO_0000302738Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei283 – 2831N6-acetyllysine; alternate1 Publication
    Modified residuei283 – 2831N6-succinyllysine; alternate1 Publication
    Modified residuei468 – 4681PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8R123.
    PaxDbiQ8R123.
    PRIDEiQ8R123.

    PTM databases

    PhosphoSiteiQ8R123.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8R123.
    BgeeiQ8R123.
    GenevestigatoriQ8R123.

    Interactioni

    Protein-protein interaction databases

    IntActiQ8R123. 1 interaction.
    MINTiMINT-4118484.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R123.
    SMRiQ8R123. Positions 18-174, 264-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 11092Molybdenum cofactor biosynthesis protein-likeAdd
    BLAST
    Regioni303 – 460158FAD synthaseAdd
    BLAST

    Domaini

    The molybdenum cofactor biosynthesis protein-like region may not be functional.

    Sequence similaritiesi

    In the N-terminal section; belongs to the MoaB/Mog family.Curated
    In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0175.
    GeneTreeiENSGT00390000007266.
    HOGENOMiHOG000007185.
    HOVERGENiHBG058211.
    KOiK00953.
    OMAiSFMRINP.
    OrthoDBiEOG7C5M9F.
    PhylomeDBiQ8R123.
    TreeFamiTF314056.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    3.40.980.10. 1 hit.
    InterProiIPR012183. FAD_synth_Mopterin-bd.
    IPR001453. Mopterin-bd_dom.
    IPR002500. PAPS_reduct.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00994. MoCF_biosynth. 1 hit.
    PF01507. PAPS_reduct. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036620. MPTbdFAD. 1 hit.
    SMARTiSM00852. MoCF_biosynth. 1 hit.
    [Graphical view]
    SUPFAMiSSF53218. SSF53218. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8R123-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASRASELPP GSGRSVTAGI IIVGDEILKG HTQDTNTYFL CRTLRSLGVQ    50
    VCRVSVVPDE VATIASEVNS FSRRFTHVLT AGGIGPTHDD VTFEAVAQAF 100
    GEELKPHPEL QAAIKTLGGE GWEKLSMVPS SARLHYGTDP RTGHPFRFPL 150
    VSVRNVYLFP GIPELLRRVL EGLKGLFQNT AVQFHLKELY VAASEGSIAP 200
    ILSEAQAHFG RRLSLGSYPD WSSNYFQVKL ILDSEEKEPL EECLAYLTAR 250
    LPQGSLVPYQ PDAVEKAGEA VYKLAESGSC LGKKVAGALQ TIETALAQYH 300
    LSQLCVGFNG GKDCTALLHL FHAAVQRKFP DVPKPLQILY IRSISPFPEL 350
    EQFLQDTIKR YNLQVLEAEG NMKQALGELQ EKHPQLEAVL MGTRRTDPYS 400
    CSLSHFSPTD PGWPSFMRIN PLLDWTYRNI WEFLRQLFVP YCILYDRGYT 450
    SLGSRENTTQ NPALKCLSPG GHPVYRPAYL LENEDEERNS RM 492
    Length:492
    Mass (Da):54,766
    Last modified:June 1, 2002 - v1
    Checksum:i75008DD249A7F43E
    GO
    Isoform 2 (identifier: Q8R123-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         492-492: M → IPKTPGASWPSPRMGHKELKKEPRTLL

    Show »
    Length:518
    Mass (Da):57,673
    Checksum:iBE331637181B8654
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731R → S in BAE36639. (PubMed:16141072)Curated
    Sequence conflicti390 – 3901L → Q in BAE36639. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei492 – 4921M → IPKTPGASWPSPRMGHKELK KEPRTLL in isoform 2. 1 PublicationVSP_027955

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK044501 mRNA. Translation: BAC31952.1.
    AK161929 mRNA. Translation: BAE36639.1.
    BC009152 mRNA. Translation: AAH09152.2.
    BC025817 mRNA. Translation: AAH25817.1.
    BC046769 mRNA. Translation: AAH46769.1.
    CCDSiCCDS38492.1. [Q8R123-1]
    RefSeqiNP_796015.2. NM_177041.3. [Q8R123-1]
    UniGeneiMm.258142.

    Genome annotation databases

    EnsembliENSMUST00000050398; ENSMUSP00000051366; ENSMUSG00000042642. [Q8R123-2]
    ENSMUST00000107426; ENSMUSP00000103049; ENSMUSG00000042642. [Q8R123-1]
    ENSMUST00000129308; ENSMUSP00000122252; ENSMUSG00000042642. [Q8R123-1]
    GeneIDi319945.
    KEGGimmu:319945.
    UCSCiuc008pzh.2. mouse. [Q8R123-2]
    uc008pzi.1. mouse. [Q8R123-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK044501 mRNA. Translation: BAC31952.1 .
    AK161929 mRNA. Translation: BAE36639.1 .
    BC009152 mRNA. Translation: AAH09152.2 .
    BC025817 mRNA. Translation: AAH25817.1 .
    BC046769 mRNA. Translation: AAH46769.1 .
    CCDSi CCDS38492.1. [Q8R123-1 ]
    RefSeqi NP_796015.2. NM_177041.3. [Q8R123-1 ]
    UniGenei Mm.258142.

    3D structure databases

    ProteinModelPortali Q8R123.
    SMRi Q8R123. Positions 18-174, 264-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8R123. 1 interaction.
    MINTi MINT-4118484.

    PTM databases

    PhosphoSitei Q8R123.

    Proteomic databases

    MaxQBi Q8R123.
    PaxDbi Q8R123.
    PRIDEi Q8R123.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000050398 ; ENSMUSP00000051366 ; ENSMUSG00000042642 . [Q8R123-2 ]
    ENSMUST00000107426 ; ENSMUSP00000103049 ; ENSMUSG00000042642 . [Q8R123-1 ]
    ENSMUST00000129308 ; ENSMUSP00000122252 ; ENSMUSG00000042642 . [Q8R123-1 ]
    GeneIDi 319945.
    KEGGi mmu:319945.
    UCSCi uc008pzh.2. mouse. [Q8R123-2 ]
    uc008pzi.1. mouse. [Q8R123-1 ]

    Organism-specific databases

    CTDi 80308.
    MGIi MGI:2443030. Flad1.

    Phylogenomic databases

    eggNOGi COG0175.
    GeneTreei ENSGT00390000007266.
    HOGENOMi HOG000007185.
    HOVERGENi HBG058211.
    KOi K00953.
    OMAi SFMRINP.
    OrthoDBi EOG7C5M9F.
    PhylomeDBi Q8R123.
    TreeFami TF314056.

    Enzyme and pathway databases

    UniPathwayi UPA00277 ; UER00407 .
    Reactomei REACT_216155. Vitamin B2 (riboflavin) metabolism.

    Miscellaneous databases

    NextBioi 395713.
    PROi Q8R123.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8R123.
    Bgeei Q8R123.
    Genevestigatori Q8R123.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    3.40.980.10. 1 hit.
    InterProi IPR012183. FAD_synth_Mopterin-bd.
    IPR001453. Mopterin-bd_dom.
    IPR002500. PAPS_reduct.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00994. MoCF_biosynth. 1 hit.
    PF01507. PAPS_reduct. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036620. MPTbdFAD. 1 hit.
    SMARTi SM00852. MoCF_biosynth. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53218. SSF53218. 1 hit.
    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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Olfactory bulb and Retina.
    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] (ISOFORM 1).
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain, Liver and Mammary gland.
    3. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 230-237, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    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-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiFAD1_MOUSE
    AccessioniPrimary (citable) accession number: Q8R123
    Secondary accession number(s): Q3TSN6, Q8BXQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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