FAD1_MOUSE
ID FAD1_MOUSE Reviewed; 492 AA.
AC Q8R123; Q3TSN6; Q8BXQ1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=FAD synthase;
DE EC=2.7.7.2;
DE AltName: Full=FAD pyrophosphorylase;
DE AltName: Full=FMN adenylyltransferase;
DE AltName: Full=Flavin adenine dinucleotide synthase;
DE Includes:
DE RecName: Full=Molybdenum cofactor biosynthesis protein-like region;
DE Includes:
DE RecName: Full=FAD synthase region;
GN Name=Flad1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Retina;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Liver, and Mammary gland;
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 [3]
RP PROTEIN SEQUENCE OF 230-237, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC 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).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN) to
CC form flavin adenine dinucleotide (FAD) coenzyme. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R123-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R123-2; Sequence=VSP_027955;
CC -!- DOMAIN: The molybdenum cofactor biosynthesis protein-like region may
CC not be functional.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PAPS reductase
CC family. FAD1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK044501; BAC31952.1; -; mRNA.
DR EMBL; AK161929; BAE36639.1; -; mRNA.
DR EMBL; BC009152; AAH09152.2; -; mRNA.
DR EMBL; BC025817; AAH25817.1; -; mRNA.
DR EMBL; BC046769; AAH46769.1; -; mRNA.
DR CCDS; CCDS38492.1; -. [Q8R123-1]
DR RefSeq; NP_796015.2; NM_177041.3. [Q8R123-1]
DR AlphaFoldDB; Q8R123; -.
DR SMR; Q8R123; -.
DR BioGRID; 235643; 6.
DR IntAct; Q8R123; 1.
DR STRING; 10090.ENSMUSP00000122252; -.
DR iPTMnet; Q8R123; -.
DR PhosphoSitePlus; Q8R123; -.
DR SwissPalm; Q8R123; -.
DR EPD; Q8R123; -.
DR jPOST; Q8R123; -.
DR MaxQB; Q8R123; -.
DR PaxDb; Q8R123; -.
DR PeptideAtlas; Q8R123; -.
DR PRIDE; Q8R123; -.
DR ProteomicsDB; 267707; -. [Q8R123-1]
DR ProteomicsDB; 267708; -. [Q8R123-2]
DR Antibodypedia; 34162; 152 antibodies from 24 providers.
DR Ensembl; ENSMUST00000050398; ENSMUSP00000051366; ENSMUSG00000042642. [Q8R123-2]
DR Ensembl; ENSMUST00000107426; ENSMUSP00000103049; ENSMUSG00000042642. [Q8R123-1]
DR Ensembl; ENSMUST00000129308; ENSMUSP00000122252; ENSMUSG00000042642. [Q8R123-1]
DR GeneID; 319945; -.
DR KEGG; mmu:319945; -.
DR UCSC; uc008pzh.2; mouse. [Q8R123-2]
DR UCSC; uc008pzi.1; mouse. [Q8R123-1]
DR CTD; 80308; -.
DR MGI; MGI:2443030; Flad1.
DR VEuPathDB; HostDB:ENSMUSG00000042642; -.
DR eggNOG; KOG2644; Eukaryota.
DR GeneTree; ENSGT00390000007266; -.
DR HOGENOM; CLU_030805_8_0_1; -.
DR InParanoid; Q8R123; -.
DR OMA; PDWSNNY; -.
DR OrthoDB; 1437247at2759; -.
DR PhylomeDB; Q8R123; -.
DR TreeFam; TF314056; -.
DR Reactome; R-MMU-196843; Vitamin B2 (riboflavin) metabolism.
DR UniPathway; UPA00277; UER00407.
DR BioGRID-ORCS; 319945; 18 hits in 76 CRISPR screens.
DR ChiTaRS; Flad1; mouse.
DR PRO; PR:Q8R123; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8R123; protein.
DR Bgee; ENSMUSG00000042642; Expressed in interventricular septum and 246 other tissues.
DR ExpressionAtlas; Q8R123; baseline and differential.
DR Genevisible; Q8R123; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006747; P:FAD biosynthetic process; IBA:GO_Central.
DR CDD; cd00885; cinA; 1.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.980.10; -; 1.
DR InterPro; IPR012183; FAD_synth_MoaB/Mog-bd.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF01507; PAPS_reduct; 1.
DR PIRSF; PIRSF036620; MPTbdFAD; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; SSF53218; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..492
FT /note="FAD synthase"
FT /id="PRO_0000302738"
FT REGION 19..110
FT /note="Molybdenum cofactor biosynthesis protein-like"
FT REGION 303..460
FT /note="FAD synthase"
FT MOD_RES 283
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 283
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 492
FT /note="M -> IPKTPGASWPSPRMGHKELKKEPRTLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027955"
FT CONFLICT 73
FT /note="R -> S (in Ref. 1; BAE36639)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="L -> Q (in Ref. 1; BAE36639)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 54766 MW; 75008DD249A7F43E CRC64;
MASRASELPP GSGRSVTAGI IIVGDEILKG HTQDTNTYFL CRTLRSLGVQ VCRVSVVPDE
VATIASEVNS FSRRFTHVLT AGGIGPTHDD VTFEAVAQAF GEELKPHPEL QAAIKTLGGE
GWEKLSMVPS SARLHYGTDP RTGHPFRFPL VSVRNVYLFP GIPELLRRVL EGLKGLFQNT
AVQFHLKELY VAASEGSIAP ILSEAQAHFG RRLSLGSYPD WSSNYFQVKL ILDSEEKEPL
EECLAYLTAR LPQGSLVPYQ PDAVEKAGEA VYKLAESGSC LGKKVAGALQ TIETALAQYH
LSQLCVGFNG GKDCTALLHL FHAAVQRKFP DVPKPLQILY IRSISPFPEL EQFLQDTIKR
YNLQVLEAEG NMKQALGELQ EKHPQLEAVL MGTRRTDPYS CSLSHFSPTD PGWPSFMRIN
PLLDWTYRNI WEFLRQLFVP YCILYDRGYT SLGSRENTTQ NPALKCLSPG GHPVYRPAYL
LENEDEERNS RM
