FAD1_HUMAN
ID FAD1_HUMAN Reviewed; 587 AA.
AC Q8NFF5; Q8N5J1; Q8N686; Q8WU93; Q8WUJ4; Q96CR8; Q99764; Q9HBN6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=FAD synthase;
DE EC=2.7.7.2 {ECO:0000269|PubMed:16643857};
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;
DE Flags: Precursor;
GN Name=FLAD1; ORFNames=PP591;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2),
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND FUNCTION.
RC TISSUE=Skin;
RX PubMed=16643857; DOI=10.1016/j.bbrc.2006.04.003;
RA Brizio C., Galluccio M., Wait R., Torchetti E.M., Bafunno V., Accardi R.,
RA Gianazza E., Indiveri C., Barile M.;
RT "Over-expression in Escherichia coli and characterization of two
RT recombinant isoforms of human FAD synthetase.";
RL Biochem. Biophys. Res. Commun. 344:1008-1016(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Fischer M.J., Kempter K., Bacher A.;
RT "Cloning, expression and characterization of a human FAD synthetase.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RA Chen X.G., Li Y.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 10-587 (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 256-587 (ISOFORM 1).
RC TISSUE=Brain, Colon, Placenta, and Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-587 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=17049878; DOI=10.1016/j.pep.2006.09.002;
RA Galluccio M., Brizio C., Torchetti E.M., Ferranti P., Gianazza E.,
RA Indiveri C., Barile M.;
RT "Over-expression in Escherichia coli, purification and characterization of
RT isoform 2 of human FAD synthetase.";
RL Protein Expr. Purif. 52:175-181(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-563, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=20060505; DOI=10.1016/j.mito.2009.12.149;
RA Torchetti E.M., Brizio C., Colella M., Galluccio M., Giancaspero T.A.,
RA Indiveri C., Roberti M., Barile M.;
RT "Mitochondrial localization of human FAD synthetase isoform 1.";
RL Mitochondrion 10:263-273(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP INVOLVEMENT IN LSMFLAD, VARIANT LSMFLAD CYS-530 (ISOFORM 2),
RP CHARACTERIZATION OF VARIANT LSMFLAD CYS-530 (ISOFORM 2), VARIANT LEU-107,
RP AND FUNCTION.
RX PubMed=27259049; DOI=10.1016/j.ajhg.2016.04.006;
RA Olsen R.K., Konarikova E., Giancaspero T.A., Mosegaard S., Boczonadi V.,
RA Matakovic L., Veauville-Merllie A., Terrile C., Schwarzmayr T., Haack T.B.,
RA Auranen M., Leone P., Galluccio M., Imbard A., Gutierrez-Rios P.,
RA Palmfeldt J., Graf E., Vianey-Saban C., Oppenheim M., Schiff M.,
RA Pichard S., Rigal O., Pyle A., Chinnery P.F., Konstantopoulou V.,
RA Moeslinger D., Feichtinger R.G., Talim B., Topaloglu H., Coskun T.,
RA Gucer S., Botta A., Pegoraro E., Malena A., Vergani L., Mazza D.,
RA Zollino M., Ghezzi D., Acquaviva C., Tyni T., Boneh A., Meitinger T.,
RA Strom T.M., Gregersen N., Mayr J.A., Horvath R., Barile M., Prokisch H.;
RT "Riboflavin-responsive and -non-responsive mutations in FAD synthase cause
RT multiple Acyl-CoA dehydrogenase and combined respiratory-chain
RT deficiency.";
RL Am. J. Hum. Genet. 98:1130-1145(2016).
CC -!- FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN) to
CC form flavin adenine dinucleotide (FAD) coenzyme.
CC {ECO:0000269|PubMed:16643857, ECO:0000269|PubMed:27259049}.
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 Evidence={ECO:0000269|PubMed:16643857};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16643857, ECO:0000269|PubMed:17049878};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for FMN {ECO:0000269|PubMed:16643857,
CC ECO:0000269|PubMed:17049878};
CC KM=0.36 uM for FMN (isoform 2) {ECO:0000269|PubMed:16643857,
CC ECO:0000269|PubMed:17049878};
CC Vmax=6.1 nmol/min/mg enzyme {ECO:0000269|PubMed:16643857,
CC ECO:0000269|PubMed:17049878};
CC Vmax=3.9 nmol/min/mg enzyme (isoform 2) {ECO:0000269|PubMed:16643857,
CC ECO:0000269|PubMed:17049878};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1.
CC -!- INTERACTION:
CC Q8NFF5; Q8NFF5: FLAD1; NbExp=3; IntAct=EBI-742815, EBI-742815;
CC Q8NFF5; Q04864: REL; NbExp=3; IntAct=EBI-742815, EBI-307352;
CC Q8NFF5; O00560: SDCBP; NbExp=4; IntAct=EBI-742815, EBI-727004;
CC Q8NFF5; P15884: TCF4; NbExp=3; IntAct=EBI-742815, EBI-533224;
CC Q8NFF5-2; Q7Z2E3-7: APTX; NbExp=3; IntAct=EBI-11526128, EBI-12298187;
CC Q8NFF5-2; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-11526128, EBI-12357161;
CC Q8NFF5-2; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-11526128, EBI-350590;
CC Q8NFF5-2; P29373: CRABP2; NbExp=3; IntAct=EBI-11526128, EBI-10204806;
CC Q8NFF5-2; P50570: DNM2; NbExp=3; IntAct=EBI-11526128, EBI-346547;
CC Q8NFF5-2; Q8NFF5-2: FLAD1; NbExp=5; IntAct=EBI-11526128, EBI-11526128;
CC Q8NFF5-2; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-11526128, EBI-11985629;
CC Q8NFF5-2; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-11526128, EBI-740897;
CC Q8NFF5-2; Q9NRG1: PRTFDC1; NbExp=3; IntAct=EBI-11526128, EBI-739759;
CC Q8NFF5-2; Q04864-2: REL; NbExp=3; IntAct=EBI-11526128, EBI-10829018;
CC Q8NFF5-2; P36406: TRIM23; NbExp=3; IntAct=EBI-11526128, EBI-740098;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion matrix
CC {ECO:0000269|PubMed:20060505}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=FADS1 {ECO:0000303|PubMed:27259049};
CC IsoId=Q8NFF5-1; Sequence=Displayed;
CC Name=2; Synonyms=FADS2 {ECO:0000303|PubMed:27259049};
CC IsoId=Q8NFF5-2; Sequence=VSP_027947;
CC Name=3;
CC IsoId=Q8NFF5-3; Sequence=VSP_027947, VSP_027954;
CC Name=4;
CC IsoId=Q8NFF5-4; Sequence=VSP_027948, VSP_027949, VSP_027951,
CC VSP_027952;
CC Name=5;
CC IsoId=Q8NFF5-5; Sequence=VSP_027948, VSP_027949, VSP_027950,
CC VSP_027953;
CC -!- DOMAIN: The molybdenum cofactor biosynthesis protein-like region may
CC not be functional.
CC -!- DISEASE: Lipid storage myopathy due to flavin adenine dinucleotide
CC synthetase deficiency (LSMFLAD) [MIM:255100]: An autosomal recessive,
CC inborn error of metabolism characterized by variable mitochondrial
CC dysfunction. Clinical features range from severe cardiac and
CC respiratory insufficiency with onset in infancy and resulting in early
CC death, to mild muscle weakness with onset in adulthood. Some patients
CC show significant improvement with riboflavin treatment. Analysis of
CC skeletal muscle show multiple mitochondrial respiratory chain
CC deficiency and a lipid storage myopathy in most patients.
CC {ECO:0000269|PubMed:27259049}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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}.
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DR EMBL; DQ458779; ABE65383.1; -; mRNA.
DR EMBL; AF481877; AAO49318.1; -; mRNA.
DR EMBL; AF520568; AAM77338.1; -; mRNA.
DR EMBL; AF218022; AAG17264.1; -; mRNA.
DR EMBL; AL451085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53154.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53155.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53158.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53159.1; -; Genomic_DNA.
DR EMBL; BC011378; AAH11378.1; -; mRNA.
DR EMBL; BC014012; AAH14012.2; -; mRNA.
DR EMBL; BC020253; AAH20253.1; -; mRNA.
DR EMBL; BC021096; AAH21096.2; -; mRNA.
DR EMBL; BC032323; AAH32323.1; -; mRNA.
DR EMBL; U79241; AAB50199.1; -; mRNA.
DR CCDS; CCDS1078.1; -. [Q8NFF5-1]
DR CCDS; CCDS1079.1; -. [Q8NFF5-2]
DR CCDS; CCDS53371.1; -. [Q8NFF5-3]
DR CCDS; CCDS53372.1; -. [Q8NFF5-4]
DR RefSeq; NP_001171820.1; NM_001184891.1. [Q8NFF5-3]
DR RefSeq; NP_001171821.1; NM_001184892.1. [Q8NFF5-4]
DR RefSeq; NP_079483.3; NM_025207.4. [Q8NFF5-1]
DR RefSeq; NP_958800.1; NM_201398.2. [Q8NFF5-2]
DR AlphaFoldDB; Q8NFF5; -.
DR SMR; Q8NFF5; -.
DR BioGRID; 123221; 113.
DR IntAct; Q8NFF5; 36.
DR MINT; Q8NFF5; -.
DR STRING; 9606.ENSP00000292180; -.
DR ChEMBL; CHEMBL3879869; -.
DR GlyGen; Q8NFF5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NFF5; -.
DR PhosphoSitePlus; Q8NFF5; -.
DR BioMuta; FLAD1; -.
DR DMDM; 74751275; -.
DR EPD; Q8NFF5; -.
DR jPOST; Q8NFF5; -.
DR MassIVE; Q8NFF5; -.
DR MaxQB; Q8NFF5; -.
DR PaxDb; Q8NFF5; -.
DR PeptideAtlas; Q8NFF5; -.
DR PRIDE; Q8NFF5; -.
DR ProteomicsDB; 73297; -. [Q8NFF5-1]
DR ProteomicsDB; 73298; -. [Q8NFF5-2]
DR ProteomicsDB; 73299; -. [Q8NFF5-3]
DR ProteomicsDB; 73300; -. [Q8NFF5-4]
DR ProteomicsDB; 73301; -. [Q8NFF5-5]
DR Antibodypedia; 34162; 152 antibodies from 24 providers.
DR DNASU; 80308; -.
DR Ensembl; ENST00000292180.8; ENSP00000292180.3; ENSG00000160688.19. [Q8NFF5-1]
DR Ensembl; ENST00000315144.14; ENSP00000317296.10; ENSG00000160688.19. [Q8NFF5-2]
DR Ensembl; ENST00000368431.7; ENSP00000357416.3; ENSG00000160688.19. [Q8NFF5-4]
DR Ensembl; ENST00000368432.5; ENSP00000357417.1; ENSG00000160688.19. [Q8NFF5-3]
DR GeneID; 80308; -.
DR KEGG; hsa:80308; -.
DR MANE-Select; ENST00000292180.8; ENSP00000292180.3; NM_025207.5; NP_079483.3.
DR UCSC; uc001fgc.4; human. [Q8NFF5-1]
DR CTD; 80308; -.
DR DisGeNET; 80308; -.
DR GeneCards; FLAD1; -.
DR HGNC; HGNC:24671; FLAD1.
DR HPA; ENSG00000160688; Low tissue specificity.
DR MalaCards; FLAD1; -.
DR MIM; 255100; phenotype.
DR MIM; 610595; gene.
DR neXtProt; NX_Q8NFF5; -.
DR OpenTargets; ENSG00000160688; -.
DR Orphanet; 394532; Multiple acyl-CoA dehydrogenase deficiency, mild type.
DR Orphanet; 394529; Multiple acyl-CoA dehydrogenase deficiency, severe neonatal type.
DR PharmGKB; PA142671759; -.
DR VEuPathDB; HostDB:ENSG00000160688; -.
DR eggNOG; KOG2644; Eukaryota.
DR GeneTree; ENSGT00390000007266; -.
DR HOGENOM; CLU_030805_8_0_1; -.
DR InParanoid; Q8NFF5; -.
DR OMA; EGWAPGC; -.
DR OrthoDB; 1437247at2759; -.
DR PhylomeDB; Q8NFF5; -.
DR TreeFam; TF314056; -.
DR BioCyc; MetaCyc:HS08520-MON; -.
DR BRENDA; 2.7.7.2; 2681.
DR PathwayCommons; Q8NFF5; -.
DR Reactome; R-HSA-196843; Vitamin B2 (riboflavin) metabolism.
DR SABIO-RK; Q8NFF5; -.
DR SignaLink; Q8NFF5; -.
DR UniPathway; UPA00277; UER00407.
DR BioGRID-ORCS; 80308; 27 hits in 1079 CRISPR screens.
DR ChiTaRS; FLAD1; human.
DR GenomeRNAi; 80308; -.
DR Pharos; Q8NFF5; Tbio.
DR PRO; PR:Q8NFF5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NFF5; protein.
DR Bgee; ENSG00000160688; Expressed in apex of heart and 171 other tissues.
DR ExpressionAtlas; Q8NFF5; baseline and differential.
DR Genevisible; Q8NFF5; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IPI:IntAct.
DR GO; GO:0006747; P:FAD biosynthetic process; IBA:GO_Central.
DR GO; GO:0006771; P:riboflavin metabolic process; TAS:Reactome.
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; 2.
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; Disease variant;
KW FAD; Flavoprotein; FMN; Mitochondrion; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Primary mitochondrial disease;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..587
FT /note="FAD synthase"
FT /id="PRO_0000302737"
FT REGION 114..205
FT /note="Molybdenum cofactor biosynthesis protein-like"
FT REGION 398..555
FT /note="FAD synthase"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 378
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8R123"
FT MOD_RES 378
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8R123"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_027947"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_027948"
FT VAR_SEQ 31..124
FT /note="LEGSTRTPALPHCLFWLLQVPSTQDPLFPGYGPQCPVDLAGPPCLRPLFGGL
FT GGYWRALQRGREGRTMTSRASELSPGRSVTAGIIIVGDEILK -> MQPSSSTPPLHPY
FT STDGLIFPFNPQ (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_027949"
FT VAR_SEQ 374..437
FT /note="SSLGKKVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLP
FT DVPNPLQILYIR -> NYLMFQTPSRSCISAASPLSLSWNSFYRTLSREQAIPENQIAS
FT PPSEAKGAEEPWMGPFPGQQG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027950"
FT VAR_SEQ 374..393
FT /note="SSLGKKVAGALQTIETSLAQ -> RDLMEEGHYAQSHWWHPRSQ (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_027951"
FT VAR_SEQ 394..587
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_027952"
FT VAR_SEQ 438..587
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027953"
FT VAR_SEQ 544..587
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027954"
FT VARIANT 107
FT /note="P -> L (in dbSNP:rs773925274)"
FT /evidence="ECO:0000269|PubMed:27259049"
FT /id="VAR_077069"
FT VARIANT 530
FT /note="R -> C (in LSMFLAD; decreased protein stability;
FT decreased affinity for FMN; reduced Vmax; decreased FMN
FT adenylyltransferase activity; dbSNP:rs771466122)"
FT /evidence="ECO:0000269|PubMed:27259049"
FT /id="VAR_077070"
SQ SEQUENCE 587 AA; 65266 MW; F95918B15D9D8106 CRC64;
MGWDLGTRLF QRQEQRSRLS RIWLEKTRVF LEGSTRTPAL PHCLFWLLQV PSTQDPLFPG
YGPQCPVDLA GPPCLRPLFG GLGGYWRALQ RGREGRTMTS RASELSPGRS VTAGIIIVGD
EILKGHTQDT NTFFLCRTLR SLGVQVCRVS VVPDEVATIA AEVTSFSNRF THVLTAGGIG
PTHDDVTFEA VAQAFGDELK PHPKLEAATK ALGGEGWEKL SLVPSSARLH YGTDPCTGQP
FRFPLVSVRN VYLFPGIPEL LRRVLEGMKG LFQNPAVQFH SKELYVAADE ASIAPILAEA
QAHFGRRLGL GSYPDWGSNY YQVKLTLDSE EEGPLEECLA YLTARLPQGS LVPYMPNAVE
QASEAVYKLA ESGSSLGKKV AGALQTIETS LAQYSLTQLC VGFNGGKDCT ALLHLFHAAV
QRKLPDVPNP LQILYIRSIS PFPELEQFLQ DTIKRYNLQM LEAEGSMKQA LGELQARHPQ
LEAVLMGTRR TDPYSCSLCP FSPTDPGWPA FMRINPLLDW TYRDIWDFLR QLFVPYCILY
DRGYTSLGSR ENTVRNPALK CLSPGGHPTY RPAYLLENEE EERNSRT
