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Q8R123 (FAD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FAD synthase

EC=2.7.7.2
Alternative name(s):
FAD pyrophosphorylase
FMN adenylyltransferase
Flavin adenine dinucleotide synthase

Including the following 2 domains:

  1. Molybdenum cofactor biosynthesis protein-like region
  2. FAD synthase region
Gene names
Name:Flad1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

ATP + FMN = diphosphate + FAD.

Cofactor

Magnesium By similarity.

Pathway

Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.

Subcellular location

Cytoplasm By similarity.

Domain

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

Sequence similarities

In the N-terminal section; belongs to the MoaB/Mog family.

In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8R123-1)

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.
Isoform 2 (identifier: Q8R123-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492FAD synthase
PRO_0000302738

Regions

Region19 – 11092Molybdenum cofactor biosynthesis protein-like
Region303 – 460158FAD synthase

Amino acid modifications

Modified residue2831N6-acetyllysine; alternate Ref.5
Modified residue2831N6-succinyllysine; alternate Ref.4
Modified residue4681Phosphoserine By similarity

Natural variations

Alternative sequence4921M → IPKTPGASWPSPRMGHKELK KEPRTLL in isoform 2.
VSP_027955

Experimental info

Sequence conflict731R → S in BAE36639. Ref.1
Sequence conflict3901L → Q in BAE36639. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 75008DD249A7F43E

FASTA49254,766
        10         20         30         40         50         60 
MASRASELPP GSGRSVTAGI IIVGDEILKG HTQDTNTYFL CRTLRSLGVQ VCRVSVVPDE 

        70         80         90        100        110        120 
VATIASEVNS FSRRFTHVLT AGGIGPTHDD VTFEAVAQAF GEELKPHPEL QAAIKTLGGE 

       130        140        150        160        170        180 
GWEKLSMVPS SARLHYGTDP RTGHPFRFPL VSVRNVYLFP GIPELLRRVL EGLKGLFQNT 

       190        200        210        220        230        240 
AVQFHLKELY VAASEGSIAP ILSEAQAHFG RRLSLGSYPD WSSNYFQVKL ILDSEEKEPL 

       250        260        270        280        290        300 
EECLAYLTAR LPQGSLVPYQ PDAVEKAGEA VYKLAESGSC LGKKVAGALQ TIETALAQYH 

       310        320        330        340        350        360 
LSQLCVGFNG GKDCTALLHL FHAAVQRKFP DVPKPLQILY IRSISPFPEL EQFLQDTIKR 

       370        380        390        400        410        420 
YNLQVLEAEG NMKQALGELQ EKHPQLEAVL MGTRRTDPYS CSLSHFSPTD PGWPSFMRIN 

       430        440        450        460        470        480 
PLLDWTYRNI WEFLRQLFVP YCILYDRGYT SLGSRENTTQ NPALKCLSPG GHPVYRPAYL 

       490 
LENEDEERNS RM 

« Hide

Isoform 2 [UniParc].

Checksum: BE331637181B8654
Show »

FASTA51857,673

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS38492.1. [Q8R123-1]
RefSeqNP_796015.2. NM_177041.3. [Q8R123-1]
UniGeneMm.258142.

3D structure databases

ProteinModelPortalQ8R123.
SMRQ8R123. Positions 18-174, 264-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8R123. 1 interaction.
MINTMINT-4118484.

PTM databases

PhosphoSiteQ8R123.

Proteomic databases

MaxQBQ8R123.
PaxDbQ8R123.
PRIDEQ8R123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050398; ENSMUSP00000051366; ENSMUSG00000042642. [Q8R123-2]
ENSMUST00000107426; ENSMUSP00000103049; ENSMUSG00000042642. [Q8R123-1]
ENSMUST00000129308; ENSMUSP00000122252; ENSMUSG00000042642. [Q8R123-1]
GeneID319945.
KEGGmmu:319945.
UCSCuc008pzh.2. mouse. [Q8R123-2]
uc008pzi.1. mouse. [Q8R123-1]

Organism-specific databases

CTD80308.
MGIMGI:2443030. Flad1.

Phylogenomic databases

eggNOGCOG0175.
GeneTreeENSGT00390000007266.
HOGENOMHOG000007185.
HOVERGENHBG058211.
KOK00953.
OMASFMRINP.
OrthoDBEOG7C5M9F.
PhylomeDBQ8R123.
TreeFamTF314056.

Enzyme and pathway databases

UniPathwayUPA00277; UER00407.

Gene expression databases

ArrayExpressQ8R123.
BgeeQ8R123.
GenevestigatorQ8R123.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.40.980.10. 1 hit.
InterProIPR012183. FAD_synth_Mopterin-bd.
IPR001453. Mopterin-bd_dom.
IPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00994. MoCF_biosynth. 1 hit.
PF01507. PAPS_reduct. 1 hit.
[Graphical view]
PIRSFPIRSF036620. MPTbdFAD. 1 hit.
SMARTSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF53218. SSF53218. 1 hit.
ProtoNetSearch...

Other

NextBio395713.
PROQ8R123.
SOURCESearch...

Entry information

Entry nameFAD1_MOUSE
AccessionPrimary (citable) accession number: Q8R123
Secondary accession number(s): Q3TSN6, Q8BXQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot