Q8R123 (FAD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Molybdenum cofactor biosynthesis protein-like region
2. FAD synthase region

Gene names

Name:

Flad1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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

Keywords
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding FAD FMN Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	FAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW FMN adenylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	FAD synthase		PRO_0000302738
Regions
	Region	19 – 110	92	Molybdenum cofactor biosynthesis protein-like
	Region	303 – 460	158	FAD synthase
Amino acid modifications
	Modified residue	468	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	492	1	M → IPKTPGASWPSPRMGHKELK KEPRTLL in isoform 2.		VSP_027955
Experimental info
	Sequence conflict	73	1	R → S in BAE36639. Ref.1
	Sequence conflict	390	1	L → Q in BAE36639. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 75008DD249A7F43E	FASTA	492	54,766
	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
	Isoform 2 [UniParc]. Checksum: BE331637181B8654	FASTA	518	57,673
	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 490 500 510 LENEDEERNS RIPKTPGASW PSPRMGHKEL KKEPRTLL

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	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.
IPI	IPI00226787. IPI00831326.
RefSeq	NP_796015.2. NM_177041.3.
UniGene	Mm.258142.
3D structure databases
ProteinModelPortal	Q8R123.
SMR	Q8R123. Positions 18-174, 264-465.
ModBase	Search...
PTM databases
PhosphoSite	Q8R123.
Proteomic databases
PaxDb	Q8R123.
PRIDE	Q8R123.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000050398; ENSMUSP00000051366; ENSMUSG00000042642. ENSMUST00000107426; ENSMUSP00000103049; ENSMUSG00000042642. ENSMUST00000129308; ENSMUSP00000122252; ENSMUSG00000042642.
GeneID	319945.
KEGG	mmu:319945.
UCSC	uc008pzh.2. mouse. uc008pzi.1. mouse.
Organism-specific databases
CTD	80308.
MGI	MGI:2443030. Flad1.
Phylogenomic databases
eggNOG	COG0175.
GeneTree	ENSGT00390000007266.
HOGENOM	HOG000007185.
HOVERGEN	HBG058211.
KO	K00953.
OMA	SFMRINP.
OrthoDB	EOG4P2Q27.
Enzyme and pathway databases
UniPathway	UPA00277; UER00407.
Gene expression databases
ArrayExpress	Q8R123.
Bgee	Q8R123.
Genevestigator	Q8R123.
Family and domain databases
Gene3D	3.40.50.620. 1 hit. 3.40.980.10. 1 hit.
InterPro	IPR012183. FAD_synth_Mopterin-bd. IPR001453. Mopterin-bd_dom. IPR002500. PAPS_reduct. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF00994. MoCF_biosynth. 1 hit. PF01507. PAPS_reduct. 1 hit. [Graphical view]
PIRSF	PIRSF036620. MPTbdFAD. 1 hit.
SMART	SM00852. MoCF_biosynth. 1 hit. [Graphical view]
SUPFAM	SSF53218. MoCF_biosynth. 1 hit.
ProtoNet	Search...
Other
NextBio	395713.
SOURCE	Search...

Entry information

Entry name

FAD1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program