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Q8CFV9 (RIFK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Riboflavin kinase

EC=2.7.1.26
Alternative name(s):
ATP:riboflavin 5'-phosphotransferase
Flavokinase
KOI-4
Gene names
Name:Rfk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length155 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), hence rate-limiting enzyme in the synthesis of FAD. Essential for TNF-induced reactive oxygen species (ROS) production. Through its interaction with both TNFRSF1A and CYBA, physically and functionally couples TNFRSF1A to NADPH oxidase. TNF-activation of RFK may enhance the incorporation of FAD in NADPH oxidase, a critical step for the assembly and activation of NADPH oxidase By similarity.

Catalytic activity

ATP + riboflavin = ADP + FMN.

Cofactor

Zinc or magnesium By similarity.

Pathway

Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.

Subunit structure

Monomer By similarity. Directly interacts with TNFRSF1A death domain; this interaction may be supported by TRADD. In the absence of TNFRSF1A, interacts with TRADD. Independently of TNFRSF1A, interacts with the NADPH oxidase subunit CYBA. Ref.4

Subcellular location

Cytoplasm By similarity.

Disruption phenotype

Mutant embryos die in utero before 7.5 dpc. Ref.4

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 155155Riboflavin kinase
PRO_0000194149

Sites

Active site791Nucleophile By similarity
Metal binding271Magnesium By similarity
Binding site151ATP; via amide nitrogen By similarity
Binding site211ATP; via amide nitrogen By similarity
Binding site271ATP; via amide nitrogen By similarity
Binding site291ATP By similarity
Binding site821ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site841ATP; via carbonyl oxygen By similarity
Binding site911ATP By similarity
Binding site1041FMN By similarity
Binding site1071FMN; via amide nitrogen and carbonyl oxygen By similarity
Binding site1091FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CFV9 [UniParc].

Last modified October 3, 2003. Version 2.
Checksum: AE6577023E3D34CF

FASTA15517,437
        10         20         30         40         50         60 
MRSLPFFCRG QVVRGFGRGS KQLGIPTANF PEQVVDNLPA DVSTGIYYGW ASVGSGDVHK 

        70         80         90        100        110        120 
MVVSIGWNPY YKNVKKSMET HIIHTFKEDF YGEILNVAIV GYLRPEKNFD SLESLISAIQ 

       130        140        150 
GDIEEAKKQL DLPEHLKLKD DNFFQVSKGK IMNGH 

« Hide

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].
Strain: C57BL/6J.
Tissue: Embryonic stem cell, Kidney and Small intestine.
[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].
Tissue: Olfactory epithelium and Retina.
[3]Abrantes E.F., Silva A.M., Reis L.F.L.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-112 AND 114-155.
Strain: 129/Sv.
[4]"Riboflavin kinase couples TNF receptor 1 to NADPH oxidase."
Yazdanpanah B., Wiegmann K., Tchikov V., Krut O., Pongratz C., Schramm M., Kleinridders A., Wunderlich T., Kashkar H., Utermoehlen O., Bruening J.C., Schuetze S., Kroenke M.
Nature 460:1159-1163(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CYBA; TNFRSF1A AND TRADD, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK010607 mRNA. Translation: BAB27057.1.
AK002806 mRNA. Translation: BAB22372.1.
AK008352 mRNA. Translation: BAB25622.1.
BC033521 mRNA. Translation: AAH33521.2.
BC051021 mRNA. Translation: AAH51021.1.
AF031380 Genomic DNA. Translation: AAB86494.1.
AF031381 Genomic DNA. Translation: AAB86495.1.
CCDSCCDS29688.1.
RefSeqNP_062310.1. NM_019437.3.
UniGeneMm.7013.

3D structure databases

ProteinModelPortalQ8CFV9.
SMRQ8CFV9. Positions 2-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60455N.
STRING10090.ENSMUSP00000025617.

PTM databases

PhosphoSiteQ8CFV9.

Proteomic databases

MaxQBQ8CFV9.
PaxDbQ8CFV9.
PRIDEQ8CFV9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025617; ENSMUSP00000025617; ENSMUSG00000024712.
GeneID54391.
KEGGmmu:54391.
UCSCuc008gxo.2. mouse.

Organism-specific databases

CTD55312.
MGIMGI:1914688. Rfk.

Phylogenomic databases

eggNOGCOG0196.
GeneTreeENSGT00390000015537.
HOGENOMHOG000260803.
HOVERGENHBG049989.
InParanoidQ8CFV9.
KOK00861.
OMASLPYFCR.
OrthoDBEOG7K3TP0.
PhylomeDBQ8CFV9.
TreeFamTF313786.

Enzyme and pathway databases

UniPathwayUPA00276; UER00406.

Gene expression databases

BgeeQ8CFV9.
CleanExMM_RFK.
GenevestigatorQ8CFV9.

Family and domain databases

Gene3D2.40.30.30. 1 hit.
InterProIPR023468. Riboflavin_kinase.
IPR015865. Riboflavin_kinase_bac/euk.
IPR023465. Riboflavin_kinase_domain.
[Graphical view]
PANTHERPTHR22749. PTHR22749. 1 hit.
PfamPF01687. Flavokinase. 1 hit.
[Graphical view]
SMARTSM00904. Flavokinase. 1 hit.
[Graphical view]
SUPFAMSSF82114. SSF82114. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRFK. mouse.
NextBio311232.
PROQ8CFV9.
SOURCESearch...

Entry information

Entry nameRIFK_MOUSE
AccessionPrimary (citable) accession number: Q8CFV9
Secondary accession number(s): O35471, O35472, Q9CQ95
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: July 9, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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