Reviewed, UniProtKB/Swiss-Prot Q91WN4 (KMO_MOUSE)

Names and origin

Protein names

Recommended name:
    Kynurenine 3-monooxygenase
    EC=1.14.13.9
Alternative name(s):
    Kynurenine 3-hydroxylase

Gene names

Name:

Kmo

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract By similarity.
Catalytic activity	L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O. UniProtKB O15229
Cofactor	FAD By similarity. UniProtKB O15229
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3.
Subcellular location	Mitochondrion outer membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the aromatic-ring hydroxylase family. KMO subfamily.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	NAD metabolic process Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from direct assay. Source: MGI mitochondrial outer membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	kynurenine 3-monooxygenase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.2 (identifier: Q91WN4-1)

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 Ref.1 (identifier: Q91WN4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     367-400: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 479	479	Kynurenine 3-monooxygenase		PRO_0000229743
Regions
	Transmembrane	385 – 404	20	Potential
	Transmembrane	425 – 445	21	Potential
Amino acid modifications
	Modified residue	399	1	Phosphothreonine Ref.3
Natural variations
	Alternative sequence	367 – 400	34	Missing in isoform 2. Ref.1		VSP_051974

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: E880997DBC9C8163	FASTA	479	54,532
	10 20 30 40 50 60 MASSDTQGKR VAVIGGGLVG ALNACFLAKR NFQVDVYEAR EDIRVAKSAR GRSINLALSY 70 80 90 100 110 120 RGRQALKAIG LEDQIVSKGV PMKARMIHSL SGKKSAIPYG NKSQYILSIS RENLNKDLLT 130 140 150 160 170 180 AVESYANAKV HFGHKLSKCI PEEGVLTVLG PDKVPRDVTC DLVVGCDGAY STVRAHLMKK 190 200 210 220 230 240 PRFDYTQQYI PHGYMELTIP PKNGEYAMEP NCLHIWPRNA YMMIALPNMD KSFTCTLFMP 250 260 270 280 290 300 FEEFERLPTR SDVLDFFQKN FPDAIPLMGE QALMRDFFLL PAQPMISVKC SPFHLKSHCV 310 320 330 340 350 360 LMGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFNNNLSM CLPEFSRFRI PDDHAISDLS 370 380 390 400 410 420 MYNYIEMRAH VNSRWFLFQK LLDKFLHAIM PSTFIPLYTM VAFTRIRYHE AVLRWHWQKK 430 440 450 460 470 VINRGLFVLG SLIAIGGTYL LVHHLSLRPL EFLRRPAWMG TTGYWTRSTD ISLQVPWSY
	Isoform 2. Checksum: E2B58D64DDF95BCC	FASTA	445	50,396
	10 20 30 40 50 60 MASSDTQGKR VAVIGGGLVG ALNACFLAKR NFQVDVYEAR EDIRVAKSAR GRSINLALSY 70 80 90 100 110 120 RGRQALKAIG LEDQIVSKGV PMKARMIHSL SGKKSAIPYG NKSQYILSIS RENLNKDLLT 130 140 150 160 170 180 AVESYANAKV HFGHKLSKCI PEEGVLTVLG PDKVPRDVTC DLVVGCDGAY STVRAHLMKK 190 200 210 220 230 240 PRFDYTQQYI PHGYMELTIP PKNGEYAMEP NCLHIWPRNA YMMIALPNMD KSFTCTLFMP 250 260 270 280 290 300 FEEFERLPTR SDVLDFFQKN FPDAIPLMGE QALMRDFFLL PAQPMISVKC SPFHLKSHCV 310 320 330 340 350 360 LMGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFNNNLSM CLPEFSRFRI PDDHAISDLS 370 380 390 400 410 420 MYNYIEVAFT RIRYHEAVLR WHWQKKVINR GLFVLGSLIA IGGTYLLVHH LSLRPLEFLR 430 440 RPAWMGTTGY WTRSTDISLQ VPWSY

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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N. Tissue: Liver.
[3]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK129011 mRNA. No translation available. BC014683 mRNA. Translation: AAH14683.1.
IPI	IPI00128271. IPI00742309.
RefSeq	NP_598570.1.
UniGene	Mm.27217
3D structure databases
SMR	Q91WN4. Positions 10-362.
ModBase	Search...
Protein-protein interaction databases
STRING	Q91WN4.
PTM databases
PhosphoSite	Q91WN4.
Proteomic databases
PRIDE	Q91WN4.
Genome annotation databases
Ensembl	ENSMUST00000040250; ENSMUSP00000038914; ENSMUSG00000039783; Mus musculus. [Genome view] ENSMUST00000097458; ENSMUSP00000095067; ENSMUSG00000039783; Mus musculus. [Genome view]
GeneID	98256.
KEGG	mmu:98256.
NMPDR	fig|10090.3.peg.1585.
UCSC	uc007dtp.1. mouse.
Organism-specific databases
CTD	98256.
MGI	MGI:2138151. Kmo.
Phylogenomic databases
HOGENOM	HBG430104.
HOVERGEN	Q91WN4.
InParanoid	Q91WN4.
OMA	HWQKKVI.
PhylomeDB	Q91WN4.
Enzyme and pathway databases
BRENDA	1.14.13.9. 244.
Gene expression databases
ArrayExpress	Q91WN4.
Bgee	Q91WN4.
Genevestigator	Q91WN4.
GermOnline	ENSMUSG00000039783. Mus musculus.
Family and domain databases
InterPro	IPR002938. mOase_FAD_bd. IPR003042. Rng_hydrolase-like. [Graphical view]
Pfam	PF01494. FAD_binding_3. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...
Other Resources
NextBio	353386.
SOURCE	Search...

Entry information

Entry name

KMO_MOUSE

Accession

Primary (citable) accession number: Q91WN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	December 1, 2001
Last modified:	February 9, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)