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UniProtKB/Swiss-Prot entry Q9NYQ2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HAOX2_MOUSE
Primary accession number Q9NYQ2
Secondary accession numbers Q9JHS7 Q9JI00
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 71)
Name and origin of the protein
Protein name Hydroxyacid oxidase 2
Synonyms HAOX2
EC 1.1.3.15
(S)-2-hydroxy-acid oxidase, peroxisomal
Medium chain alpha-hydroxy acid oxidase
Medium-chain L-2-hydroxy acid oxidase
Gene name
Name: Hao2
Synonyms: Hao3, Haox2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.275.17.12590; PubMed=10777549 [NCBI, ExPASy, EBI, Israel, Japan]
Jones J.M., Morrell J.C., Gould S.J.;
"Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases.";
J. Biol. Chem. 275:12590-12597(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Spielbauer B., Conzelmann E.;
"Mus musculus long-chain L-2-hydroxy acid oxidase.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Van Veldhoven P.P.;
"Search for PTS1-containing protein in mammals.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Cecum;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF231918; AAF40201.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF272947; AAF81795.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ251820; CAB96380.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK078908; BAC37452.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Mm.281874
3D structure databases
HSSP P05414; 1GOX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
SMR Q9NYQ2; 3-350.
ModBase Q9NYQ2.
Organism-specific databases
MGI MGI:1860477; Hao3.
Gene expression databases
ArrayExpress Q9NYQ2; -.
CleanEx MM_HAO3; -.
GermOnline ENSMUSG00000027870; Mus musculus.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (traceable author statement from ProtInc).
GO:0003973; Molecular function: (S)-2-hydroxy-acid oxidase activity (traceable author statement from ProtInc).
GO:0006631; Biological process: fatty acid metabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR012133; Alpha_OHA_DHase_FMN.
IPR008259; FMN_hydac_DHase_AS.
IPR000262; FMN_OHA_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01070; FMN_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000138; Al-hdrx_acd_dh; 1.
PROSITE PS00557; FMN_HYDROXY_ACID_DH_1; 1.
PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9NYQ2.
Genome annotation databases
Ensembl ENSMUSG00000027870; Mus musculus. [Contig view]
Phylogenomic databases
HOGENOM Q9NYQ2; -.
HOVERGEN Q9NYQ2; -.
Other
SOURCE Hao2; Mus musculus.
ProtoNet Q9NYQ2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Flavoprotein; FMN; Oxidoreductase; Peroxisome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   353  353     Hydroxyacid oxidase 2. PRO_0000206321
DOMAIN   1   353  353     FMN hydroxy acid dehydrogenase. 
NP_BIND   279   303  25     FMN (By similarity). 
MOTIF   351   353  3     Microbody targeting signal (Potential). 
ACT_SITE   248   248        Proton acceptor (By similarity). 
BINDING   106   106        FMN (By similarity). 
BINDING   128   128        FMN (By similarity). 
BINDING   130   130        Substrate (By similarity). 
BINDING   156   156        FMN (By similarity). 
BINDING   165   165        Substrate (By similarity). 
BINDING   224   224        FMN (By similarity). 
BINDING   251   251        Substrate (Potential). 
CONFLICT   164   164        N -> H (in Ref. 3; CAB96380). 
Sequence information
Length: 353 AA [This is the length of the unprocessed precursor] Molecular weight: 38700 Da [This is the MW of the unprocessed precursor] CRC64: 0604D529F69DE3C7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLLCLADFK AQAQKQLSKT SWDFIEGEAD DGITYNDNLA AFRRIRLRPR YLRDVSKIDT 

        70         80         90        100        110        120 
RTTIQGQEIN APICISPTAF HSIAWADGEK STAKAAQKAN ICYVISSYAS YTVEDIVAAA 

       130        140        150        160        170        180 
PGGLHWFQLY VQPDWDINKQ MVQRIEALGF KALVVTVDAP VLGNRRGNKR SLLDLEANIK 

       190        200        210        220        230        240 
LKDLRSPGES KSGLPTPLSM PSSSSCWNDL PLLQSMTRLP IILKGILTKE DAELAVKHNI 

       250        260        270        280        290        300 
RGIIVSNHGG RQLDEVPASI DALREVVAAV NGKIEVYMDG GVRTGNDVLK ALALGARCIF 

       310        320        330        340        350 
LGRPIIWGLA CKGEDGVKEV LDILKEELHT CMALSGCRSV AEISPDLIQF SRL 

Q9NYQ2 in FASTA format

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