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Reviewed, UniProtKB/Swiss-Prot Q9NYQ2 (HAOX2_MOUSE)

Last modified February 9, 2010. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Hydroxyacid oxidase 2
      Short name=HAOX2
    EC=1.1.3.15
Alternative name(s):
    (S)-2-hydroxy-acid oxidase, peroxisomal
    Medium chain alpha-hydroxy acid oxidase
    Medium-chain L-2-hydroxy acid oxidase
Gene names
Name: Hao2
Synonyms: Hao3, Haox2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Has 2-hydroxyacid oxidase activity. Most active on medium-chain substrates.

Catalytic activity

(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.

Cofactor

FMN.

Subunit structure

Homotetramer or homooctamer By similarity.

Subcellular location

Peroxisome.

Tissue specificity

Pancreas.

Sequence similarities

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.

Contains 1 FMN hydroxy acid dehydrogenase domain.

Caution

Was originally (Ref.1) thought to originate from human.

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Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processfatty acid metabolic process Ref.1

Traceable author statement. Source: ProtInc

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

peroxisome Ref.1

Traceable author statement. Source: ProtInc

   Molecular function(S)-2-hydroxy-acid oxidase activity Ref.1

Traceable author statement. Source: ProtInc

FMN binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 353353Hydroxyacid oxidase 2
PRO_0000206321

Regions

Domain1 – 353353FMN hydroxy acid dehydrogenase
Nucleotide binding279 – 30325FMN By similarity
Motif351 – 3533Microbody targeting signal Potential

Sites

Active site2481Proton acceptor By similarity
Binding site1061FMN By similarity
Binding site1281FMN By similarity
Binding site1301Substrate By similarity
Binding site1561FMN By similarity
Binding site1651Substrate By similarity
Binding site2241FMN By similarity
Binding site2511Substrate Potential

Experimental info

Sequence conflict1641N → H in CAB96380. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Q9NYQ2-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0604D529F69DE3C7

FASTA35338,700
        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

« Hide

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References

« Hide 'large scale' references
[1]"Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases."
Jones J.M., Morrell J.C., Gould S.J.
J. Biol. Chem. 275:12590-12597(2000) [PubMed: 10777549] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Mus musculus long-chain L-2-hydroxy acid oxidase."
Spielbauer B., Conzelmann E.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Search for PTS1-containing protein in mammals."
Van Veldhoven P.P.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cecum.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF231918 mRNA. Translation: AAF40201.1.
AF272947 mRNA. Translation: AAF81795.1.
AJ251820 mRNA. Translation: CAB96380.1.
AK078908 mRNA. Translation: BAC37452.1.
IPIIPI00123412.
RefSeqNP_062418.3.
UniGeneMm.281874

3D structure databases

SMRQ9NYQ2. Positions 3-350.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9NYQ2.

Proteomic databases

PRIDEQ9NYQ2.

Genome annotation databases

EnsemblENSMUST00000029464; ENSMUSP00000029464; ENSMUSG00000027870; Mus musculus. [Genome view]
GeneID56185.
KEGGmmu:56185.
UCSCuc008qqj.1. mouse.

Organism-specific databases

CTD56185.
MGIMGI:1860477. Hao3.

Phylogenomic databases

HOGENOMHBG517781.
HOVERGENQ9NYQ2.
InParanoidQ9NYQ2.
OMATRDDNIA.
OrthoDBEOG9QZB6B.
PhylomeDBQ9NYQ2.

Enzyme and pathway databases

BRENDA1.1.3.15. 244.

Gene expression databases

ArrayExpressQ9NYQ2.
BgeeQ9NYQ2.
CleanExMM_HAO3.
GenevestigatorQ9NYQ2.
GermOnlineENSMUSG00000027870. Mus musculus.

Family and domain databases

InterProIPR012133. a-Hydoxy_acid_DH_FMN.
IPR013785. Aldolase_TIM.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameHAOX2_MOUSE
AccessionPrimary (citable) accession number: Q9NYQ2
Secondary accession number(s): Q9JHS7, Q9JI00
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents