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Q9NYQ2 (HAOX2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. 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:
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) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 353352Hydroxyacid oxidase 2
PRO_0000206321

Regions

Domain2 – 353352FMN 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
Binding site3031FMN By similarity

Experimental info

Sequence conflict1641N → H in CAB96380. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9NYQ2 [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

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cecum.
+Additional computationally mapped references.

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.
RefSeqNP_062418.3. NM_019545.4.
UniGeneMm.281874.

3D structure databases

ProteinModelPortalQ9NYQ2.
SMRQ9NYQ2. Positions 3-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000029464.

PTM databases

PhosphoSiteQ9NYQ2.

Proteomic databases

PaxDbQ9NYQ2.
PRIDEQ9NYQ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029464; ENSMUSP00000029464; ENSMUSG00000027870.
GeneID56185.
KEGGmmu:56185.
UCSCuc008qqj.2. mouse.

Organism-specific databases

CTD51179.
MGIMGI:96012. Hao2.

Phylogenomic databases

eggNOGCOG1304.
GeneTreeENSGT00390000018717.
HOGENOMHOG000217463.
HOVERGENHBG051881.
InParanoidQ9NYQ2.
KOK11517.
OMAKEXIDAL.
OrthoDBEOG7B5WW0.
PhylomeDBQ9NYQ2.
TreeFamTF313363.

Gene expression databases

BgeeQ9NYQ2.
CleanExMM_HAO3.
GenevestigatorQ9NYQ2.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
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

ChiTaRSHAO2. mouse.
NextBio311970.
PROQ9NYQ2.
SOURCESearch...

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: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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