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Q9NYQ2

- HAOX2_MOUSE

UniProt

Q9NYQ2 - HAOX2_MOUSE

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Protein
Hydroxyacid oxidase 2
Gene
Hao2, Hao3, Haox2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Cofactori

FMN.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061FMN By similarity
Binding sitei128 – 1281FMN By similarity
Binding sitei130 – 1301Substrate By similarity
Binding sitei156 – 1561FMN By similarity
Binding sitei165 – 1651Substrate By similarity
Binding sitei224 – 2241FMN By similarity
Active sitei248 – 2481Proton acceptor By similarity
Binding sitei251 – 2511Substrate Reviewed prediction
Binding sitei303 – 3031FMN By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi279 – 30325FMN By similarity
Add
BLAST

GO - Molecular functioni

  1. FMN binding Source: Ensembl
  2. long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB-EC
  3. medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
  4. very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. fatty acid oxidation Source: Ensembl
  2. mandelate metabolic process Source: Ensembl
  3. protein homooligomerization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyacid oxidase 2 (EC:1.1.3.15)
Short name:
HAOX2
Alternative name(s):
(S)-2-hydroxy-acid oxidase, peroxisomal
Medium chain alpha-hydroxy acid oxidase
Medium-chain L-2-hydroxy acid oxidase
Gene namesi
Name:Hao2
Synonyms:Hao3, Haox2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:96012. Hao2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: MGI
  2. peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 353352Hydroxyacid oxidase 2
PRO_0000206321Add
BLAST

Proteomic databases

MaxQBiQ9NYQ2.
PaxDbiQ9NYQ2.
PRIDEiQ9NYQ2.

PTM databases

PhosphoSiteiQ9NYQ2.

Expressioni

Tissue specificityi

Pancreas.

Gene expression databases

BgeeiQ9NYQ2.
CleanExiMM_HAO3.
GenevestigatoriQ9NYQ2.

Interactioni

Subunit structurei

Homotetramer or homooctamer By similarity.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029464.

Structurei

3D structure databases

ProteinModelPortaliQ9NYQ2.
SMRiQ9NYQ2. Positions 3-352.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 353352FMN hydroxy acid dehydrogenase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi351 – 3533Microbody targeting signal Reviewed prediction

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1304.
GeneTreeiENSGT00390000018717.
HOGENOMiHOG000217463.
HOVERGENiHBG051881.
InParanoidiQ9NYQ2.
KOiK11517.
OMAiTAFHSIA.
OrthoDBiEOG7B5WW0.
PhylomeDBiQ9NYQ2.
TreeFamiTF313363.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NYQ2-1 [UniParc]FASTAAdd to Basket

« Hide

MSLLCLADFK AQAQKQLSKT SWDFIEGEAD DGITYNDNLA AFRRIRLRPR    50
YLRDVSKIDT RTTIQGQEIN APICISPTAF HSIAWADGEK STAKAAQKAN 100
ICYVISSYAS YTVEDIVAAA PGGLHWFQLY VQPDWDINKQ MVQRIEALGF 150
KALVVTVDAP VLGNRRGNKR SLLDLEANIK LKDLRSPGES KSGLPTPLSM 200
PSSSSCWNDL PLLQSMTRLP IILKGILTKE DAELAVKHNI RGIIVSNHGG 250
RQLDEVPASI DALREVVAAV NGKIEVYMDG GVRTGNDVLK ALALGARCIF 300
LGRPIIWGLA CKGEDGVKEV LDILKEELHT CMALSGCRSV AEISPDLIQF 350
SRL 353
Length:353
Mass (Da):38,700
Last modified:October 1, 2000 - v1
Checksum:i0604D529F69DE3C7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641N → H in CAB96380. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF231918 mRNA. Translation: AAF40201.1.
AF272947 mRNA. Translation: AAF81795.1.
AJ251820 mRNA. Translation: CAB96380.1.
AK078908 mRNA. Translation: BAC37452.1.
CCDSiCCDS17671.1.
RefSeqiNP_062418.3. NM_019545.4.
UniGeneiMm.281874.

Genome annotation databases

EnsembliENSMUST00000029464; ENSMUSP00000029464; ENSMUSG00000027870.
GeneIDi56185.
KEGGimmu:56185.
UCSCiuc008qqj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF231918 mRNA. Translation: AAF40201.1 .
AF272947 mRNA. Translation: AAF81795.1 .
AJ251820 mRNA. Translation: CAB96380.1 .
AK078908 mRNA. Translation: BAC37452.1 .
CCDSi CCDS17671.1.
RefSeqi NP_062418.3. NM_019545.4.
UniGenei Mm.281874.

3D structure databases

ProteinModelPortali Q9NYQ2.
SMRi Q9NYQ2. Positions 3-352.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000029464.

PTM databases

PhosphoSitei Q9NYQ2.

Proteomic databases

MaxQBi Q9NYQ2.
PaxDbi Q9NYQ2.
PRIDEi Q9NYQ2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029464 ; ENSMUSP00000029464 ; ENSMUSG00000027870 .
GeneIDi 56185.
KEGGi mmu:56185.
UCSCi uc008qqj.2. mouse.

Organism-specific databases

CTDi 51179.
MGIi MGI:96012. Hao2.

Phylogenomic databases

eggNOGi COG1304.
GeneTreei ENSGT00390000018717.
HOGENOMi HOG000217463.
HOVERGENi HBG051881.
InParanoidi Q9NYQ2.
KOi K11517.
OMAi TAFHSIA.
OrthoDBi EOG7B5WW0.
PhylomeDBi Q9NYQ2.
TreeFami TF313363.

Miscellaneous databases

ChiTaRSi HAO2. mouse.
NextBioi 311970.
PROi Q9NYQ2.
SOURCEi Search...

Gene expression databases

Bgeei Q9NYQ2.
CleanExi MM_HAO3.
Genevestigatori Q9NYQ2.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view ]
Pfami PF01070. FMN_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEi PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiHAOX2_MOUSE
AccessioniPrimary (citable) accession number: Q9NYQ2
Secondary accession number(s): Q9JHS7, Q9JI00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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