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Protein

Hydroxyacid oxidase 2

Gene

Hao2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061FMNPROSITE-ProRule annotation
Binding sitei128 – 1281FMNPROSITE-ProRule annotation
Binding sitei130 – 1301SubstratePROSITE-ProRule annotation
Binding sitei156 – 1561FMNPROSITE-ProRule annotation
Binding sitei165 – 1651SubstratePROSITE-ProRule annotation
Binding sitei224 – 2241FMNPROSITE-ProRule annotation
Active sitei248 – 2481Proton acceptorPROSITE-ProRule annotation
Binding sitei251 – 2511SubstratePROSITE-ProRule annotation
Binding sitei303 – 3031FMNPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi279 – 30325FMNPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:96012. Hao2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 353352Hydroxyacid oxidase 2PRO_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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 353352FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi351 – 3533Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1304.
GeneTreeiENSGT00390000018717.
HOGENOMiHOG000217463.
HOVERGENiHBG051881.
InParanoidiQ9NYQ2.
KOiK11517.
OMAiSKTSWDF.
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

        10         20         30         40         50
MSLLCLADFK AQAQKQLSKT SWDFIEGEAD DGITYNDNLA AFRRIRLRPR
60 70 80 90 100
YLRDVSKIDT RTTIQGQEIN APICISPTAF HSIAWADGEK STAKAAQKAN
110 120 130 140 150
ICYVISSYAS YTVEDIVAAA PGGLHWFQLY VQPDWDINKQ MVQRIEALGF
160 170 180 190 200
KALVVTVDAP VLGNRRGNKR SLLDLEANIK LKDLRSPGES KSGLPTPLSM
210 220 230 240 250
PSSSSCWNDL PLLQSMTRLP IILKGILTKE DAELAVKHNI RGIIVSNHGG
260 270 280 290 300
RQLDEVPASI DALREVVAAV NGKIEVYMDG GVRTGNDVLK ALALGARCIF
310 320 330 340 350
LGRPIIWGLA CKGEDGVKEV LDILKEELHT CMALSGCRSV AEISPDLIQF

SRL
Length:353
Mass (Da):38,700
Last modified:October 1, 2000 - v1
Checksum:i0604D529F69DE3C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641N → H in CAB96380 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9NYQ2.
SMRiQ9NYQ2. Positions 3-352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029464.

PTM databases

PhosphoSiteiQ9NYQ2.

Proteomic databases

MaxQBiQ9NYQ2.
PaxDbiQ9NYQ2.
PRIDEiQ9NYQ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51179.
MGIiMGI:96012. Hao2.

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiHao2. mouse.
NextBioi311970.
PROiQ9NYQ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NYQ2.
CleanExiMM_HAO3.
GenevestigatoriQ9NYQ2.

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]
ProtoNetiSearch...

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: May 27, 2015
This is version 129 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 thought to originate from human.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.