HAOX2_MOUSE
ID HAOX2_MOUSE Reviewed; 353 AA.
AC Q9NYQ2; Q9JHS7; Q9JI00;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=2-Hydroxyacid oxidase 2;
DE Short=HAOX2;
DE EC=1.1.3.15 {ECO:0000305|PubMed:10777549};
DE AltName: Full=(S)-2-hydroxy-acid oxidase, peroxisomal;
DE AltName: Full=Medium chain alpha-hydroxy acid oxidase;
DE AltName: Full=Medium-chain L-2-hydroxy acid oxidase;
GN Name=Hao2; Synonyms=Hao3, Haox2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND PATHWAY.
RX PubMed=10777549; DOI=10.1074/jbc.275.17.12590;
RA Jones J.M., Morrell J.C., Gould S.J.;
RT "Identification and characterization of HAOX1, HAOX2, and HAOX3, three
RT human peroxisomal 2-hydroxy acid oxidases.";
RL J. Biol. Chem. 275:12590-12597(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Spielbauer B., Conzelmann E.;
RT "Mus musculus long-chain L-2-hydroxy acid oxidase.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Van Veldhoven P.P.;
RT "Search for PTS1-containing protein in mammals.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Oxidase that catalyzes the oxidation of medium chain
CC hydroxyacids such as 2-hydroxyoctanoate, to the correspondong 2-
CC oxoacids. Its role in the oxidation of 2-hydroxy fatty acids may
CC contribute to the general pathway of fatty acid alpha-oxidation. Active
CC in vitro with the artificial electron acceptor 2,6-
CC dichlorophenolindophenol (DCIP), but O2 is believed to be the
CC physiological electron acceptor, leading to the production of H2O2. Is
CC not active on glycolate, glyoxylate, L-lactate, 2-hydroxybutanoate and
CC 2-hydroxyhexadecanoate. {ECO:0000269|PubMed:10777549}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2;
CC Xref=Rhea:RHEA:16789, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:35179, ChEBI:CHEBI:58123; EC=1.1.3.15;
CC Evidence={ECO:0000305|PubMed:10777549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790;
CC Evidence={ECO:0000305|PubMed:10777549};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyoctanoate + O2 = 2-oxooctanoate + H2O2;
CC Xref=Rhea:RHEA:67940, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:133514, ChEBI:CHEBI:176689;
CC Evidence={ECO:0000305|PubMed:10777549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67941;
CC Evidence={ECO:0000305|PubMed:10777549};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9UJM8};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:10777549}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9UJM8}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10777549}.
CC -!- TISSUE SPECIFICITY: Pancreas.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
CC -!- CAUTION: Was originally thought to originate from human.
CC {ECO:0000305|PubMed:10777549}.
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DR EMBL; AF231918; AAF40201.1; -; mRNA.
DR EMBL; AF272947; AAF81795.1; -; mRNA.
DR EMBL; AJ251820; CAB96380.1; -; mRNA.
DR EMBL; AK078908; BAC37452.1; -; mRNA.
DR CCDS; CCDS17671.1; -.
DR RefSeq; NP_062418.3; NM_019545.4.
DR RefSeq; XP_011238471.1; XM_011240169.2.
DR AlphaFoldDB; Q9NYQ2; -.
DR SMR; Q9NYQ2; -.
DR STRING; 10090.ENSMUSP00000029464; -.
DR iPTMnet; Q9NYQ2; -.
DR PhosphoSitePlus; Q9NYQ2; -.
DR jPOST; Q9NYQ2; -.
DR MaxQB; Q9NYQ2; -.
DR PaxDb; Q9NYQ2; -.
DR PRIDE; Q9NYQ2; -.
DR ProteomicsDB; 269764; -.
DR Antibodypedia; 33905; 119 antibodies from 22 providers.
DR DNASU; 56185; -.
DR Ensembl; ENSMUST00000029464; ENSMUSP00000029464; ENSMUSG00000027870.
DR GeneID; 56185; -.
DR KEGG; mmu:56185; -.
DR UCSC; uc008qqj.2; mouse.
DR CTD; 51179; -.
DR MGI; MGI:96012; Hao2.
DR VEuPathDB; HostDB:ENSMUSG00000027870; -.
DR eggNOG; KOG0538; Eukaryota.
DR GeneTree; ENSGT00390000018717; -.
DR HOGENOM; CLU_020639_6_1_1; -.
DR InParanoid; Q9NYQ2; -.
DR OMA; FQYEIYL; -.
DR OrthoDB; 879633at2759; -.
DR PhylomeDB; Q9NYQ2; -.
DR TreeFam; TF313363; -.
DR BRENDA; 1.1.3.15; 3474.
DR Reactome; R-MMU-390918; Peroxisomal lipid metabolism.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 56185; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Hao2; mouse.
DR PRO; PR:Q9NYQ2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9NYQ2; protein.
DR Bgee; ENSMUSG00000027870; Expressed in left colon and 47 other tissues.
DR Genevisible; Q9NYQ2; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; ISO:MGI.
DR GO; GO:0010181; F:FMN binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019395; P:fatty acid oxidation; ISO:MGI.
DR GO; GO:0018924; P:mandelate metabolic process; ISO:MGI.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Flavoprotein; FMN; Lipid metabolism; Oxidoreductase;
KW Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..353
FT /note="2-Hydroxyacid oxidase 2"
FT /id="PRO_0000206321"
FT DOMAIN 2..353
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT MOTIF 351..353
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 77..79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 128
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 130
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 156
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 165
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 224
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 251
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 279..283
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 302..303
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 164
FT /note="N -> H (in Ref. 3; CAB96380)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 38700 MW; 0604D529F69DE3C7 CRC64;
MSLLCLADFK AQAQKQLSKT SWDFIEGEAD DGITYNDNLA AFRRIRLRPR YLRDVSKIDT
RTTIQGQEIN APICISPTAF HSIAWADGEK STAKAAQKAN ICYVISSYAS YTVEDIVAAA
PGGLHWFQLY VQPDWDINKQ MVQRIEALGF KALVVTVDAP VLGNRRGNKR SLLDLEANIK
LKDLRSPGES KSGLPTPLSM PSSSSCWNDL PLLQSMTRLP IILKGILTKE DAELAVKHNI
RGIIVSNHGG RQLDEVPASI DALREVVAAV NGKIEVYMDG GVRTGNDVLK ALALGARCIF
LGRPIIWGLA CKGEDGVKEV LDILKEELHT CMALSGCRSV AEISPDLIQF SRL
