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Hydroxyacid oxidase 2 (HAOX2) (EC 1.1.3.15) ((S)-2-hydroxy-acid oxidase, peroxisomal) (Medium chain alpha-hydroxy acid oxidase) (Medium-chain L-2-hydroxy acid oxidase)

 HAOX2_MOUSE             Reviewed;         353 AA.
Q9NYQ2; Q9JHS7; Q9JI00;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
30-AUG-2017, entry version 144.
RecName: Full=Hydroxyacid oxidase 2;
Short=HAOX2;
EC=1.1.3.15;
AltName: Full=(S)-2-hydroxy-acid oxidase, peroxisomal;
AltName: Full=Medium chain alpha-hydroxy acid oxidase;
AltName: Full=Medium-chain L-2-hydroxy acid oxidase;
Name=Hao2; Synonyms=Hao3, Haox2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10777549; DOI=10.1074/jbc.275.17.12590;
Jones J.M., Morrell J.C., Gould S.J.;
"Identification and characterization of HAOX1, HAOX2, and HAOX3, three
human peroxisomal 2-hydroxy acid oxidases.";
J. Biol. Chem. 275:12590-12597(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Spielbauer B., Conzelmann E.;
"Mus musculus long-chain L-2-hydroxy acid oxidase.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Van Veldhoven P.P.;
"Search for PTS1-containing protein in mammals.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cecum;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Has 2-hydroxyacid oxidase activity. Most active on
medium-chain substrates.
-!- CATALYTIC ACTIVITY: (S)-2-hydroxy acid + O(2) = 2-oxo acid +
H(2)O(2).
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
-!- SUBUNIT: Homotetramer or homooctamer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Peroxisome.
-!- TISSUE SPECIFICITY: Pancreas.
-!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
-!- CAUTION: Was originally thought to originate from human.
{ECO:0000305|PubMed:10777549}.
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EMBL; AF231918; AAF40201.1; -; mRNA.
EMBL; AF272947; AAF81795.1; -; mRNA.
EMBL; AJ251820; CAB96380.1; -; mRNA.
EMBL; AK078908; BAC37452.1; -; mRNA.
CCDS; CCDS17671.1; -.
RefSeq; NP_062418.3; NM_019545.4.
RefSeq; XP_011238471.1; XM_011240169.2.
UniGene; Mm.281874; -.
ProteinModelPortal; Q9NYQ2; -.
SMR; Q9NYQ2; -.
STRING; 10090.ENSMUSP00000029464; -.
iPTMnet; Q9NYQ2; -.
PhosphoSitePlus; Q9NYQ2; -.
MaxQB; Q9NYQ2; -.
PaxDb; Q9NYQ2; -.
PRIDE; Q9NYQ2; -.
Ensembl; ENSMUST00000029464; ENSMUSP00000029464; ENSMUSG00000027870.
GeneID; 56185; -.
KEGG; mmu:56185; -.
UCSC; uc008qqj.2; mouse.
CTD; 51179; -.
MGI; MGI:96012; Hao2.
eggNOG; KOG0538; Eukaryota.
eggNOG; COG1304; LUCA.
GeneTree; ENSGT00390000018717; -.
HOGENOM; HOG000217463; -.
HOVERGEN; HBG051881; -.
InParanoid; Q9NYQ2; -.
KO; K11517; -.
OMA; NEFHTSM; -.
OrthoDB; EOG091G0ADA; -.
PhylomeDB; Q9NYQ2; -.
TreeFam; TF313363; -.
Reactome; R-MMU-390918; Peroxisomal lipid metabolism.
ChiTaRS; Hao2; mouse.
PRO; PR:Q9NYQ2; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027870; -.
CleanEx; MM_HAO3; -.
Genevisible; Q9NYQ2; MM.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005777; C:peroxisome; ISO:MGI.
GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; ISO:MGI.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; ISO:MGI.
GO; GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
GO; GO:0019395; P:fatty acid oxidation; ISO:MGI.
CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
InterPro; IPR000262; FMN-dep_DH.
InterPro; IPR008259; FMN_hydac_DH_AS.
Pfam; PF01070; FMN_dh; 1.
PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
1: Evidence at protein level;
Complete proteome; Flavoprotein; FMN; Oxidoreductase; Peroxisome;
Phosphoprotein; Reference proteome.
CHAIN 1 353 Hydroxyacid oxidase 2.
/FTId=PRO_0000206321.
DOMAIN 2 353 FMN hydroxy acid dehydrogenase.
{ECO:0000255|PROSITE-ProRule:PRU00683}.
NP_BIND 279 303 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00683}.
MOTIF 351 353 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 248 248 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00683}.
BINDING 106 106 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00683}.
BINDING 128 128 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00683}.
BINDING 130 130 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU00683}.
BINDING 156 156 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00683}.
BINDING 165 165 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU00683}.
BINDING 224 224 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00683}.
BINDING 251 251 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU00683}.
BINDING 303 303 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00683}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 164 164 N -> H (in Ref. 3; CAB96380).
{ECO:0000305}.
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


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