ACOX3_HUMAN
ID ACOX3_HUMAN Reviewed; 700 AA.
AC O15254; Q96AJ8;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 3;
DE EC=1.3.3.6 {ECO:0000250|UniProtKB:Q63448};
DE AltName: Full=Branched-chain acyl-CoA oxidase;
DE Short=BRCACox;
DE AltName: Full=Pristanoyl-CoA oxidase {ECO:0000250|UniProtKB:Q63448};
GN Name=ACOX3; Synonyms=BRCOX, PRCOX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9271077; DOI=10.1042/bj3250593;
RA Vanhooren J.C.T., Marynen P., Mannaerts G.P., van Veldhoven P.P.;
RT "Evidence for the existence of a pristanoyl-CoA oxidase gene in man.";
RL Biochem. J. 325:593-599(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-281, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids.
CC {ECO:0000250|UniProtKB:Q63448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-pristanoyl-CoA + O2 = (2E)-pristenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40459, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:77099, ChEBI:CHEBI:77293;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40460;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40319, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:74693;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + O2 = (2E)-hexadecenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:61526;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanedioyl-CoA + O2 = (2E)-hexadecenedioyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40275, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:77075, ChEBI:CHEBI:77085;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15254-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15254-2; Sequence=VSP_023355, VSP_023356;
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; Y11411; CAA72214.1; -; mRNA.
DR EMBL; BC017053; AAH17053.1; -; mRNA.
DR CCDS; CCDS3401.1; -. [O15254-1]
DR CCDS; CCDS47017.1; -. [O15254-2]
DR RefSeq; NP_001095137.1; NM_001101667.1. [O15254-2]
DR RefSeq; NP_003492.2; NM_003501.2. [O15254-1]
DR RefSeq; XP_005248068.1; XM_005248011.4.
DR RefSeq; XP_005248070.1; XM_005248013.3.
DR RefSeq; XP_011511867.1; XM_011513565.2. [O15254-1]
DR AlphaFoldDB; O15254; -.
DR SMR; O15254; -.
DR BioGRID; 113907; 70.
DR IntAct; O15254; 9.
DR MINT; O15254; -.
DR STRING; 9606.ENSP00000348775; -.
DR ChEMBL; CHEMBL4105817; -.
DR iPTMnet; O15254; -.
DR PhosphoSitePlus; O15254; -.
DR BioMuta; ACOX3; -.
DR EPD; O15254; -.
DR jPOST; O15254; -.
DR MassIVE; O15254; -.
DR MaxQB; O15254; -.
DR PaxDb; O15254; -.
DR PeptideAtlas; O15254; -.
DR PRIDE; O15254; -.
DR ProteomicsDB; 48541; -. [O15254-1]
DR ProteomicsDB; 48542; -. [O15254-2]
DR Antibodypedia; 52278; 116 antibodies from 23 providers.
DR DNASU; 8310; -.
DR Ensembl; ENST00000356406.10; ENSP00000348775.4; ENSG00000087008.16. [O15254-1]
DR Ensembl; ENST00000413009.6; ENSP00000413994.2; ENSG00000087008.16. [O15254-2]
DR Ensembl; ENST00000503233.5; ENSP00000421625.1; ENSG00000087008.16. [O15254-1]
DR GeneID; 8310; -.
DR KEGG; hsa:8310; -.
DR MANE-Select; ENST00000356406.10; ENSP00000348775.4; NM_003501.3; NP_003492.2.
DR UCSC; uc003glc.5; human. [O15254-1]
DR CTD; 8310; -.
DR DisGeNET; 8310; -.
DR GeneCards; ACOX3; -.
DR HGNC; HGNC:121; ACOX3.
DR HPA; ENSG00000087008; Low tissue specificity.
DR MIM; 603402; gene.
DR neXtProt; NX_O15254; -.
DR OpenTargets; ENSG00000087008; -.
DR PharmGKB; PA24445; -.
DR VEuPathDB; HostDB:ENSG00000087008; -.
DR eggNOG; KOG0135; Eukaryota.
DR GeneTree; ENSGT00940000159423; -.
DR HOGENOM; CLU_014629_4_2_1; -.
DR InParanoid; O15254; -.
DR OMA; YVTRAPI; -.
DR OrthoDB; 226134at2759; -.
DR PhylomeDB; O15254; -.
DR TreeFam; TF314226; -.
DR PathwayCommons; O15254; -.
DR Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; O15254; -.
DR UniPathway; UPA00661; -.
DR BioGRID-ORCS; 8310; 9 hits in 1073 CRISPR screens.
DR ChiTaRS; ACOX3; human.
DR GeneWiki; ACOX3; -.
DR GenomeRNAi; 8310; -.
DR Pharos; O15254; Tchem.
DR PRO; PR:O15254; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O15254; protein.
DR Bgee; ENSG00000087008; Expressed in lower esophagus mucosa and 148 other tissues.
DR ExpressionAtlas; O15254; baseline and differential.
DR Genevisible; O15254; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016402; F:pristanoyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR CDD; cd01150; AXO; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR034171; ACO.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR012258; Acyl-CoA_oxidase.
DR InterPro; IPR002655; Acyl-CoA_oxidase_C.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR PANTHER; PTHR10909; PTHR10909; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR SUPFAM; SSF47203; SSF47203; 2.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; FAD; Fatty acid metabolism;
KW Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..700
FT /note="Peroxisomal acyl-coenzyme A oxidase 3"
FT /id="PRO_0000204685"
FT MOTIF 698..700
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250|UniProtKB:Q63448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VAR_SEQ 610..624
FT /note="GGYFSGEQAGEVLES -> AERRCSCPGRRDRSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023355"
FT VAR_SEQ 625..700
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023356"
FT VARIANT 34
FT /note="E -> A (in dbSNP:rs12513296)"
FT /id="VAR_030802"
FT VARIANT 497
FT /note="D -> N (in dbSNP:rs13434465)"
FT /id="VAR_030803"
FT CONFLICT 34..35
FT /note="EL -> DV (in Ref. 1; CAA72214)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..45
FT /note="ML -> NV (in Ref. 1; CAA72214)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="D -> A (in Ref. 1; CAA72214)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="A -> G (in Ref. 1; CAA72214)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="S -> K (in Ref. 1; CAA72214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 700 AA; 77629 MW; 40D1CD3DC6A620C1 CRC64;
MASTVEGGDT ALLPEFPRGP LDAYRARASF SWKELALFTE GEGMLRFKKT IFSALENDPL
FARSPGADLS LEKYRELNFL RCKRIFEYDF LSVEDMFKSP LKVPALIQCL GMYDSSLAAK
YLLHSLVFGS AVYSSGSERH LTYIQKIFRM EIFGCFALTE LSHGSNTKAI RTTAHYDPAT
EEFIIHSPDF EAAKFWVGNM GKTATHAVVF AKLCVPGDQC HGLHPFIVQI RDPKTLLPMP
GVMVGDIGKK LGQNGLDNGF AMFHKVRVPR QSLLNRMGDV TPEGTYVSPF KDVRQRFGAS
LGSLSSGRVS IVSLAILNLK LAVAIALRFS ATRRQFGPTE EEEIPVLEYP MQQWRLLPYL
AAVYALDHFS KSLFLDLVEL QRGLASGDRS ARQAELGREI HALASASKPL ASWTTQQGIQ
ECREACGGHG YLAMNRLGVL RDDNDPNCTY EGDNNILLQQ TSNYLLGLLA HQVHDGACFR
SPLKSVDFLD AYPGILDQKF EVSSVADCLD SAVALAAYKW LVCYLLRETY QKLNQEKRSG
SSDFEARNKC QVSHGRPLAL AFVELTVVQR FHEHVHQPSV PPSLRAVLGR LSALYALWSL
SRHAALLYRG GYFSGEQAGE VLESAVLALC SQLKDDAVAL VDVIAPPDFV LDSPIGRADG
ELYKNLWGAV LQESKVLERA SWWPEFSVNK PVIGSLKSKL
