ACOX3_RAT
ID ACOX3_RAT Reviewed; 700 AA.
AC Q63448;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 3;
DE EC=1.3.3.6 {ECO:0000269|PubMed:1400324};
DE AltName: Full=Branched-chain acyl-CoA oxidase;
DE Short=BRCACox;
DE AltName: Full=Pristanoyl-CoA oxidase {ECO:0000303|PubMed:1400324};
GN Name=Acox3; Synonyms=Prcox;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND MICROBODY TARGETING.
RC TISSUE=Liver;
RX PubMed=8706733; DOI=10.1111/j.1432-1033.1996.0302u.x;
RA Vanhooren J.C.T., Fransen M., de Bethune B., Baumgart E., Baes M.,
RA Torrekens S., van Leuven F., Mannaerts G.P., van Veldhoven P.P.;
RT "Rat pristanoyl-CoA oxidase. cDNA cloning and recognition of its C-terminal
RT (SQL) by the peroxisomal-targeting signal 1 receptor.";
RL Eur. J. Biochem. 239:302-309(1996).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1400324; DOI=10.1016/s0021-9258(19)88666-0;
RA Van Veldhoven P.P., Vanhove G., Assselberghs S., Eyssen H.J.,
RA Mannaerts G.P.;
RT "Substrate specificities of rat liver peroxisomal acyl-CoA oxidases:
RT palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase
RT (non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase.";
RL J. Biol. Chem. 267:20065-20074(1992).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids.
CC {ECO:0000269|PubMed:1400324, ECO:0000269|PubMed:8706733}.
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:0000269|PubMed:1400324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000305|PubMed:1400324};
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:0000269|PubMed:1400324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40460;
CC Evidence={ECO:0000305|PubMed:1400324};
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:0000269|PubMed:1400324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320;
CC Evidence={ECO:0000305|PubMed:1400324};
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:0000269|PubMed:1400324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000305|PubMed:1400324};
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:0000269|PubMed:1400324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276;
CC Evidence={ECO:0000305|PubMed:1400324};
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|PubMed:8706733}.
CC -!- TISSUE SPECIFICITY: Most abundant in liver, kidney, lung, and testis.
CC Present in all tissues tested. {ECO:0000269|PubMed:8706733}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; X95188; CAA64487.1; -; mRNA.
DR RefSeq; NP_445791.1; NM_053339.1.
DR AlphaFoldDB; Q63448; -.
DR SMR; Q63448; -.
DR IntAct; Q63448; 1.
DR STRING; 10116.ENSRNOP00000042002; -.
DR SwissLipids; SLP:000000545; -.
DR iPTMnet; Q63448; -.
DR PhosphoSitePlus; Q63448; -.
DR jPOST; Q63448; -.
DR PaxDb; Q63448; -.
DR PRIDE; Q63448; -.
DR GeneID; 83522; -.
DR KEGG; rno:83522; -.
DR CTD; 8310; -.
DR RGD; 69245; Acox3.
DR eggNOG; KOG0135; Eukaryota.
DR InParanoid; Q63448; -.
DR OrthoDB; 226134at2759; -.
DR PhylomeDB; Q63448; -.
DR Reactome; R-RNO-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR SABIO-RK; Q63448; -.
DR UniPathway; UPA00661; -.
DR PRO; PR:Q63448; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
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; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
DR GO; GO:0016402; F:pristanoyl-CoA oxidase activity; IDA:RGD.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IDA:RGD.
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; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR PANTHER; PTHR10909; PTHR10909; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 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 Direct protein sequencing; FAD; Fatty acid metabolism; Flavoprotein;
KW Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..700
FT /note="Peroxisomal acyl-coenzyme A oxidase 3"
FT /id="PRO_0000204687"
FT MOTIF 698..700
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000269|PubMed:8706733"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15254"
FT MOD_RES 505
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPL9"
SQ SEQUENCE 700 AA; 78446 MW; DE2327CEFA7423DF CRC64;
MGSSSERRDS VLWSDIPKGP LSAYRARASF NSKELMLFWD GQDVLDFKKT IFSTLENDPL
FARPFGADLP LEKERELNFL RCKRVFEYGF FNAEDMLKNP LKILVLMNCL GMYDWSLANK
CVLHMLVFGS TIIGSGSEHH FKYLEKIYNL EIFGCFALTE LSHGSNTKAM RTTAHYDPAT
QEFILHSPDF EAAKFWVGNL GKTATHAVVF AQLYTPDGQC RGLHSFLVQI RDPKTLLPMP
GVMVGDMGKK LGQNGLDNGF AMFHKVRIPR QNLLDRTGNV TSEGHYHTPF KDVRQRLGAS
LGSLSSGRIS IISISVVNLK LAVIIAIRFS ATRRQFGPTD KEEIPVLEYP LQQWRLLPYL
AAAYALDHFS KTIFLDLIEL QRAGKVGTTV TGRQSSGREI HALASAGKPL ASWTAQRGIQ
ECREVVGGHG YLAMNRFGEL RNDNDPNCTY EGDNNVLLQQ TSNYLLSLLE HPLQDGAHFT
SPLKTVNFLE AYPGILGQKF MASSKADWLD SEAPLAAYRW LVCYLLRESH QRYCQEKKSR
GSDFEARNNS QVYGCRPLAL AFMELTVMQR FHEHTHSSSV PPSLRTVLGR LSMLYGLWCL
SQHTALLYRG GYISGEQTGK AMEDAILMLC VQLKDDAVAL VDAIAPSDFV LGSPIGRADG
ELYKNLWAAV LQQSGVLERA AWWPEFTANK SVANRLKSQL
