PECR_RAT
ID PECR_RAT Reviewed; 303 AA.
AC Q9WVK3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Peroxisomal trans-2-enoyl-CoA reductase {ECO:0000305};
DE Short=TERP;
DE EC=1.3.1.38 {ECO:0000250|UniProtKB:Q9JIF5};
DE AltName: Full=PX-2,4-DCR1;
DE AltName: Full=Peroxisomal 2,4-dienoyl-CoA reductase;
DE AltName: Full=RLF98;
GN Name=Pecr {ECO:0000312|RGD:70925};
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10561551; DOI=10.1016/s0167-4838(99)00218-6;
RA Zhang J., Underwood L.E.;
RT "Molecular cloning and characterization of a new fasting-inducible short-
RT chain dehydrogenase/reductase from rat liver.";
RL Biochim. Biophys. Acta 1435:184-190(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Naylor D.J., Koivurantac K.T., Stines A.P., Hiltunen J.K., Hoogenraad N.J.,
RA Hoj P.B.;
RT "Mitochondria and peroxisomes contain distinct isoforms of 2,4-dienoyl CoA
RT reductase that interact with an Hsp70 member: isolation and
RT characterisation of a cDNA encoding rat peroxisomal 2,4-dienoyl CoA
RT reductase.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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).
CC -!- FUNCTION: Participates in chain elongation of fatty acids. Catalyzes
CC the reduction of trans-2-enoyl-CoAs of varying chain lengths from 6:1
CC to 16:1, having maximum activity with 10:1 CoA. Has no 2,4-dienoyl-CoA
CC reductase activity. {ECO:0000250|UniProtKB:Q9JIF5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E)-enoyl-CoA + H(+) + NADPH = a 2,3-saturated acyl-CoA +
CC NADP(+); Xref=Rhea:RHEA:33763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.1.38;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33764;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexenoyl-CoA + H(+) + NADPH = hexanoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:44956, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44957;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenoyl-CoA + H(+) + NADPH = NADP(+) + octanoyl-CoA;
CC Xref=Rhea:RHEA:44952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62242;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44953;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-decenoyl-CoA + H(+) + NADPH = decanoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:44960, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:61406, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44961;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-dodecenoyl-CoA + H(+) + NADPH = dodecanoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:44964, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44965;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-tetradecenoyl-CoA + H(+) + NADPH = NADP(+) +
CC tetradecanoyl-CoA; Xref=Rhea:RHEA:44968, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61405; Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44969;
CC Evidence={ECO:0000250|UniProtKB:Q9JIF5};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q9JIF5}.
CC -!- SUBUNIT: Interacts with PEX5, probably required to target it into
CC peroxisomes. {ECO:0000250|UniProtKB:Q9BY49}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q9JIF5}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and kidney. Weakly
CC expressed in other tissues. {ECO:0000269|PubMed:10561551}.
CC -!- INDUCTION: Up-regulated by fasting. {ECO:0000269|PubMed:10561551}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF099742; AAD38447.1; -; mRNA.
DR EMBL; AF021854; AAF14047.1; -; mRNA.
DR EMBL; BC060546; AAH60546.1; -; mRNA.
DR RefSeq; NP_579833.1; NM_133299.2.
DR AlphaFoldDB; Q9WVK3; -.
DR SMR; Q9WVK3; -.
DR IntAct; Q9WVK3; 4.
DR STRING; 10116.ENSRNOP00000021512; -.
DR iPTMnet; Q9WVK3; -.
DR PhosphoSitePlus; Q9WVK3; -.
DR PRIDE; Q9WVK3; -.
DR Ensembl; ENSRNOT00000089283; ENSRNOP00000073815; ENSRNOG00000055295.
DR GeneID; 113956; -.
DR KEGG; rno:113956; -.
DR UCSC; RGD:70925; rat.
DR CTD; 55825; -.
DR RGD; 70925; Pecr.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000156882; -.
DR InParanoid; Q9WVK3; -.
DR OrthoDB; 1194344at2759; -.
DR PhylomeDB; Q9WVK3; -.
DR TreeFam; TF315256; -.
DR Reactome; R-RNO-389599; Alpha-oxidation of phytanate.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9WVK3; -.
DR Proteomes; UP000002494; Chromosome 9.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033306; P:phytol metabolic process; ISO:RGD.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; Peroxisome;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ7"
FT CHAIN 2..303
FT /note="Peroxisomal trans-2-enoyl-CoA reductase"
FT /id="PRO_0000054743"
FT MOTIF 301..303
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 23..47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ7"
FT MOD_RES 5
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ7"
FT MOD_RES 32
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ7"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY49"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ7"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ7"
FT MOD_RES 179
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY49"
SQ SEQUENCE 303 AA; 32433 MW; F137C5517D655D7B CRC64;
MGSWKSGQSY LAAGLLQNQV AVVTGGATGI GKAISRELLH LGCNVVIASR KLDRLTAAVD
ELRASQPPSS STQVTAIQCN IRKEEEVNNL VKSTLAKYGK INFLVNNAGG QFMAPAEDIT
AKGWQAVIET NLTGTFYMCK AVYNSWMKDH GGSIVNIIVL LNNGFPTAAH SGAARAGVYN
LTKTMALTWA SSGVRINCVA PGTIYSQTAV DNYGELGQTM FEMAFENIPA KRVGLPEEIS
PLVCFLLSPA ASFITGQLIN VDGGQALYTR NFTIPDHDNW PVGAGDSSFI KKVKESLKKQ
ARL
