PECR_MOUSE
ID PECR_MOUSE Reviewed; 303 AA.
AC Q99MZ7; Q9CX01; Q9JIF4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Peroxisomal trans-2-enoyl-CoA reductase {ECO:0000305};
DE Short=TERP;
DE EC=1.3.1.38 {ECO:0000250|UniProtKB:Q9JIF5};
GN Name=Pecr {ECO:0000312|MGI:MGI:2148199};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10811639; DOI=10.1074/jbc.m001168200;
RA Das A.K., Uhler M.D., Hajra A.K.;
RT "Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-
RT coenzyme A reductase cDNAs.";
RL J. Biol. Chem. 275:24333-24340(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11669066; DOI=10.2174/1386207013330832;
RA Amery L., Mannaerts G.P., Subramani S., Van Veldhoven P.P., Fransen M.;
RT "Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase
RT related protein using the M13 phage protein VI phage display technology.";
RL Comb. Chem. High Throughput Screen. 4:545-552(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Pancreas;
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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-5; LYS-17 AND LYS-32, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-83 AND LYS-97, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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. Expressed at
CC lowe level in heart and skeletal muscle. Expressed at weak level in
CC other tissues. {ECO:0000269|PubMed:10811639}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF232011; AAF69800.1; -; mRNA.
DR EMBL; AF242204; AAK28336.1; -; mRNA.
DR EMBL; AK010260; BAB26803.1; -; mRNA.
DR EMBL; BC013530; AAH13530.1; -; mRNA.
DR CCDS; CCDS35607.1; -.
DR RefSeq; NP_076012.3; NM_023523.5.
DR AlphaFoldDB; Q99MZ7; -.
DR SMR; Q99MZ7; -.
DR BioGRID; 226267; 9.
DR STRING; 10090.ENSMUSP00000027381; -.
DR iPTMnet; Q99MZ7; -.
DR PhosphoSitePlus; Q99MZ7; -.
DR SwissPalm; Q99MZ7; -.
DR REPRODUCTION-2DPAGE; Q99MZ7; -.
DR EPD; Q99MZ7; -.
DR jPOST; Q99MZ7; -.
DR MaxQB; Q99MZ7; -.
DR PaxDb; Q99MZ7; -.
DR PeptideAtlas; Q99MZ7; -.
DR PRIDE; Q99MZ7; -.
DR ProteomicsDB; 289343; -.
DR Antibodypedia; 20074; 203 antibodies from 27 providers.
DR DNASU; 111175; -.
DR Ensembl; ENSMUST00000027381; ENSMUSP00000027381; ENSMUSG00000026189.
DR GeneID; 111175; -.
DR KEGG; mmu:111175; -.
DR UCSC; uc007bki.2; mouse.
DR CTD; 55825; -.
DR MGI; MGI:2148199; Pecr.
DR VEuPathDB; HostDB:ENSMUSG00000026189; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000156882; -.
DR HOGENOM; CLU_010194_1_2_1; -.
DR InParanoid; Q99MZ7; -.
DR OMA; RIWDSKV; -.
DR OrthoDB; 1194344at2759; -.
DR PhylomeDB; Q99MZ7; -.
DR TreeFam; TF315256; -.
DR BRENDA; 1.3.1.38; 3474.
DR Reactome; R-MMU-389599; Alpha-oxidation of phytanate.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 111175; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Pecr; mouse.
DR PRO; PR:Q99MZ7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q99MZ7; protein.
DR Bgee; ENSMUSG00000026189; Expressed in right kidney and 223 other tissues.
DR ExpressionAtlas; Q99MZ7; baseline and differential.
DR Genevisible; Q99MZ7; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; ISA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; ISS:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; ISA:MGI.
DR GO; GO:0033306; P:phytol metabolic process; ISO:MGI.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein 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:0007744|PubMed:23806337"
FT CHAIN 2..303
FT /note="Peroxisomal trans-2-enoyl-CoA reductase"
FT /id="PRO_0000054741"
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:0007744|PubMed:23806337"
FT MOD_RES 5
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 17
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 32
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY49"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 179
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY49"
FT CONFLICT 89
FT /note="N -> Y (in Ref. 3; BAB26803)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..232
FT /note="AKR -> VSA (in Ref. 1; AAF69800)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..244
FT /note="PLVC -> LLAR (in Ref. 1; AAF69800)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="Y -> H (in Ref. 1; AAF69800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 32410 MW; 97AD4047A20B30D0 CRC64;
MGSWKTGQSY LAAGLLKNQV AVVTGGGTGI GKAVSRELLH LGCNVVIASR KLDRLTAAVD
ELRASLPPSS SAEVSAIQCN IRKEEEVSNL VKSTLAKYGK INFLVNNGGG QFMAPVEDIT
AKGWHAVIET NLTGTFYMCK EVYNSWMREH GGSIVNIIVL LNNGFPTAAH TGAAREGVYN
LTKSMALAWA SSGVRINCVA PGTIYSQTAV DNYGEMGQTL FEMAFDSIPA KRLGVPEEIS
PLVCFLLSPA ASYITGQLIN VDGGQALYTH AFSIPDHDNW PVGAGDLSIV KRIKESFKKK
AKL
