ID   MECR_RAT                Reviewed;         373 AA.
AC   Q9Z311; F1LPY7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase, mitochondrial;
DE            EC=1.3.1.104 {ECO:0000250|UniProtKB:Q9BV79};
DE   AltName: Full=2-enoyl thioester reductase {ECO:0000303|PubMed:12654921};
DE   AltName: Full=Nuclear receptor-binding factor 1;
DE            Short=NRBF-1;
DE   Flags: Precursor;
GN   Name=Mecr; Synonyms=Nrbf1;
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] (ISOFORM 1).
RX   PubMed=9795230; DOI=10.1016/s0378-1119(98)00461-2;
RA   Masuda N., Yasumo H., Furusawa T., Tsukamoto T., Sadano H., Osumi T.;
RT   "Nuclear receptor binding factor-1 (NRBF-1), a protein interacting with a
RT   wide spectrum of nuclear hormone receptors.";
RL   Gene 221:225-233(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2),
RP   AND INTERACTION WITH PPARA (ISOFORM 2).
RX   PubMed=25031892; DOI=10.3803/enm.2014.29.2.185;
RA   Kim D.G., Yoo J.C., Kim E., Lee Y.S., Yarishkin O.V., Lee da Y., Lee K.H.,
RA   Hong S.G., Hwang E.M., Park J.Y.;
RT   "A novel cytosolic isoform of mitochondrial Trans-2-Enoyl-CoA reductase
RT   enhances peroxisome proliferator-activated receptor alpha activity.";
RL   Endocrinol. Metab. 29:185-194(2014).
RN   [4]
RP   SUBCELLULAR LOCATION (ISOFORM 1).
RX   PubMed=12654921; DOI=10.1074/jbc.m302851200;
RA   Miinalainen I.J., Chen Z.-J., Torkko J.M., Pirilae P.L., Sormunen R.T.,
RA   Bergmann U., Qin Y.-M., Hiltunen J.K.;
RT   "Characterization of 2-enoyl thioester reductase from mammals: an ortholog
RT   of Ybr026p/Mrf1'p of the yeast mitochondrial fatty acid synthesis type
RT   II.";
RL   J. Biol. Chem. 278:20154-20161(2003).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of trans-2-enoyl
CC       thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis
CC       type II). Fatty acid chain elongation in mitochondria uses acyl carrier
CC       protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP
CC       and CoA thioesters as substrates in vitro. Displays a preference for
CC       medium-chain over short- and long-chain substrates (By similarity). May
CC       provide the octanoyl chain used for lipoic acid biosynthesis,
CC       regulating protein lipoylation and mitochondrial respiratory activity
CC       particularly in Purkinje cells (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BV79, ECO:0000250|UniProtKB:Q9DCS3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC         H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC         COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.104;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78453, ChEBI:CHEBI:78454;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-hexenoyl-[ACP] + H(+) + NADPH = hexanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78458, ChEBI:CHEBI:78459;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-octenoyl-[ACP] + H(+) + NADPH = NADP(+) + octanoyl-[ACP];
CC         Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78462, ChEBI:CHEBI:78463;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-decenoyl-[ACP] + H(+) + NADPH = decanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78467, ChEBI:CHEBI:78468;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-dodecenoyl-[ACP] + H(+) + NADPH = dodecanoyl-[ACP] +
CC         NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-
CC         COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:65264, ChEBI:CHEBI:78472;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-tetradecenoyl-[ACP] + H(+) + NADPH = NADP(+) +
CC         tetradecanoyl-[ACP]; Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647,
CC         Rhea:RHEA-COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78475, ChEBI:CHEBI:78477;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADPH = hexadecanoyl-[ACP] +
CC         NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-
CC         COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78481, ChEBI:CHEBI:78483;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913;
CC         Evidence={ECO:0000250|UniProtKB:Q9BV79};
CC   -!- SUBUNIT: Homodimer (By similarity). Isoform 2 interacts with PPARA in
CC       the nucleus and increases its activity (PubMed:25031892).
CC       {ECO:0000250|UniProtKB:Q9BV79, ECO:0000269|PubMed:25031892}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC       {ECO:0000269|PubMed:12654921}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000269|PubMed:25031892}. Nucleus {ECO:0000269|PubMed:25031892}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z311-1; Sequence=Displayed;
CC       Name=2; Synonyms=cMECR;
CC         IsoId=Q9Z311-2; Sequence=VSP_057305;
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:9795230) thought to be a nuclear
CC       protein that interact with nuclear receptor. However, it was shown
CC       later to be mitochondrial (PubMed:12654921), a function related to
CC       nuclear receptors being unsure. {ECO:0000305|PubMed:12654921,
CC       ECO:0000305|PubMed:9795230}.
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DR   EMBL; AB015724; BAA34804.1; -; mRNA.
DR   EMBL; AABR06040190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06040191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_058905.1; NM_017209.1. [Q9Z311-1]
DR   AlphaFoldDB; Q9Z311; -.
DR   SMR; Q9Z311; -.
DR   STRING; 10116.ENSRNOP00000031375; -.
DR   iPTMnet; Q9Z311; -.
DR   PhosphoSitePlus; Q9Z311; -.
DR   PaxDb; 10116-ENSRNOP00000031375; -.
DR   GeneID; 29470; -.
DR   KEGG; rno:29470; -.
DR   UCSC; RGD:3208; rat. [Q9Z311-1]
DR   AGR; RGD:3208; -.
DR   CTD; 51102; -.
DR   RGD; 3208; Mecr.
DR   eggNOG; KOG0025; Eukaryota.
DR   InParanoid; Q9Z311; -.
DR   OrthoDB; 6213at2759; -.
DR   PhylomeDB; Q9Z311; -.
DR   TreeFam; TF312886; -.
DR   Reactome; R-RNO-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR   PRO; PR:Q9Z311; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; ISS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IDA:RGD.
DR   GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; ISO:RGD.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR   CDD; cd08290; ETR; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43981; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43981:SF9; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW   NADP; Nucleus; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..53
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           54..373
FT                   /note="Enoyl-[acyl-carrier-protein] reductase,
FT                   mitochondrial"
FT                   /id="PRO_0000000890"
FT   ACT_SITE        94
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         167
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         193..196
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         216..218
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         285..288
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         310..312
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         368
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   MOD_RES         61
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCS3"
FT   MOD_RES         61
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCS3"
FT   MOD_RES         252
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCS3"
FT   MOD_RES         252
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCS3"
FT   MOD_RES         267
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCS3"
FT   MOD_RES         267
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCS3"
FT   MOD_RES         316
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCS3"
FT   VAR_SEQ         1..76
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057305"
SQ   SEQUENCE   373 AA;  40327 MW;  94D5A057D666320D CRC64;
     MLVSRRLTGA RARAPLLASL LEAWCRQGRT TSSYSAFSEP SHVRALVYGN HGDPAKVIQL
     KNLELTAVEG SDVHVKMLAA PINPSDINMI QGNYGLLPKL PAVGGNEGVG QVIAVGSSVS
     GLKPGDWVIP ANAGLGTWRT EAVFSEEALI GVPKDIPLQS AATLGVNPCT AYRMLVDFEQ
     LQPGDSVIQN ASNSGVGQAV IQIASALGLK TINVIRDRPD IKKLTDRLKD LGADYVLTEE
     ELRMPETKNI FKDLPLPRLA LNCVGGKSST ELLRHLAPGG TMVTYGGMAK QPVTASVSML
     IFKDLKLRGF WLSQWKKNHS PDEFKELILI LCNLIRQGQL TAPAWSGIPL QDYQQALEAS
     MKPFVSLKQI LTM
//