ID ETR1_YEAST Reviewed; 380 AA. AC P38071; Q6Q5P2; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 25-NOV-2008, entry version 76. DE RecName: Full=Enoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrial; DE EC=1.3.1.10; DE AltName: Full=Trans-2-enoyl-CoA reductase; DE EC=1.3.1.38; DE AltName: Full=Mitochondrial respiratory function protein 1; DE Flags: Precursor; GN Name=ETR1; Synonyms=MRF1, MRF1'; OrderedLocusNames=YBR026C; GN ORFNames=YBR0310; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 10-25. RC STRAIN=ATCC 26786 / X2180-1A; RX MEDLINE=94253088; PubMed=8195160; RA Yamazoe M., Shirahige K., Rashid M.B., Kaneko Y., Nakayama T., RA Ogasawara N., Yoshikawa H.; RT "A protein which binds preferentially to single-stranded core sequence RT of autonomously replicating sequence is essential for respiratory RT function in mitochondrial of Saccharomyces cerevisiae."; RL J. Biol. Chem. 269:15244-15252(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=94378725; PubMed=8091864; DOI=10.1002/yea.320100010; RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.; RT "The complete sequence of a 33 kb fragment on the right arm of RT chromosome II from Saccharomyces cerevisiae reveals 16 open reading RT frames, including ten new open reading frames, five previously RT identified genes and a homologue of the SCO1 gene."; RL Yeast 10:S75-S80(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=95112788; PubMed=7813418; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., RA Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., RA Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., RA Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., RA Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., RA Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., RA Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., RA Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., RA Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., RA Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., RA Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., RA van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., RA Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., RA Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP SUBCELLULAR LOCATION. RX MEDLINE=21393706; PubMed=11502169; DOI=10.1021/bi010277r; RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., RA Manon S., Schmitter J.-M.; RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular RT complex."; RL Biochemistry 40:9758-9769(2001). RN [6] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX MEDLINE=21400968; PubMed=11509667; RX DOI=10.1128/MCB.21.18.6243-6253.2001; RA Torkko J.M., Koivuranta K.T., Miinalainen I.J., Yagi A.I., Schmitz W., RA Kastaniotis A.J., Airenne T.T., Gurvitz A., Hiltunen K.J.; RT "Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p RT (Mrf1'p), 2-enoyl thioester reductases essential for mitochondrial RT respiratory competence."; RL Mol. Cell. Biol. 21:6243-6253(2001). RN [7] RP FUNCTION, AND MUTAGENESIS OF TYR-73. RX PubMed=12614607; DOI=10.1016/S0022-2836(03)00038-X; RA Airenne T.T., Torkko J.M., Van den plas S., Sormunen R.T., RA Kastaniotis A.J., Wierenga R.K., Hiltunen J.K.; RT "Structure-function analysis of enoyl thioester reductase involved in RT mitochondrial maintenance."; RL J. Mol. Biol. 327:47-59(2003). RN [8] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RX MEDLINE=22975177; PubMed=14576278; DOI=10.1073/pnas.2135385100; RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., RA Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., RA Rehling P., Pfanner N., Meisinger C.; RT "The proteome of Saccharomyces cerevisiae mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-339, AND RP MASS SPECTROMETRY. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). CC -!- FUNCTION: Required for respiration and the maintenance of the CC mitochondrial compartment. May have a role in the mitochondrial CC synthesis of fatty acids. CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + NADP(+) = trans- CC 2,3-dehydroacyl-[acyl-carrier-protein] + NADPH. CC -!- CATALYTIC ACTIVITY: Acyl-CoA + NADP(+) = trans-2,3-dehydroacyl-CoA CC + NADPH. CC -!- SUBUNIT: Homodimer or in a complex with other proteins. Interacts CC with ARS1. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. CC -!- CAUTION: Was originally (PubMed:8195160) thought to be a nuclear CC protein involved in transcriptional regulation of genes required CC for the functional assembly of mitochondrial respiratory proteins. CC This was later proven not to be the case (PubMed:11509667). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D26606; BAA05651.1; -; Genomic_DNA. DR EMBL; Z35895; CAA84968.1; -; Genomic_DNA. DR EMBL; X76078; CAA53683.1; -; Genomic_DNA. DR EMBL; AY557872; AAS56198.1; -; Genomic_DNA. DR RefSeq; NP_009582.1; -. DR HSSP; Q8WZM3; 1GYR. DR IntAct; P38071; -. DR PeptideAtlas; P38071; -. DR Ensembl; YBR026C; Saccharomyces cerevisiae. DR GeneID; 852314; -. DR GenomeReviews; Y13134_GR; YBR026C. DR KEGG; sce:YBR026C; -. DR NMPDR; fig|4932.3.peg.277; -. DR CYGD; YBR026c; -. DR SGD; S000000230; ETR1. DR HOGENOM; P38071; -. DR LinkHub; P38071; -. DR NextBio; 971002; -. DR GermOnline; YBR026C; Saccharomyces cerevisiae. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004319; F:enoyl-[acyl-carrier-protein] reductase (NAD...; IEA:EC. DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IMP:SGD. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR013154; AlcDHase_GroES-like. DR InterPro; IPR002085; AlcDHase_SF_Zn. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF08240; ADH_N; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; DNA-binding; KW Fatty acid biosynthesis; Lipid synthesis; Mitochondrion; NADP; KW Oxidoreductase; Phosphoprotein; Transit peptide. FT TRANSIT 1 9 Mitochondrion. FT CHAIN 10 380 Enoyl-[acyl-carrier protein] reductase FT [NADPH, B-specific], mitochondrial. FT /FTId=PRO_0000160924. FT MOD_RES 135 135 Phosphoserine. FT MOD_RES 339 339 Phosphoserine. FT MUTAGEN 73 73 Y->N: 0.1% of catalytic activity. No FT specific ARS1 binding. FT CONFLICT 24 24 I -> T (in Ref. 4; AAS56198). SQ SEQUENCE 380 AA; 42067 MW; 9795013283C3E9F8 CRC64; MLPTFKRYMS SSAHQIPKHF KSLIYSTHEV EDCTKVLSVK NYTPKQDLSQ SIVLKTLAFP INPSDINQLQ GVYPSRPEKT YDYSTDEPAA IAGNEGVFEV VSLPSGSSKG DLKLGDRVIP LQANQGTWSN YRVFSSSSDL IKVNDLDLFS AATVSVNGCT GFQLVSDYID WNSNGNEWII QNAGTSSVSK IVTQVAKAKG IKTLSVIRDR DNFDEVAKVL EDKYGATKVI SESQNNDKTF AKEVLSKILG ENARVRLALN SVGGKSSASI ARKLENNALM LTYGGMSKQP VTLPTSLHIF KGLTSKGYWV TEKNKKNPQS KIDTISDFIK MYNYGHIISP RDEIETLTWN TNTTTDEQLL ELVKKGITGK GKKKMVVLEW //