TECR_YEAST
ID TECR_YEAST Reviewed; 310 AA.
AC Q99190; D6VRX4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Very-long-chain enoyl-CoA reductase {ECO:0000305};
DE EC=1.3.1.93 {ECO:0000269|PubMed:11113186};
DE AltName: Full=Enoyl reductase TSC13;
DE AltName: Full=Temperature-sensitive CSG2 suppressor protein 13;
DE AltName: Full=Trans-2-enoyl-CoA reductase;
GN Name=TSC13; OrderedLocusNames=YDL015C; ORFNames=D2865;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, INTERACTION
RP WITH ELO2 AND ELO3, AND MUTAGENESIS OF GLN-81.
RX PubMed=11113186; DOI=10.1128/mcb.21.1.109-125.2001;
RA Kohlwein S.D., Eder S., Oh C.-S., Martin C.E., Gable K., Bacikova D.,
RA Dunn T.M.;
RT "Tsc13p is required for fatty acid elongation and localizes to a novel
RT structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 21:109-125(2001).
RN [4]
RP CATALYTIC ACTIVITY.
RX PubMed=12087109; DOI=10.1074/jbc.m205620200;
RA Han G., Gable K., Kohlwein S.D., Beaudoin F., Napier J.A., Dunn T.M.;
RT "The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of
RT the microsomal fatty acid elongase.";
RL J. Biol. Chem. 277:35440-35449(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NVJ1.
RX PubMed=15958487; DOI=10.1091/mbc.e05-04-0290;
RA Kvam E., Gable K., Dunn T.M., Goldfarb D.S.;
RT "Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-
RT chain fatty acids in the biogenesis of microautophagic vesicles.";
RL Mol. Biol. Cell 16:3987-3998(2005).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP CATALYTIC ACTIVITY.
RX PubMed=17719544; DOI=10.1016/j.cell.2007.06.031;
RA Denic V., Weissman J.S.;
RT "A molecular caliper mechanism for determining very long-chain fatty acid
RT length.";
RL Cell 130:663-677(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the last of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of 2 carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme
CC reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA
CC that can be further elongated by entering a new cycle of elongation.
CC Thereby, it participates in the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators. VLCFAs serve for
CC instance as precursors for ceramide and sphingolipids. Required for
CC normal biogenesis of piecemeal microautophagy of the nucleus (PMN)
CC bleps and vesicles during nutrient stress.
CC {ECO:0000269|PubMed:11113186, ECO:0000269|PubMed:15958487}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain 2,3-saturated fatty acyl-CoA + NADP(+) = a
CC very-long-chain (2E)-enoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:14473,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83724, ChEBI:CHEBI:83728; EC=1.3.1.93;
CC Evidence={ECO:0000269|PubMed:11113186};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14475;
CC Evidence={ECO:0000305|PubMed:11113186};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + octadecanoyl-CoA = (2E)-octadecenoyl-CoA + H(+) +
CC NADPH; Xref=Rhea:RHEA:35351, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:71412;
CC Evidence={ECO:0000269|PubMed:12087109, ECO:0000269|PubMed:17719544};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35353;
CC Evidence={ECO:0000305|PubMed:12087109, ECO:0000305|PubMed:17719544};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-eicosenoyl-CoA + H(+) + NADPH = eicosanoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:39179, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:74691;
CC Evidence={ECO:0000269|PubMed:17719544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39180;
CC Evidence={ECO:0000305|PubMed:17719544};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-docosenoyl-CoA + H(+) + NADPH = docosanoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:39191, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65059, ChEBI:CHEBI:74692;
CC Evidence={ECO:0000269|PubMed:17719544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39192;
CC Evidence={ECO:0000305|PubMed:17719544};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-tetracosenoyl-CoA + H(+) + NADPH = NADP(+) +
CC tetracosanoyl-CoA; Xref=Rhea:RHEA:39203, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65052,
CC ChEBI:CHEBI:74693; Evidence={ECO:0000269|PubMed:17719544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39204;
CC Evidence={ECO:0000305|PubMed:17719544};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexacosenoyl-CoA + H(+) + NADPH = hexacosanoyl-CoA +
CC NADP(+); Xref=Rhea:RHEA:39215, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:64868, ChEBI:CHEBI:74281;
CC Evidence={ECO:0000269|PubMed:17719544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39216;
CC Evidence={ECO:0000305|PubMed:17719544};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:11113186}.
CC -!- SUBUNIT: Interacts with the fatty acid elongation system components
CC ELO2 and ELO3. Interacts with NVJ1. {ECO:0000269|PubMed:11113186,
CC ECO:0000269|PubMed:15958487}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11113186, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15958487}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11113186, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15958487}. Note=Accumulates at nucleus-vacuole (NV)
CC junctions. Sequestred to NV junctions by NVJ1. Accumulates in nuclear
CC PMN bleps and vesicles during stationary phase and nitrogen starvation.
CC {ECO:0000269|PubMed:11113186, ECO:0000269|PubMed:15958487}.
CC -!- MISCELLANEOUS: Present with 23600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; Z48432; CAA88344.1; -; Genomic_DNA.
DR EMBL; Z74063; CAA98573.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11834.1; -; Genomic_DNA.
DR PIR; S52504; S52504.
DR RefSeq; NP_010269.1; NM_001180074.1.
DR AlphaFoldDB; Q99190; -.
DR SMR; Q99190; -.
DR BioGRID; 32039; 414.
DR DIP; DIP-5599N; -.
DR IntAct; Q99190; 28.
DR MINT; Q99190; -.
DR STRING; 4932.YDL015C; -.
DR SwissLipids; SLP:000000503; -.
DR iPTMnet; Q99190; -.
DR MaxQB; Q99190; -.
DR PaxDb; Q99190; -.
DR PRIDE; Q99190; -.
DR EnsemblFungi; YDL015C_mRNA; YDL015C; YDL015C.
DR GeneID; 851547; -.
DR KEGG; sce:YDL015C; -.
DR SGD; S000002173; TSC13.
DR VEuPathDB; FungiDB:YDL015C; -.
DR eggNOG; KOG1639; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_059260_0_0_1; -.
DR InParanoid; Q99190; -.
DR OMA; TVFVIEY; -.
DR BioCyc; MetaCyc:G3O-29445-MON; -.
DR BioCyc; YEAST:G3O-29445-MON; -.
DR BRENDA; 1.3.1.93; 984.
DR Reactome; R-SCE-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q99190; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q99190; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IMP:SGD.
DR GO; GO:0102758; F:very-long-chain enoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:SGD.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039357; SRD5A/TECR.
DR PANTHER; PTHR10556; PTHR10556; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..310
FT /note="Very-long-chain enoyl-CoA reductase"
FT /id="PRO_0000262739"
FT TOPO_DOM 1..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..141
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..201
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 243..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..268
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 269..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT MUTAGEN 81
FT /note="Q->K: In TSC13-1; reduces fatty acid elongation
FT activity by 50%."
FT /evidence="ECO:0000269|PubMed:11113186"
SQ SEQUENCE 310 AA; 36768 MW; 006DFCDDBFFAE2E9 CRC64;
MPITIKSRSK GLRDTEIDLS KKPTLDDVLK KISANNHNIS KYRIRLTYKK ESKQVPVISE
SFFQEEADDS MEFFIKDLGP QISWRLVFFC EYLGPVLVHS LFYYLSTIPT VVDRWHSASS
DYNPFLNRVA YFLILGHYGK RLFETLFVHQ FSLATMPIFN LFKNCFHYWV LSGLISFGYF
GYGFPFGNAK LFKYYSYLKL DDLSTLIGLF VLSELWNFYC HIKLRLWGDY QKKHGNAKIR
VPLNQGIFNL FVAPNYTFEV WSWIWFTFVF KFNLFAVLFL TVSTAQMYAW AQKKNKKYHT
RRAFLIPFVF
