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UniProtKB/Swiss-Prot entry Q99190


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TSC13_YEAST
Primary accession number Q99190
Secondary accession numbers None
Integrated into Swiss-Prot on November 28, 2006
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 47)
Name and origin of the protein
Protein name Enoyl reductase TSC13
Synonyms EC 1.3.1.38
Trans-2-enoyl-CoA reductase
Temperature-sensitive CSG2 suppressor protein 13
Gene name
Name: TSC13
OrderedLocusNames: YDL015C
ORFNames: D2865
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ELO2 NAD ELO3, AND MUTAGENESIS OF GLN-81.
DOI=10.1128/MCB.21.1.109-125.2001; PubMed=11113186 [NCBI, ExPASy, EBI, Israel, Japan]
Kohlwein S.D., Eder S., Oh C.-S., Martin C.E., Gable K., Bacikova D., Dunn T.M.;
"Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 21:109-125(2001).
[3]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NVJ1.
DOI=10.1091/mbc.E05-04-0290; PubMed=15958487 [NCBI, ExPASy, EBI, Israel, Japan]
Kvam E., Gable K., Dunn T.M., Goldfarb D.S.;
"Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles.";
Mol. Biol. Cell 16:3987-3998(2005).
[6]
TOPOLOGY [LARGE SCALE ANALYSIS].
DOI=10.1073/pnas.0604075103; PubMed=16847258 [NCBI, ExPASy, EBI, Israel, Japan]
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
Comments
  • FUNCTION: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long chain fatty acids (VLCFA) from palmitate. Catalyzes the last step in each elongation cycle that lengthens palmitate by two carbon units. VLCFAs serve as precursors for ceramide and sphingolipids. Required for normal biogenesis of piecemeal microautophagy of the nucleus (PMN) bleps and vesicles during nutrient stress.
  • CATALYTIC ACTIVITY: Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.
  • SUBUNIT: Interacts with the fatty acid elongation system components ELO2 and ELO3. Interacts with NVJ1.
  • SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Accumulates at nucleus-vacuole (NV) junctions. Sequestred to NV junctions by NVJ1. Accumulates in nuclear PMN bleps and vesicles during stationary phase and nitrogen starvation.
  • MISCELLANEOUS: Present with 23600 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the steroid 5-alpha reductase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z48432; CAA88344.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74063; CAA98573.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S52504; S52504.
RefSeq NP_010269.1; -.
3D structure databases
ModBase Q99190.
Protein-protein interaction databases
DIP DIP:5599N; -.
IntAct Q99190; 31.
Organism-specific databases
CYGD YDL015c; -.
SGD S000002173; TSC13.
Yeast-GFP YDL015C.
Gene expression databases
ArrayExpress Q99190; -.
GermOnline YDL015C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from direct assay from SGD).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0019166; Molecular function: trans-2-enoyl-CoA reductase (NADPH) activity (inferred from electronic annotation from EC).
GO:0008610; Biological process: lipid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0000038; Biological process: very-long-chain fatty acid metabolic process (inferred from genetic interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001104; 3-oxo-5_a-steroid_4-DHase_C.
Graphical view of domain structure.
Pfam PF02544; Steroid_dh; 1.
Pfam graphical view of domain structure.
PROSITE PS50244; S5A_REDUCTASE; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas Q99190; -.
Genome annotation databases
Ensembl YDL015C; Saccharomyces cerevisiae. [Contig view]
GeneID 851547; -.
GenomeReviews Z71256_GR; YDL015C.
KEGG sce:YDL015C; -.
NMPDR fig|4932.3.peg.1011; -.
Phylogenomic databases
HOGENOM Q99190; -.
Other
LinkHub Q99190; -.
NextBio 968961; -.
ProtoNet Q99190.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; Lipid synthesis; Membrane; NADP; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   310  310     Enoyl reductase TSC13. PRO_0000262739
TOPO_DOM   1    85  85     Cytoplasmic (Potential). 
TRANSMEM   86   106  21     Potential. 
TOPO_DOM   107   141  35     Lumenal (Potential). 
TRANSMEM   142   162  21     Potential. 
TOPO_DOM   163   165  3     Cytoplasmic (Potential). 
TRANSMEM   166   186  21     Potential. 
TOPO_DOM   187   201  15     Lumenal (Potential). 
TRANSMEM   202   222  21     Potential. 
TOPO_DOM   223   242  20     Cytoplasmic (Potential). 
TRANSMEM   243   265  23     Potential. 
TOPO_DOM   266   268  3     Lumenal (Potential). 
TRANSMEM   269   291  23     Potential. 
TOPO_DOM   292   310  19     Cytoplasmic (Potential). 
MUTAGEN   81    81        Q->K: In TSC13-1; reduces fatty acid elongation activity by 50%. 
Sequence information
Length: 310 AA [This is the length of the unprocessed precursor] Molecular weight: 36768 Da [This is the MW of the unprocessed precursor] CRC64: 006DFCDDBFFAE2E9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPITIKSRSK GLRDTEIDLS KKPTLDDVLK KISANNHNIS KYRIRLTYKK ESKQVPVISE 

        70         80         90        100        110        120 
SFFQEEADDS MEFFIKDLGP QISWRLVFFC EYLGPVLVHS LFYYLSTIPT VVDRWHSASS 

       130        140        150        160        170        180 
DYNPFLNRVA YFLILGHYGK RLFETLFVHQ FSLATMPIFN LFKNCFHYWV LSGLISFGYF 

       190        200        210        220        230        240 
GYGFPFGNAK LFKYYSYLKL DDLSTLIGLF VLSELWNFYC HIKLRLWGDY QKKHGNAKIR 

       250        260        270        280        290        300 
VPLNQGIFNL FVAPNYTFEV WSWIWFTFVF KFNLFAVLFL TVSTAQMYAW AQKKNKKYHT 

       310 
RRAFLIPFVF 

Q99190 in FASTA format

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