Reviewed, UniProtKB/Swiss-Prot Q99190 (TSC13_YEAST)

Names and origin

Protein names

Recommended name:
    Enoyl reductase TSC13
    EC=1.3.1.38
Alternative name(s):
    Trans-2-enoyl-CoA reductase
    Temperature-sensitive CSG2 suppressor protein 13

Gene names

Name:	TSC13
Ordered Locus Names:	YDL015C
ORF Names:	D2865

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	310 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Ref.2 Ref.5
Catalytic activity	Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.
Subunit structure	Interacts with the fatty acid elongation system components ELO2 and ELO3. Interacts with NVJ1. Ref.2 Ref.5
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. Ref.2 Ref.5 Ref.3
Miscellaneous	Present with 23600 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the steroid 5-alpha reductase family.

Ontologies

Keywords
Biological process	Lipid synthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW very-long-chain fatty acid metabolic process Ref.2 Inferred from genetic interaction. Source: SGD
Cellular component	endoplasmic reticulum membrane Ref.2 Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from direct assay. Source: SGD
Molecular function	trans-2-enoyl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 310	310	Enoyl reductase TSC13		PRO_0000262739
Regions
	Topological domain	1 – 85	85	Cytoplasmic Potential
	Transmembrane	86 – 106	21	Potential
	Topological domain	107 – 141	35	Lumenal Potential
	Transmembrane	142 – 162	21	Potential
	Topological domain	163 – 165	3	Cytoplasmic Potential
	Transmembrane	166 – 186	21	Potential
	Topological domain	187 – 201	15	Lumenal Potential
	Transmembrane	202 – 222	21	Potential
	Topological domain	223 – 242	20	Cytoplasmic Potential
	Transmembrane	243 – 265	23	Potential
	Topological domain	266 – 268	3	Lumenal Potential
	Transmembrane	269 – 291	23	Potential
	Topological domain	292 – 310	19	Cytoplasmic Potential
Experimental info
	Mutagenesis	81	1	Q → K in TSC13-1; reduces fatty acid elongation activity by 50%. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q99190-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 006DFCDDBFFAE2E9	FASTA	310	36,768
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." 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. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae." Kohlwein S.D., Eder S., Oh C.-S., Martin C.E., Gable K., Bacikova D., Dunn T.M. Mol. Cell. Biol. 21:109-125(2001) [PubMed: 11113186] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ELO2 NAD ELO3, MUTAGENESIS OF GLN-81.
[3]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles." Kvam E., Gable K., Dunn T.M., Goldfarb D.S. Mol. Biol. Cell 16:3987-3998(2005) [PubMed: 15958487] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NVJ1.
[6]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z48432 Genomic DNA. Translation: CAA88344.1. Z74063 Genomic DNA. Translation: CAA98573.1.
PIR	S52504.
RefSeq	NP_010269.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5599N.
IntAct	Q99190. 28 interactions.
Proteomic databases
PeptideAtlas	Q99190.
PRIDE	Q99190.
Genome annotation databases
Ensembl	YDL015C. Saccharomyces cerevisiae. [Contig view]
GeneID	851547.
GenomeReviews	Gene locus YDL015C in contig Z71256_GR.
KEGG	sce:YDL015C.
NMPDR	fig|4932.3.peg.1011.
Organism-specific databases
CYGD	YDL015c.
SGD	S000002173. TSC13.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q99190.
OMA	Q99190. IANFYCH.
Enzyme and pathway databases
BRENDA	1.3.1.38. 250.
Gene expression databases
ArrayExpress	Q99190.
GermOnline	YDL015C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001104. 3-oxo-5_a-steroid_4-DH_C. [Graphical view]
Pfam	PF02544. Steroid_dh. 1 hit. [Graphical view]
PROSITE	PS50244. S5A_REDUCTASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	968961.

Entry information

Entry name

TSC13_YEAST

Accession

Primary (citable) accession number: Q99190

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)