Q08921 (TCO89_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Target of rapamycin complex 1 subunit TCO89
Short name=TORC1 subunit TCO89

Alternative name(s):
89 kDa TOR complex 1 protein

Gene names

Name:	TCO89
Ordered Locus Names:	YPL180W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	799 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions. Ref.5
Subunit structure	The target of rapamycin complex 1 (TORC1) is composed of at least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2 (TORC1-B). TORC1 binds to and is inhibited by FKBP-rapamycin.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Vacuole membrane; Peripheral membrane protein; Cytoplasmic side. Note: Also localizes to membranous structures both proximal to, yet distinct from, the plasma membrane as well as within the cell interior, probably endosomal or Golgi membranes. Ref.3 Ref.5
Miscellaneous	Present with 243 molecules/cell in log phase SD medium. Ref.4

Ontologies

Keywords
Cellular component	Cell membrane Membrane Vacuole
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	TOR signaling cascade Inferred by curator Ref.5. Source: SGD fungal-type cell wall organization Inferred from mutant phenotype Ref.5. Source: SGD glycerol metabolic process Inferred from genetic interaction. Source: SGD regulation of cell growth Inferred from physical interaction Ref.5. Source: SGD response to salt stress Inferred from mutant phenotype. Source: SGD
Cellular component	TORC1 complex Inferred from physical interaction Ref.5. Source: SGD extrinsic to internal side of plasma membrane Inferred from direct assay Ref.5. Source: SGD extrinsic to vacuolar membrane Inferred from direct assay Ref.5. Source: SGD fungal-type vacuole membrane Inferred from direct assay Ref.3. Source: SGD
Molecular function	protein binding Inferred from physical interaction Ref.5. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NAP1	P25293	2	EBI-37395,EBI-11850
TOR1	P35169	4	EBI-37395,EBI-19374

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 799	799	Target of rapamycin complex 1 subunit TCO89		PRO_0000271786
Amino acid modifications
	Modified residue	40	1	Phosphoserine Ref.8
	Modified residue	43	1	Phosphoserine Ref.8
	Modified residue	52	1	Phosphothreonine Ref.7 Ref.8 Ref.9
	Modified residue	73	1	Phosphoserine Ref.8 Ref.9
	Modified residue	84	1	Phosphoserine Ref.6 Ref.9
	Modified residue	104	1	Phosphoserine Ref.7
	Modified residue	107	1	Phosphoserine Ref.7 Ref.9
	Modified residue	120	1	Phosphoserine Ref.9
	Modified residue	124	1	Phosphothreonine Ref.9
	Modified residue	138	1	Phosphoserine Ref.9
	Modified residue	141	1	Phosphoserine Ref.9
	Modified residue	144	1	Phosphoserine Ref.9
	Modified residue	227	1	Phosphoserine Ref.9
	Modified residue	255	1	Phosphoserine Ref.9
	Modified residue	258	1	Phosphoserine Ref.9
	Modified residue	267	1	Phosphoserine Ref.9
	Modified residue	288	1	Phosphoserine Ref.9
	Modified residue	290	1	Phosphoserine Ref.8 Ref.9
	Modified residue	386	1	Phosphoserine Ref.9
	Modified residue	387	1	Phosphoserine Ref.8 Ref.9
	Modified residue	390	1	Phosphothreonine Ref.9
	Modified residue	397	1	Phosphoserine Ref.9
	Modified residue	411	1	Phosphoserine Ref.9
	Modified residue	412	1	Phosphothreonine Ref.9
	Modified residue	707	1	Phosphoserine Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Q08921 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7243C08F4C74633D	FASTA	799	88,845
	10 20 30 40 50 60 MVHRGRTLKS DTDVTSLNAS TVSHQSKPFR QFSTRSRAKS NASFKGLRRV LTHDGTLDND 70 80 90 100 110 120 YFNKHNVSQK CKSSDALFRK RTISGLNMTA LTRVKSNQGK RSASFHSPVH NTLLSPKNSS 130 140 150 160 170 180 HSNTGTAGFG LKPRRSKSTQ SVLSLRDAQE SKKSESTTDE EVECFSEDNI EDGKVNNDKV 190 200 210 220 230 240 IAEHVMPEEK KNVQQLNQNE LQSPDSIDEQ EEDKSGTDGK ENHRAVSLPL PHLSSNNYFG 250 260 270 280 290 300 ESSHSIEHQK DGETSPSSIE TKLNATSVIN EEGQSKVTKE ADIDDLSSHS QNLRASLVKA 310 320 330 340 350 360 GDNISEAPYD KEKKILDVGN TLAAHKSNQK PSHSDEQFDQ EDHIDAPRSN SSRKSDSSFM 370 380 390 400 410 420 SLRRQSSKQH KLLNEEEDLI KPDDISSAGT KDIEGHSLLE NYAPNMILSQ STGVERRFEN 430 440 450 460 470 480 SSSIQNSLGN EIHDSGEHMA SGDTFNELDD GKLRKSKKNG GRSQLGQNIP NSQSTFPTIA 490 500 510 520 530 540 NIGSKDNNVP QHNFSTSISS LTNNLRRAAP ESFHGSRMNN IFHKKGNQNL LLRSNDLNKN 550 560 570 580 590 600 SAAPASPLSN EHITSSTNSG SDANRQSNSG AKFNSFAQFL KSDGIDAESR TQRKLWLQRE 610 620 630 640 650 660 NSIMDLSSQN DGSDSIFMAG NIDAKREFER ISHEYSNVKR FYNPLDEALL RVQPIITGNA 670 680 690 700 710 720 NNIRKKSHND AQSIAHSSSD TDHKDEDDLL FTNYDKKFDD LYPHLASAKI QAVLSGIWKS 730 740 750 760 770 780 ESYLFNKDVN PINKNRTTST NHSVGHTASQ NARNLLRGPM GSSTTLHHQR VINSLQPTTR 790 AVNRRMENVG YMHTQPQQR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[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]	"TOR complex 1 includes a novel component, Tco89p (YPL180w), and cooperates with Ssd1p to maintain cellular integrity in Saccharomyces cerevisiae." Reinke A., Anderson S., McCaffery J.M., Yates J.R. III, Aronova S., Chu S., Fairclough S., Iverson C., Wedaman K.P., Powers T. J. Biol. Chem. 279:14752-14762(2004) [PubMed: 14736892] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN TORC1, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[6]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, MASS SPECTROMETRY. Strain: YAL6B.
[7]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52; SER-104 AND SER-107, MASS SPECTROMETRY.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-43; THR-52; SER-73; SER-290 AND SER-387, MASS SPECTROMETRY.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52; SER-73; SER-84; SER-107; SER-120; THR-124; SER-138; SER-141; SER-144; SER-227; SER-255; SER-258; SER-267; SER-288; SER-290; SER-386; SER-387; THR-390; SER-397; SER-411; THR-412 AND SER-707, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z73536 Genomic DNA. Translation: CAA97887.1. BK006949 Genomic DNA. Translation: DAA11254.1.
PIR	S65192.
RefSeq	NP_015145.1. NM_001183994.1.
3D structure databases
ProteinModelPortal	Q08921.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5347N.
IntAct	Q08921. 18 interactions.
MINT	MINT-551152.
STRING	Q08921.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YPL180W; YPL180W; YPL180W.
GeneID	855922.
KEGG	sce:YPL180W.
NMPDR	fig|4932.3.peg.6274.
Organism-specific databases
CYGD	YPL180w.
SGD	S000006101. TCO89.
Phylogenomic databases
eggNOG	fuNOG09905.
OMA	MILSQST.
OrthoDB	EOG40P7GD.
Gene expression databases
ArrayExpress	Q08921.
Genevestigator	Q08921.
Family and domain databases
InterPro	IPR018857. TORC1_cplx_su_TCO89. [Graphical view]
Pfam	PF10452. TCO89. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	980646.

Entry information

Entry name

TCO89_YEAST

Accession

Primary (citable) accession number: Q08921
Secondary accession number(s): D6W3I8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program