Reviewed, UniProtKB/Swiss-Prot Q04749 (AVO2_YEAST)

Names and origin

Protein names

Recommended name:
    Target of rapamycin complex 2 subunit AVO2
      Short name=TORC2 subunit AVO2
Alternative name(s):
    Adheres voraciously to TOR2 protein 2

Gene names

Name:	AVO2
Ordered Locus Names:	YMR068W
ORF Names:	YM9916.07

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

General annotation (Comments)

Function	Component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway.
Subunit structure	The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a homodimer. Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin. AVO2 is peripherally associated to AVO1 and TSC11. Ref.6
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Vacuole membrane; Peripheral membrane protein; Cytoplasmic side Ref.3.
Miscellaneous	Present with 1180 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Contains 5 ANK repeats.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Vacuole
Domain	ANK repeat Repeat
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	TOR signaling pathway Ref.2 Inferred by curator. Source: SGD establishment or maintenance of actin cytoskeleton polarity Ref.2 Inferred from physical interaction. Source: SGD fungal-type cell wall organization Ref.2 Inferred from physical interaction. Source: SGD regulation of cell growth Ref.2 Inferred from physical interaction. Source: SGD
Cellular component	TORC2 complex Ref.2 Inferred from physical interaction. Source: SGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW vacuole Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Ref.2 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P53060	1	EBI-28131,EBI-24228
AVO1	Q08236	1	EBI-28131,EBI-29284
ECM4	P36156	1	EBI-28131,EBI-2042717
LSB3	P43603	1	EBI-28131,EBI-22980
LST8	P41318	1	EBI-28131,EBI-28598
SLM2	P53955	1	EBI-28131,EBI-28706
TOR2	P32600	1	EBI-28131,EBI-19385
TSC11	P40061	1	EBI-28131,EBI-22621
YSC84	P32793	1	EBI-28131,EBI-24460

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 426	426	Target of rapamycin complex 2 subunit AVO2		PRO_0000067247
Regions
	Repeat	4 – 33	30	ANK 1
	Repeat	39 – 68	30	ANK 2
	Repeat	74 – 104	31	ANK 3
	Repeat	108 – 137	30	ANK 4
	Repeat	141 – 171	31	ANK 5
Amino acid modifications
	Modified residue	273	1	Phosphoserine Ref.7
	Modified residue	330	1	Phosphothreonine Ref.7
	Modified residue	332	1	Phosphothreonine Ref.7
	Modified residue	350	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q04749-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 0A17E78BF449CBFE	FASTA	426	47,139
	10 20 30 40 50 60 MLKEPSVRLR EAIIEGNLLI VKRLLRRNPD LLTNIDSENG WSSLHYASYH GRYLICVYLI 70 80 90 100 110 120 QLGHDKHELI KTFKGNTCVH LALMKGHEQT LHLLLQQFPR FINHRGENGR APIHIACMND 130 140 150 160 170 180 YYQCLSLLIG VGADLWVMDT NGDTPLHVCL EYGSISCMKM LLNEGEVSLD DNVRDKGNWK 190 200 210 220 230 240 PIDVAQTFEV GNIYSKVLKE VKKKGPPLGA GKKPSSFRTP ILNAKATFED GPSPVLSMNS 250 260 270 280 290 300 PYSLYSNNSP LPVLPRRIST HTTSGNGGNR RSSITNPVFN PRKPTLSTDS FSSSSNSSSR 310 320 330 340 350 360 LRVNSINVKT PVGVSPKKEL VSESVRHSAT PTSPHNNIAL INRYLLPNKS NDNVRGDSQT 370 380 390 400 410 420 ATINDDGGGG NGGDATIGMG LRKDPDDENE NKYKIKVNNG EPRRRVSLLN IPISKLRNSN NTRAED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control." Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L., Bonenfant D., Oppliger W., Jenoe P., Hall M.N. Mol. Cell 10:457-468(2002) [PubMed: 12408816] [Abstract] Cited for: IDENTIFICATION IN TORC2, MASS SPECTROMETRY.
[3]	"Tor kinases are in distinct membrane-associated protein complexes in Saccharomyces cerevisiae." Wedaman K.P., Reinke A., Anderson S., Yates J.R. III, McCaffery J.M., Powers T. Mol. Biol. Cell 14:1204-1220(2003) [PubMed: 12631735] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN TORC2, MASS SPECTROMETRY.
[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]	"The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2." Fadri M., Daquinag A., Wang S., Xue T., Kunz J. Mol. Biol. Cell 16:1883-1900(2005) [PubMed: 15689497] [Abstract] Cited for: INTERACTION WITH SLM1 AND SLM2.
[6]	"Molecular organization of target of rapamycin complex 2." Wullschleger S., Loewith R., Oppliger W., Hall M.N. J. Biol. Chem. 280:30697-30704(2005) [PubMed: 16002396] [Abstract] Cited for: SUBUNIT.
[7]	"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 SER-273; THR-330; THR-332 AND SER-350, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z48952 Genomic DNA. Translation: CAA88793.1.
PIR	S52828.
RefSeq	NP_013784.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1958N.
IntAct	Q04749. 11 interactions.
STRING	Q04749.
Proteomic databases
PRIDE	Q04749.
Genome annotation databases
Ensembl	YMR068W; YMR068W; YMR068W; Saccharomyces cerevisiae. [Genome view]
GeneID	855090.
KEGG	sce:YMR068W.
NMPDR	fig|4932.3.peg.4831.
Organism-specific databases
CYGD	YMR068w.
SGD	S000004672. AVO2.
Phylogenomic databases
HOGENOM	HBG203408.
OMA	HGRYLIC.
OrthoDB	EOG97M3FC.
Gene expression databases
ArrayExpress	Q04749.
Genevestigator	Q04749.
GermOnline	YMR068W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 1 hit.
Pfam	PF00023. Ank. 5 hits. [Graphical view]
SMART	SM00248. ANK. 4 hits. [Graphical view]
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	978393.

Entry information

Entry name

AVO2_YEAST

Accession

Primary (citable) accession number: Q04749

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	December 15, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)