AVO2_YEAST
ID AVO2_YEAST Reviewed; 426 AA.
AC Q04749; D6VZP2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Target of rapamycin complex 2 subunit AVO2;
DE Short=TORC2 subunit AVO2;
DE AltName: Full=Adheres voraciously to TOR2 protein 2;
GN Name=AVO2; OrderedLocusNames=YMR068W; ORFNames=YM9916.07;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 IDENTIFICATION IN TORC2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12408816; DOI=10.1016/s1097-2765(02)00636-6;
RA Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L.,
RA Bonenfant D., Oppliger W., Jenoe P., Hall M.N.;
RT "Two TOR complexes, only one of which is rapamycin sensitive, have distinct
RT roles in cell growth control.";
RL Mol. Cell 10:457-468(2002).
RN [4]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN TORC2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12631735; DOI=10.1091/mbc.e02-09-0609;
RA Wedaman K.P., Reinke A., Anderson S., Yates J.R. III, McCaffery J.M.,
RA Powers T.;
RT "Tor kinases are in distinct membrane-associated protein complexes in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:1204-1220(2003).
RN [5]
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 [6]
RP INTERACTION WITH SLM1 AND SLM2.
RX PubMed=15689497; DOI=10.1091/mbc.e04-07-0564;
RA Fadri M., Daquinag A., Wang S., Xue T., Kunz J.;
RT "The pleckstrin homology domain proteins Slm1 and Slm2 are required for
RT actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-
RT bisphosphate and TORC2.";
RL Mol. Biol. Cell 16:1883-1900(2005).
RN [7]
RP SUBUNIT.
RX PubMed=16002396; DOI=10.1074/jbc.m505553200;
RA Wullschleger S., Loewith R., Oppliger W., Hall M.N.;
RT "Molecular organization of target of rapamycin complex 2.";
RL J. Biol. Chem. 280:30697-30704(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of TORC2, which regulates cell cycle-dependent
CC polarization of the actin-cytoskeleton and cell wall integrity. TORC2
CC controls polarity of the actin cytoskeleton, which is required for
CC orienting the secretory pathway toward discrete growth sites, via the
CC RHO1/PKC1/MAPK cell integrity pathway.
CC -!- SUBUNIT: The target of rapamycin complex 2 (TORC2) is composed of at
CC least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a
CC homodimer. Contrary to TORC1, TORC2 does not bind to and is not
CC sensitive to FKBP-rapamycin. AVO2 is peripherally associated to AVO1
CC and TSC11. {ECO:0000269|PubMed:12408816, ECO:0000269|PubMed:12631735,
CC ECO:0000269|PubMed:16002396}.
CC -!- INTERACTION:
CC Q04749; P41318: LST8; NbExp=2; IntAct=EBI-28131, EBI-28598;
CC Q04749; P32600: TOR2; NbExp=4; IntAct=EBI-28131, EBI-19385;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12631735};
CC Peripheral membrane protein {ECO:0000269|PubMed:12631735}; Cytoplasmic
CC side {ECO:0000269|PubMed:12631735}. Vacuole membrane
CC {ECO:0000269|PubMed:12631735}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12631735}; Cytoplasmic side
CC {ECO:0000269|PubMed:12631735}.
CC -!- MISCELLANEOUS: Present with 1180 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z48952; CAA88793.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09966.1; -; Genomic_DNA.
DR PIR; S52828; S52828.
DR RefSeq; NP_013784.1; NM_001182566.1.
DR PDB; 6EMK; EM; 8.00 A; G/H=1-426.
DR PDBsum; 6EMK; -.
DR AlphaFoldDB; Q04749; -.
DR SMR; Q04749; -.
DR BioGRID; 35243; 89.
DR ComplexPortal; CPX-1717; TORC2 complex.
DR DIP; DIP-1958N; -.
DR IntAct; Q04749; 8.
DR MINT; Q04749; -.
DR STRING; 4932.YMR068W; -.
DR iPTMnet; Q04749; -.
DR PaxDb; Q04749; -.
DR PRIDE; Q04749; -.
DR EnsemblFungi; YMR068W_mRNA; YMR068W; YMR068W.
DR GeneID; 855090; -.
DR KEGG; sce:YMR068W; -.
DR SGD; S000004672; AVO2.
DR VEuPathDB; FungiDB:YMR068W; -.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_036011_0_0_1; -.
DR InParanoid; Q04749; -.
DR OMA; HIACMND; -.
DR BioCyc; YEAST:G3O-32770-MON; -.
DR PRO; PR:Q04749; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04749; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031932; C:TORC2 complex; IPI:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IPI:SGD.
DR GO; GO:0001558; P:regulation of cell growth; IPI:SGD.
DR GO; GO:0031929; P:TOR signaling; IC:SGD.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF13637; Ank_4; 2.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Vacuole.
FT CHAIN 1..426
FT /note="Target of rapamycin complex 2 subunit AVO2"
FT /id="PRO_0000067247"
FT REPEAT 4..33
FT /note="ANK 1"
FT REPEAT 39..68
FT /note="ANK 2"
FT REPEAT 74..104
FT /note="ANK 3"
FT REPEAT 108..137
FT /note="ANK 4"
FT REPEAT 141..171
FT /note="ANK 5"
FT REGION 259..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 426 AA; 47139 MW; 0A17E78BF449CBFE CRC64;
MLKEPSVRLR EAIIEGNLLI VKRLLRRNPD LLTNIDSENG WSSLHYASYH GRYLICVYLI
QLGHDKHELI KTFKGNTCVH LALMKGHEQT LHLLLQQFPR FINHRGENGR APIHIACMND
YYQCLSLLIG VGADLWVMDT NGDTPLHVCL EYGSISCMKM LLNEGEVSLD DNVRDKGNWK
PIDVAQTFEV GNIYSKVLKE VKKKGPPLGA GKKPSSFRTP ILNAKATFED GPSPVLSMNS
PYSLYSNNSP LPVLPRRIST HTTSGNGGNR RSSITNPVFN PRKPTLSTDS FSSSSNSSSR
LRVNSINVKT PVGVSPKKEL VSESVRHSAT PTSPHNNIAL INRYLLPNKS NDNVRGDSQT
ATINDDGGGG NGGDATIGMG LRKDPDDENE NKYKIKVNNG EPRRRVSLLN IPISKLRNSN
NTRAED
