AVO1_YEAST
ID AVO1_YEAST Reviewed; 1176 AA.
AC Q08236; D6W1Y9;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Target of rapamycin complex 2 subunit AVO1;
DE Short=TORC2 subunit AVO1;
DE AltName: Full=Adheres voraciously to TOR2 protein 1;
GN Name=AVO1; OrderedLocusNames=YOL078W; ORFNames=O1110;
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 [GENOMIC DNA].
RX PubMed=9178509;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<583::aid-yea111>3.0.co;2-y;
RA Tzermia M., Katsoulou C., Alexandraki D.;
RT "Sequence analysis of a 33.2 kb segment from the left arm of yeast
RT chromosome XV reveals eight known genes and ten new open reading frames
RT including homologues of ABC transporters, inositol phosphatases and human
RT expressed sequence tags.";
RL Yeast 13:583-589(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP SUBUNIT, AND PHOSPHORYLATION.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-144 AND SER-552, AND
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 IDENTIFICATION BY 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-400; SER-509 AND THR-510, AND
RP IDENTIFICATION BY 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).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. AVO1 is required for TORC2 integrity by
CC tethering AVO2 and TSC11 to the complex. {ECO:0000269|PubMed:12408816,
CC ECO:0000269|PubMed:12631735, ECO:0000269|PubMed:16002396}.
CC -!- INTERACTION:
CC Q08236; P41318: LST8; NbExp=2; IntAct=EBI-29284, EBI-28598;
CC Q08236; P32600: TOR2; NbExp=4; IntAct=EBI-29284, 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 -!- PTM: Autophosphorylated by TORC2. {ECO:0000269|PubMed:16002396}.
CC -!- MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SIN1 family. {ECO:0000305}.
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DR EMBL; Z74820; CAA99089.1; -; Genomic_DNA.
DR EMBL; Z74819; CAA99088.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10705.1; -; Genomic_DNA.
DR PIR; S66771; S66771.
DR RefSeq; NP_014563.1; NM_001183332.1.
DR PDB; 3ULB; X-ray; 1.90 A; A/B=1056-1176.
DR PDB; 3ULC; X-ray; 2.80 A; A=1056-1176.
DR PDB; 6EMK; EM; 8.00 A; I/J=1-1176.
DR PDBsum; 3ULB; -.
DR PDBsum; 3ULC; -.
DR PDBsum; 6EMK; -.
DR AlphaFoldDB; Q08236; -.
DR SMR; Q08236; -.
DR BioGRID; 34323; 435.
DR ComplexPortal; CPX-1717; TORC2 complex.
DR DIP; DIP-6357N; -.
DR IntAct; Q08236; 16.
DR MINT; Q08236; -.
DR STRING; 4932.YOL078W; -.
DR CarbonylDB; Q08236; -.
DR iPTMnet; Q08236; -.
DR MaxQB; Q08236; -.
DR PaxDb; Q08236; -.
DR PRIDE; Q08236; -.
DR EnsemblFungi; YOL078W_mRNA; YOL078W; YOL078W.
DR GeneID; 854076; -.
DR KEGG; sce:YOL078W; -.
DR SGD; S000005438; AVO1.
DR VEuPathDB; FungiDB:YOL078W; -.
DR eggNOG; KOG3739; Eukaryota.
DR GeneTree; ENSGT00390000000642; -.
DR HOGENOM; CLU_008055_0_0_1; -.
DR InParanoid; Q08236; -.
DR OMA; HWHENVK; -.
DR BioCyc; YEAST:G3O-33482-MON; -.
DR Reactome; R-SCE-1257604; PIP3 activates AKT signaling.
DR Reactome; R-SCE-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR PRO; PR:Q08236; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08236; protein.
DR GO; GO:0005737; C:cytoplasm; IPI:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0031932; C:TORC2 complex; IPI:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISS:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:SGD.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:SGD.
DR GO; GO:0001558; P:regulation of cell growth; IPI:SGD.
DR GO; GO:0031929; P:TOR signaling; IC:SGD.
DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR031567; CRIM_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR008828; Sin1/Avo1.
DR InterPro; IPR031313; Sin1_PH_dom.
DR PANTHER; PTHR13335; PTHR13335; 1.
DR Pfam; PF16978; CRIM; 1.
DR Pfam; PF16979; SIN1_PH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Vacuole.
FT CHAIN 1..1176
FT /note="Target of rapamycin complex 2 subunit AVO1"
FT /id="PRO_0000218771"
FT REGION 87..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 510
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT STRAND 1069..1090
FT /evidence="ECO:0007829|PDB:3ULB"
FT STRAND 1093..1097
FT /evidence="ECO:0007829|PDB:3ULB"
FT STRAND 1112..1115
FT /evidence="ECO:0007829|PDB:3ULB"
FT HELIX 1116..1118
FT /evidence="ECO:0007829|PDB:3ULB"
FT STRAND 1119..1124
FT /evidence="ECO:0007829|PDB:3ULB"
FT STRAND 1131..1136
FT /evidence="ECO:0007829|PDB:3ULB"
FT STRAND 1145..1153
FT /evidence="ECO:0007829|PDB:3ULB"
FT HELIX 1154..1173
FT /evidence="ECO:0007829|PDB:3ULB"
SQ SEQUENCE 1176 AA; 131379 MW; ED2B30D014EE5652 CRC64;
MDTVTVLNEL RAQFLRVCPE KDQMKRIIKP YIPVDEFNTE QCLDSSIREL YMNSDGVSLL
PELESPPVSK DFMENYASLG KMRIMRENEG QKGKANQNLI GAEKTERDEE ETRNLQDKSA
KNTLIVEENG TLRYNPLNSS ASNSLLNDDD HTSGKHHKTS SKEDSYLNSS MEMQKKSSKR
SSLPFVRIFK SRRDHSNTSG NKNVMNTTNT RAKSSTLHPP GARHNKKGSK FDMNFDFDEN
LEEEDDDDDD DEEGDDIHSQ FFQLDDDFDA KGSGASPAHK GINGMSNNKN NTYTNNRNSI
SILDDRESSN GNIGSASRLK SHFPTSQKGK IFLTDNKNDG QKSDSLNANK GIHGDGSSAS
GNGSVSRDGL TETESNNISD MESYINEKDL DDLNFDTVTS NINKTVSDLG GHESTNDGTA
VMNRDSKDSR SNSNEFNAQN RDRITPGSSY GKSLLGSEYS EERYSNNDSS TMESGEMSLD
SDMQTNTIPS HSIPMSMQKY GIYHGDDDST LNNVFDKAVL TMNSSRHPKE RRDTVISGKE
PTSLTSSNRK FSVSSNLTST RSPLLRGHGR TSSTASSEHM KAPKVSDSVL HRARKSTLTL
KQDHSQPSVP SSVHKSSKEG NILIEKTTDY LVSKPKASQL SNMFNKKKKR TNTNSVDVLE
YFSFVCGDKV PNYESMGLEI YIQASKKYKR NSFTTKVRKS STIFEVIGFA LFLYSTEKKP
DNFEEDGLTV EDISNPNNFS LKIVDEDGEP FEDNFGKLDR KSTIQSISDS EVVLCKVDDA
EKSQNEIETP LPFETGGGLM DASTLDANSS HDTTDGTINQ LSFYKPIIGN EDDIDKTNGS
KIIDVTVYLY PNVNPKFNYT TISVLVTSHI NDILVKYCKM KNMDPNEYAL KVLGKNYILD
LNDTVLRLDG INKVELISKK DARELHLEKM KPDLKKPVLP TIQSNDLTPL TLEPLNSYLK
ADAGGAVAAI PENTKVTSKA KKISTKYKLG LAKQHSSSSV ASGSVSTAGG LANGNGFFKN
KNSSKSSLHG TLQFHNINRS QSTMEHTPDT PNGVGDNFQD LFTGAYHKYK VWRRQQMSFI
NKHERTLAID GDYIYIVPPE GRIHWHDNVK TKSLHISQVV LVKKSKRVPE HFKIFVRREG
QDDIKRYYFE AVSGQECTEI VTRLQNLLSA YRMNHK
