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Protein

Target of rapamycin complex 2 subunit AVO1

Gene

AVO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • phosphatidylinositol-4,5-bisphosphate binding Source: SGD
  • Ras GTPase binding Source: SGD

GO - Biological processi

  • establishment or maintenance of actin cytoskeleton polarity Source: SGD
  • fungal-type cell wall organization Source: SGD
  • negative regulation of Ras protein signal transduction Source: SGD
  • regulation of cell growth Source: SGD
  • stress-activated protein kinase signaling cascade Source: GO_Central
  • TORC2 signaling Source: GO_Central
  • TOR signaling Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-33482-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Target of rapamycin complex 2 subunit AVO1
Short name:
TORC2 subunit AVO1
Alternative name(s):
Adheres voraciously to TOR2 protein 1
Gene namesi
Name:AVO1
Ordered Locus Names:YOL078W
ORF Names:O1110
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL078W.
SGDiS000005438. AVO1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • plasma membrane Source: SGD
  • TORC2 complex Source: SGD
  • vacuolar membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002187711 – 1176Target of rapamycin complex 2 subunit AVO1Add BLAST1176

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei140PhosphoserineCombined sources1
Modified residuei144PhosphoserineCombined sources1
Modified residuei400PhosphoserineCombined sources1
Modified residuei509PhosphoserineCombined sources1
Modified residuei510PhosphothreonineCombined sources1
Modified residuei552PhosphoserineCombined sources1

Post-translational modificationi

Autophosphorylated by TORC2.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ08236.
PRIDEiQ08236.

PTM databases

iPTMnetiQ08236.

Interactioni

Subunit structurei

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. AVO1 is required for TORC2 integrity by tethering AVO2 and TSC11 to the complex.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LST8P413182EBI-29284,EBI-28598
TOR2P326004EBI-29284,EBI-19385

GO - Molecular functioni

  • Ras GTPase binding Source: SGD

Protein-protein interaction databases

BioGridi34323. 35 interactors.
DIPiDIP-6357N.
IntActiQ08236. 12 interactors.
MINTiMINT-661438.

Structurei

Secondary structure

11176
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1069 – 1090Combined sources22
Beta strandi1093 – 1097Combined sources5
Beta strandi1112 – 1115Combined sources4
Helixi1116 – 1118Combined sources3
Beta strandi1119 – 1124Combined sources6
Beta strandi1131 – 1136Combined sources6
Beta strandi1145 – 1153Combined sources9
Helixi1154 – 1173Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ULBX-ray1.90A/B1056-1176[»]
3ULCX-ray2.80A1056-1176[»]
ProteinModelPortaliQ08236.
SMRiQ08236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SIN1 family.Curated

Phylogenomic databases

HOGENOMiHOG000034238.
InParanoidiQ08236.
OMAiNKHERTL.
OrthoDBiEOG092C0HRG.

Family and domain databases

InterProiIPR031567. CRIM_dom.
IPR008828. Sin1/Avo1.
IPR031313. Sin1_PH_dom.
[Graphical view]
PANTHERiPTHR13335. PTHR13335. 2 hits.
PfamiPF16978. CRIM. 1 hit.
PF16979. SIN1_PH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTVTVLNEL RAQFLRVCPE KDQMKRIIKP YIPVDEFNTE QCLDSSIREL
60 70 80 90 100
YMNSDGVSLL PELESPPVSK DFMENYASLG KMRIMRENEG QKGKANQNLI
110 120 130 140 150
GAEKTERDEE ETRNLQDKSA KNTLIVEENG TLRYNPLNSS ASNSLLNDDD
160 170 180 190 200
HTSGKHHKTS SKEDSYLNSS MEMQKKSSKR SSLPFVRIFK SRRDHSNTSG
210 220 230 240 250
NKNVMNTTNT RAKSSTLHPP GARHNKKGSK FDMNFDFDEN LEEEDDDDDD
260 270 280 290 300
DEEGDDIHSQ FFQLDDDFDA KGSGASPAHK GINGMSNNKN NTYTNNRNSI
310 320 330 340 350
SILDDRESSN GNIGSASRLK SHFPTSQKGK IFLTDNKNDG QKSDSLNANK
360 370 380 390 400
GIHGDGSSAS GNGSVSRDGL TETESNNISD MESYINEKDL DDLNFDTVTS
410 420 430 440 450
NINKTVSDLG GHESTNDGTA VMNRDSKDSR SNSNEFNAQN RDRITPGSSY
460 470 480 490 500
GKSLLGSEYS EERYSNNDSS TMESGEMSLD SDMQTNTIPS HSIPMSMQKY
510 520 530 540 550
GIYHGDDDST LNNVFDKAVL TMNSSRHPKE RRDTVISGKE PTSLTSSNRK
560 570 580 590 600
FSVSSNLTST RSPLLRGHGR TSSTASSEHM KAPKVSDSVL HRARKSTLTL
610 620 630 640 650
KQDHSQPSVP SSVHKSSKEG NILIEKTTDY LVSKPKASQL SNMFNKKKKR
660 670 680 690 700
TNTNSVDVLE YFSFVCGDKV PNYESMGLEI YIQASKKYKR NSFTTKVRKS
710 720 730 740 750
STIFEVIGFA LFLYSTEKKP DNFEEDGLTV EDISNPNNFS LKIVDEDGEP
760 770 780 790 800
FEDNFGKLDR KSTIQSISDS EVVLCKVDDA EKSQNEIETP LPFETGGGLM
810 820 830 840 850
DASTLDANSS HDTTDGTINQ LSFYKPIIGN EDDIDKTNGS KIIDVTVYLY
860 870 880 890 900
PNVNPKFNYT TISVLVTSHI NDILVKYCKM KNMDPNEYAL KVLGKNYILD
910 920 930 940 950
LNDTVLRLDG INKVELISKK DARELHLEKM KPDLKKPVLP TIQSNDLTPL
960 970 980 990 1000
TLEPLNSYLK ADAGGAVAAI PENTKVTSKA KKISTKYKLG LAKQHSSSSV
1010 1020 1030 1040 1050
ASGSVSTAGG LANGNGFFKN KNSSKSSLHG TLQFHNINRS QSTMEHTPDT
1060 1070 1080 1090 1100
PNGVGDNFQD LFTGAYHKYK VWRRQQMSFI NKHERTLAID GDYIYIVPPE
1110 1120 1130 1140 1150
GRIHWHDNVK TKSLHISQVV LVKKSKRVPE HFKIFVRREG QDDIKRYYFE
1160 1170
AVSGQECTEI VTRLQNLLSA YRMNHK
Length:1,176
Mass (Da):131,379
Last modified:November 1, 1996 - v1
Checksum:iED2B30D014EE5652
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74820 Genomic DNA. Translation: CAA99089.1.
Z74819 Genomic DNA. Translation: CAA99088.1.
BK006948 Genomic DNA. Translation: DAA10705.1.
PIRiS66771.
RefSeqiNP_014563.1. NM_001183332.1.

Genome annotation databases

EnsemblFungiiYOL078W; YOL078W; YOL078W.
GeneIDi854076.
KEGGisce:YOL078W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74820 Genomic DNA. Translation: CAA99089.1.
Z74819 Genomic DNA. Translation: CAA99088.1.
BK006948 Genomic DNA. Translation: DAA10705.1.
PIRiS66771.
RefSeqiNP_014563.1. NM_001183332.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ULBX-ray1.90A/B1056-1176[»]
3ULCX-ray2.80A1056-1176[»]
ProteinModelPortaliQ08236.
SMRiQ08236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34323. 35 interactors.
DIPiDIP-6357N.
IntActiQ08236. 12 interactors.
MINTiMINT-661438.

PTM databases

iPTMnetiQ08236.

Proteomic databases

MaxQBiQ08236.
PRIDEiQ08236.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL078W; YOL078W; YOL078W.
GeneIDi854076.
KEGGisce:YOL078W.

Organism-specific databases

EuPathDBiFungiDB:YOL078W.
SGDiS000005438. AVO1.

Phylogenomic databases

HOGENOMiHOG000034238.
InParanoidiQ08236.
OMAiNKHERTL.
OrthoDBiEOG092C0HRG.

Enzyme and pathway databases

BioCyciYEAST:G3O-33482-MONOMER.

Miscellaneous databases

PROiQ08236.

Family and domain databases

InterProiIPR031567. CRIM_dom.
IPR008828. Sin1/Avo1.
IPR031313. Sin1_PH_dom.
[Graphical view]
PANTHERiPTHR13335. PTHR13335. 2 hits.
PfamiPF16978. CRIM. 1 hit.
PF16979. SIN1_PH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAVO1_YEAST
AccessioniPrimary (citable) accession number: Q08236
Secondary accession number(s): D6W1Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 704 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.