CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005986
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 V-type proton ATPase subunit C 
Protein Synonyms/Alias
 V-ATPase subunit C; V-ATPase 42 kDa subunit; Vacuolar proton pump subunit C 
Gene Name
 VMA5 
Gene Synonyms/Alias
 VAT3; VATC; YKL080W; YKL410 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
49RAFVSDFKIPEFKIGacetylation[1]
203VAVPKSLKSDFEKSYacetylation[1]
208SLKSDFEKSYETLSKubiquitination[2]
241FNVHLFKKNVQEFTTacetylation[1]
271EELIDQLKKEHDSAAacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic activity of the catalytic sector. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding; Reference proteome; Transport; Vacuole. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 392 AA 
Protein Sequence
MATALYTAND FILISLPQNA QPVTAPGSKT DSWFNETLIG GRAFVSDFKI PEFKIGSLDT 60
LIVESEELSK VDNQIGASIG KIIEILQGLN ETSTNAYRTL PINNMPVPEY LENFQWQTRK 120
FKLDKSIKDL ITLISNESSQ LDADVRATYA NYNSAKTNLA AAERKKTGDL SVRSLHDIVK 180
PEDFVLNSEH LTTVLVAVPK SLKSDFEKSY ETLSKNVVPA SASVIAEDAE YVLFNVHLFK 240
KNVQEFTTAA REKKFIPREF NYSEELIDQL KKEHDSAASL EQSLRVQLVR LAKTAYVDVF 300
INWFHIKALR VYVESVLRYG LPPHFNIKII AVPPKNLSKC KSELIDAFGF LGGNAFMKDK 360
KGKINKQDTS LHQYASLVDT EYEPFVMYII NL 392 
Gene Ontology
 GO:0000329; C:fungal-type vacuole membrane; TAS:SGD.
 GO:0016021; C:integral to membrane; ISM:SGD.
 GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; TAS:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; TAS:SGD.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0007035; P:vacuolar acidification; TAS:SGD. 
Interpro
 IPR004907; ATPase_V1-cplx_csu. 
Pfam
 PF03223; V-ATPase_C 
SMART
  
PROSITE
  
PRINTS