Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

V-type proton ATPase catalytic subunit A

Gene

VMA1

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

Functioni

Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca2+ homeostasis. This is a catalytic subunit.1 Publication
PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it.1 Publication

Miscellaneous

Present with 199895 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).PROSITE-ProRule annotation

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi257 – 264ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

  • ATP metabolic process Source: InterPro
  • cellular protein metabolic process Source: SGD
  • intein-mediated protein splicing Source: InterPro
  • intron homing Source: UniProtKB-KW
  • vacuolar acidification Source: SGD

Keywordsi

Molecular functionDNA-binding, Endonuclease, Hydrolase, Nuclease
Biological processHydrogen ion transport, Intron homing, Ion transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29571-MONOMER
ReactomeiR-SCE-1222556 ROS, RNS production in phagocytes
R-SCE-77387 Insulin receptor recycling
R-SCE-917977 Transferrin endocytosis and recycling

Protein family/group databases

MEROPSiN09.001
REBASEi2615 PI-SceI
TCDBi3.A.2.2.3 the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase catalytic subunit A (EC:3.6.3.14)
Short name:
V-ATPase subunit A
Alternative name(s):
Vacuolar proton pump subunit A
Cleaved into the following chain:
Alternative name(s):
Sce VMA intein
VMA1-derived endonuclease
Short name:
VDE
Gene namesi
Name:VMA1
Synonyms:CLS8, TFP1
Ordered Locus Names:YDL185W
ORF Names:D1286
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL185W
SGDiS000002344 VMA1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi284C → S: Reduces splicing reaction speed. Inhibits splicing; when associated with N-362; S-737 and S-738 in X10SSS VDE. 3 Publications1
Mutagenesisi362H → N: Inhibits splicing; when associated with S-284; S-737 and S-738 in X10SSS VDE. 1 Publication1
Mutagenesisi737N → S: Inhibits splicing; when associated with S-284; N-362 and S-738 in X10SSS VDE. 2 Publications1
Mutagenesisi738C → S: Reduces splicing reaction speed. Inhibits splicing; when associated with S-284; N-362 and S-737 in X10SSS VDE. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00000024582 – 283V-type proton ATPase catalytic subunit A, 1st partAdd BLAST282
ChainiPRO_0000002459284 – 737Endonuclease PI-SceIAdd BLAST454
ChainiPRO_0000002460738 – 1071V-type proton ATPase catalytic subunit A, 2nd partAdd BLAST334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei131PhosphothreonineCombined sources1
Modified residuei858PhosphoserineCombined sources1
Modified residuei928PhosphoserineCombined sources1

Post-translational modificationi

This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.

Keywords - PTMi

Acetylation, Autocatalytic cleavage, Phosphoprotein, Protein splicing

Proteomic databases

MaxQBiP17255
PaxDbiP17255
PRIDEiP17255

2D gel databases

UCD-2DPAGEiP17255

PTM databases

iPTMnetiP17255

Miscellaneous databases

PMAP-CutDBiP17255

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi31859, 480 interactors
ComplexPortaliCPX-1192 Vacuolar proton translocating ATPase complex, Golgi variant
CPX-1193 Vacuolar proton translocating ATPase complex, vacuole variant
DIPiDIP-2293N
IntActiP17255, 117 interactors
MINTiP17255
STRINGi4932.YDL185W

Structurei

Secondary structure

11071
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi283 – 285Combined sources3
Beta strandi290 – 293Combined sources4
Beta strandi298 – 300Combined sources3
Helixi301 – 303Combined sources3
Beta strandi309 – 312Combined sources4
Beta strandi315 – 322Combined sources8
Beta strandi325 – 335Combined sources11
Beta strandi343 – 345Combined sources3
Beta strandi347 – 349Combined sources3
Beta strandi355 – 359Combined sources5
Beta strandi363 – 369Combined sources7
Beta strandi372 – 379Combined sources8
Beta strandi382 – 396Combined sources15
Beta strandi398 – 400Combined sources3
Beta strandi402 – 414Combined sources13
Helixi415 – 417Combined sources3
Helixi420 – 431Combined sources12
Beta strandi434 – 443Combined sources10
Helixi444 – 449Combined sources6
Helixi452 – 457Combined sources6
Beta strandi459 – 462Combined sources4
Turni471 – 474Combined sources4
Beta strandi479 – 481Combined sources3
Beta strandi485 – 487Combined sources3
Helixi488 – 501Combined sources14
Beta strandi506 – 514Combined sources9
Helixi516 – 528Combined sources13
Beta strandi531 – 533Combined sources3
Beta strandi534 – 537Combined sources4
Beta strandi538 – 540Combined sources3
Turni541 – 543Combined sources3
Beta strandi544 – 548Combined sources5
Turni556 – 559Combined sources4
Helixi570 – 575Combined sources6
Beta strandi579 – 584Combined sources6
Helixi588 – 591Combined sources4
Helixi595 – 609Combined sources15
Beta strandi610 – 613Combined sources4
Beta strandi619 – 625Combined sources7
Helixi627 – 639Combined sources13
Beta strandi643 – 650Combined sources8
Helixi654 – 656Combined sources3
Beta strandi657 – 659Combined sources3
Beta strandi661 – 669Combined sources9
Helixi672 – 678Combined sources7
Turni684 – 686Combined sources3
Beta strandi692 – 694Combined sources3
Beta strandi700 – 702Combined sources3
Beta strandi704 – 714Combined sources11
Beta strandi721 – 723Combined sources3
Beta strandi725 – 729Combined sources5
Beta strandi733 – 736Combined sources4

3D structure databases

ProteinModelPortaliP17255
SMRiP17255
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17255

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini494 – 642DOD-type homing endonucleasePROSITE-ProRule annotationAdd BLAST149

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074787
HOGENOMiHOG000141780
InParanoidiP17255
KOiK02145
OMAiHNTVTQH
OrthoDBiEOG092C12O0

Family and domain databases

Gene3Di1.10.1140.10, 1 hit
2.40.30.20, 1 hit
3.10.28.10, 2 hits
InterProiView protein in InterPro
IPR031686 ATP-synth_a_Xtn
IPR023366 ATP_synth_asu-like_sf
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR024034 ATPase_F1/V1_b/a_C
IPR003586 Hint_dom_C
IPR003587 Hint_dom_N
IPR036844 Hint_dom_sf
IPR007868 Hom_end_hint
IPR007869 Homing_endonuc_PI-Sce
IPR027434 Homing_endonucl
IPR006142 INTEIN
IPR030934 Intein_C
IPR004042 Intein_endonuc
IPR006141 Intein_N
IPR027417 P-loop_NTPase
IPR022878 V-ATPase_asu
PANTHERiPTHR43607 PTHR43607, 1 hit
PfamiView protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
PF16886 ATP-synt_ab_Xtn, 1 hit
PF05204 Hom_end, 2 hits
PF05203 Hom_end_hint, 1 hit
PRINTSiPR00379 INTEIN
SMARTiView protein in SMART
SM00305 HintC, 1 hit
SM00306 HintN, 1 hit
SUPFAMiSSF50615 SSF50615, 1 hit
SSF51294 SSF51294, 2 hits
SSF52540 SSF52540, 2 hits
SSF55608 SSF55608, 2 hits
PROSITEiView protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 1 hit
PS50818 INTEIN_C_TER, 1 hit
PS50819 INTEIN_ENDONUCLEASE, 1 hit
PS50817 INTEIN_N_TER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17255-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAIENARK EIKRISLEDH AESEYGAIYS VSGPVVIAEN MIGCAMYELV
60 70 80 90 100
KVGHDNLVGE VIRIDGDKAT IQVYEETAGL TVGDPVLRTG KPLSVELGPG
110 120 130 140 150
LMETIYDGIQ RPLKAIKEES QSIYIPRGID TPALDRTIKW QFTPGKFQVG
160 170 180 190 200
DHISGGDIYG SVFENSLISS HKILLPPRSR GTITWIAPAG EYTLDEKILE
210 220 230 240 250
VEFDGKKSDF TLYHTWPVRV PRPVTEKLSA DYPLLTGQRV LDALFPCVQG
260 270 280 290 300
GTTCIPGAFG CGKTVISQSL SKYSNSDAII YVGCFAKGTN VLMADGSIEC
310 320 330 340 350
IENIEVGNKV MGKDGRPREV IKLPRGRETM YSVVQKSQHR AHKSDSSREV
360 370 380 390 400
PELLKFTCNA THELVVRTPR SVRRLSRTIK GVEYFEVITF EMGQKKAPDG
410 420 430 440 450
RIVELVKEVS KSYPISEGPE RANELVESYR KASNKAYFEW TIEARDLSLL
460 470 480 490 500
GSHVRKATYQ TYAPILYEND HFFDYMQKSK FHLTIEGPKV LAYLLGLWIG
510 520 530 540 550
DGLSDRATFS VDSRDTSLME RVTEYAEKLN LCAEYKDRKE PQVAKTVNLY
560 570 580 590 600
SKVVRGNGIR NNLNTENPLW DAIVGLGFLK DGVKNIPSFL STDNIGTRET
610 620 630 640 650
FLAGLIDSDG YVTDEHGIKA TIKTIHTSVR DGLVSLARSL GLVVSVNAEP
660 670 680 690 700
AKVDMNGTKH KISYAIYMSG GDVLLNVLSK CAGSKKFRPA PAAAFARECR
710 720 730 740 750
GFYFELQELK EDDYYGITLS DDSDHQFLLA NQVVVHNCGE RGNEMAEVLM
760 770 780 790 800
EFPELYTEMS GTKEPIMKRT TLVANTSNMP VAAREASIYT GITLAEYFRD
810 820 830 840 850
QGKNVSMIAD SSSRWAEALR EISGRLGEMP ADQGFPAYLG AKLASFYERA
860 870 880 890 900
GKAVALGSPD RTGSVSIVAA VSPAGGDFSD PVTTATLGIT QVFWGLDKKL
910 920 930 940 950
AQRKHFPSIN TSVSYSKYTN VLNKFYDSNY PEFPVLRDRM KEILSNAEEL
960 970 980 990 1000
EQVVQLVGKS ALSDSDKITL DVATLIKEDF LQQNGYSTYD AFCPIWKTFD
1010 1020 1030 1040 1050
MMRAFISYHD EAQKAVANGA NWSKLADSTG DVKHAVSSSK FFEPSRGEKE
1060 1070
VHGEFEKLLS TMQERFAEST D
Length:1,071
Mass (Da):118,637
Last modified:January 23, 2007 - v3
Checksum:i2A4C65D2F59426FD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti875G → D in AAB63978 (PubMed:2905423).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05409 Genomic DNA Translation: AAA34664.1
X83276 Genomic DNA Translation: CAA58261.1
Z74233 Genomic DNA Translation: CAA98760.1
Z74233 Genomic DNA Translation: CAA98761.1 Sequence problems.
Z74233 Genomic DNA Translation: CAA98762.1
X58857 Genomic DNA Translation: CAA41657.1
M21609 Genomic DNA Translation: AAB63978.1
BK006938 Genomic DNA Translation: DAA11677.1
PIRiA35746 PXBYVA
RefSeqiNP_010096.1, NM_001180245.1

Genome annotation databases

EnsemblFungiiYDL185W; YDL185W; YDL185W
GeneIDi851342
KEGGisce:YDL185W

Similar proteinsi

Entry informationi

Entry nameiVATA_YEAST
AccessioniPrimary (citable) accession number: P17255
Secondary accession number(s): D6VRG7, O74301, Q9Y7W5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 225 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health