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P17255

- VATA_YEAST

UniProt

P17255 - VATA_YEAST

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Protein

V-type proton ATPase catalytic subunit A

Gene

VMA1

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

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi257 – 2648ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. endodeoxyribonuclease activity Source: SGD
  4. proton-transporting ATPase activity, rotational mechanism Source: SGD

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. cellular protein metabolic process Source: SGD
  3. DNA catabolic process, endonucleolytic Source: GOC
  4. intein-mediated protein splicing Source: InterPro
  5. intron homing Source: SGD
  6. vacuolar acidification Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Hydrogen ion transport, Intron homing, Ion transport, Transport

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29571-MONOMER.
ReactomeiREACT_189031. Phagosomal maturation (early endosomal stage).
REACT_189190. 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
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

SGDiS000002344. VMA1.

Subcellular locationi

Endomembrane system 1 Publication. Vacuole membrane 1 Publication
Note: Membranes of various intracellular acidic compartments.

GO - Cellular componenti

  1. fungal-type vacuole membrane Source: UniProtKB
  2. vacuolar proton-transporting V-type ATPase, V1 domain Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi284 – 2841C → S: Reduces splicing reaction speed. Inhibits splicing; when associated with N-362; S-737 and S-738 in X10SSS VDE. 3 Publications
Mutagenesisi362 – 3621H → N: Inhibits splicing; when associated with S-284; S-737 and S-738 in X10SSS VDE. 1 Publication
Mutagenesisi737 – 7371N → S: Inhibits splicing; when associated with S-284; N-362 and S-738 in X10SSS VDE. 2 Publications
Mutagenesisi738 – 7381C → S: Reduces splicing reaction speed. Inhibits splicing; when associated with S-284; N-362 and S-737 in X10SSS VDE. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 283282V-type proton ATPase catalytic subunit A, 1st partPRO_0000002458Add
BLAST
Chaini284 – 737454Endonuclease PI-SceIPRO_0000002459Add
BLAST
Chaini738 – 1071334V-type proton ATPase catalytic subunit A, 2nd partPRO_0000002460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei131 – 1311Phosphothreonine1 Publication
Modified residuei858 – 8581Phosphoserine1 Publication
Modified residuei928 – 9281Phosphoserine1 Publication

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.
PeptideAtlasiP17255.
PRIDEiP17255.

2D gel databases

UCD-2DPAGEP17255.

Miscellaneous databases

PMAP-CutDBP17255.

Expressioni

Gene expression databases

GenevestigatoriP17255.

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

WithEntry#Exp.IntActNotes
RAV1P471042EBI-20245,EBI-25471
VMA6P323662EBI-20245,EBI-20201

Protein-protein interaction databases

BioGridi31859. 373 interactions.
DIPiDIP-2293N.
IntActiP17255. 71 interactions.
MINTiMINT-641889.

Structurei

Secondary structure

1
1071
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi290 – 2934
Beta strandi298 – 3003
Helixi301 – 3033
Beta strandi309 – 3124
Beta strandi315 – 3228
Beta strandi325 – 33511
Beta strandi343 – 3453
Beta strandi347 – 3493
Beta strandi355 – 3595
Beta strandi363 – 3697
Beta strandi372 – 3798
Beta strandi382 – 39615
Beta strandi398 – 4003
Beta strandi402 – 41413
Helixi415 – 4173
Helixi420 – 43112
Beta strandi434 – 44310
Helixi444 – 4496
Helixi452 – 4576
Beta strandi459 – 4624
Turni471 – 4744
Beta strandi479 – 4813
Beta strandi485 – 4873
Helixi488 – 50114
Beta strandi506 – 5149
Helixi516 – 52813
Beta strandi531 – 5333
Beta strandi534 – 5374
Beta strandi538 – 5403
Turni541 – 5433
Beta strandi544 – 5485
Turni556 – 5594
Helixi570 – 5756
Beta strandi579 – 5846
Helixi588 – 5914
Helixi595 – 60915
Beta strandi610 – 6134
Beta strandi619 – 6257
Helixi627 – 63913
Beta strandi643 – 6508
Helixi654 – 6563
Beta strandi657 – 6593
Beta strandi661 – 6699
Helixi672 – 6787
Turni684 – 6863
Helixi693 – 6953
Beta strandi700 – 7023
Beta strandi704 – 71916
Beta strandi721 – 7233
Beta strandi727 – 7293
Beta strandi733 – 7353

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DFAX-ray2.00A284-737[»]
1EF0X-ray2.10A/B283-741[»]
1GPPX-ray1.35A284-736[»]
1JVAX-ray2.10A/B274-747[»]
1LWSX-ray3.50A284-737[»]
1LWTX-ray3.20A284-737[»]
1UM2X-ray2.90A/B284-737[»]
C/D274-747[»]
1VDEX-ray2.40A/B284-737[»]
ProteinModelPortaliP17255.
SMRiP17255. Positions 46-1063.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17255.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini494 – 642149DOD-type homing endonucleasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated
Contains 1 DOD-type homing endonuclease domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1372.
GeneTreeiENSGT00550000074787.
HOGENOMiHOG000141780.
InParanoidiP17255.
KOiK02145.
OMAiVHNCGER.
OrthoDBiEOG7M98QZ.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
2.170.16.10. 1 hit.
3.10.28.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR028992. Hedgehog/Intein_dom.
IPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR007868. Hom_end_hint.
IPR007869. Homing_endonuc_PI-Sce.
IPR027434. Homing_endonucl.
IPR006142. INTEIN.
IPR004042. Intein_endonuc.
IPR006141. Intein_splice_site.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
PF05204. Hom_end. 2 hits.
PF05203. Hom_end_hint. 1 hit.
[Graphical view]
PRINTSiPR00379. INTEIN.
SMARTiSM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF51294. SSF51294. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF55608. SSF55608. 2 hits.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
PS50818. INTEIN_C_TER. 1 hit.
PS50819. INTEIN_ENDONUCLEASE. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti875 – 8751G → D in AAB63978. (PubMed:2905423)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Web resourcesi

Description of Sce VMA in Inbase

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A35746. PXBYVA.
RefSeqi NP_010096.1. NM_001180245.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DFA X-ray 2.00 A 284-737 [» ]
1EF0 X-ray 2.10 A/B 283-741 [» ]
1GPP X-ray 1.35 A 284-736 [» ]
1JVA X-ray 2.10 A/B 274-747 [» ]
1LWS X-ray 3.50 A 284-737 [» ]
1LWT X-ray 3.20 A 284-737 [» ]
1UM2 X-ray 2.90 A/B 284-737 [» ]
C/D 274-747 [» ]
1VDE X-ray 2.40 A/B 284-737 [» ]
ProteinModelPortali P17255.
SMRi P17255. Positions 46-1063.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31859. 373 interactions.
DIPi DIP-2293N.
IntActi P17255. 71 interactions.
MINTi MINT-641889.

Protein family/group databases

MEROPSi N09.001.
REBASEi 2615. PI-SceI.
TCDBi 3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

UCD-2DPAGE P17255.

Proteomic databases

MaxQBi P17255.
PaxDbi P17255.
PeptideAtlasi P17255.
PRIDEi P17255.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL185W ; YDL185W ; YDL185W .
GeneIDi 851342.
KEGGi sce:YDL185W.

Organism-specific databases

SGDi S000002344. VMA1.

Phylogenomic databases

eggNOGi COG1372.
GeneTreei ENSGT00550000074787.
HOGENOMi HOG000141780.
InParanoidi P17255.
KOi K02145.
OMAi VHNCGER.
OrthoDBi EOG7M98QZ.

Enzyme and pathway databases

BioCyci YEAST:G3O-29571-MONOMER.
Reactomei REACT_189031. Phagosomal maturation (early endosomal stage).
REACT_189190. Transferrin endocytosis and recycling.

Miscellaneous databases

EvolutionaryTracei P17255.
NextBioi 968420.
PMAP-CutDB P17255.
PROi P17255.

Gene expression databases

Genevestigatori P17255.

Family and domain databases

Gene3Di 1.10.1140.10. 1 hit.
2.170.16.10. 1 hit.
3.10.28.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR028992. Hedgehog/Intein_dom.
IPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR007868. Hom_end_hint.
IPR007869. Homing_endonuc_PI-Sce.
IPR027434. Homing_endonucl.
IPR006142. INTEIN.
IPR004042. Intein_endonuc.
IPR006141. Intein_splice_site.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
PF05204. Hom_end. 2 hits.
PF05203. Hom_end_hint. 1 hit.
[Graphical view ]
PRINTSi PR00379. INTEIN.
SMARTi SM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
[Graphical view ]
SUPFAMi SSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF51294. SSF51294. 2 hits.
SSF52540. SSF52540. 2 hits.
SSF55608. SSF55608. 2 hits.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
PS50818. INTEIN_C_TER. 1 hit.
PS50819. INTEIN_ENDONUCLEASE. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae."
    Hirata R., Ohsumi Y., Nakano A., Kawasaki H., Suzuki K., Anraku Y.
    J. Biol. Chem. 265:6726-6733(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 181-196; 815-820; 826-836; 862-879; 925-936 AND 1004-1013, SUBUNIT.
    Strain: ATCC 26786 / X2180-1A.
  2. "New open reading frames, one of which is similar to the nifV gene of Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of Saccharomyces cerevisiae."
    Verhasselt P., Voet M., Volckaert G.
    Yeast 11:961-966(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth and bud morphogenesis."
    Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.
    Mol. Cell. Biol. 11:4876-4884(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
    Strain: ATCC 208353 / W303-1A.
  6. Bienvenut W.V., Peters C.
    Submitted (OCT-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10; 52-63; 115-136; 173-178; 181-207; 220-239; 264-272; 770-784; 804-814; 826-842; 853-861; 918-937; 940-959; 1004-1014 AND 1058-1065, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides."
    Mizutani R., Nogami S., Kawasaki M., Ohya Y., Anraku Y., Satow Y.
    J. Mol. Biol. 316:919-929(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-6, CLEAVAGE OF INITIATOR METHIONINE, MUTAGENESIS OF CYS-284; HIS-362; ASN-737 AND CYS-738, X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 274-747.
  8. "A dominant trifluoperazine resistance gene from Saccharomyces cerevisiae has homology with F0F1 ATP synthase and confers calcium-sensitive growth."
    Shih C.K., Wagner R., Feinstein S., Kanik-Ennulat C., Neff N.
    Mol. Cell. Biol. 8:3094-3103(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-1071.
  9. "Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase."
    Kane P.M., Yamashiro C.T., Wolczyk D.F., Neff N., Goebl M., Stevens T.H.
    Science 250:651-657(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SPLICING.
  10. "Mutations at the putative junction sites of the yeast VMA1 protein, the catalytic subunit of the vacuolar membrane H(+)-ATPase, inhibit its processing by protein splicing."
    Hirata R., Anraku Y.
    Biochem. Biophys. Res. Commun. 188:40-47(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-284 AND CYS-738.
  11. "Protein splicing of the yeast TFP1 intervening protein sequence: a model for self-excision."
    Cooper A.A., Chen Y.-J., Lindorfer M.A., Stevens T.H.
    EMBO J. 12:2575-2583(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-SPLICING MECHANISM.
  12. "Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae."
    Gimble F.S., Thorner J.
    Nature 357:301-306(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF VDE.
  13. "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly."
    Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.
    Nat. Cell Biol. 3:384-391(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAV1 AND RAV2.
  14. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  15. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  16. "Homing in on an endosymbiotic endonuclease."
    Grivell L.A.
    Curr. Biol. 2:450-452(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131; SER-858 AND SER-928, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity."
    Duan X., Gimble F.S., Quiocho F.A.
    Cell 89:555-564(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF PI-SCE I.
  21. "Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking."
    Hu D., Crist M., Duan X., Quiocho F.A., Gimble F.S.
    J. Biol. Chem. 275:2705-2712(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PI-SCE I.
  22. "Structural insights into the protein splicing mechanism of PI-SceI."
    Poland B.W., Xu M.-Q., Quiocho F.A.
    J. Biol. Chem. 275:16408-16413(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 283-741, MUTAGENESIS OF CYS-284 AND ASN-737.
  23. "High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI."
    Werner E., Wende W., Pingoud A., Heinemann U.
    Nucleic Acids Res. 30:3962-3971(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 284-465.

Entry informationi

Entry nameiVATA_YEAST
AccessioniPrimary (citable) accession number: P17255
Secondary accession number(s): D6VRG7, O74301, Q9Y7W5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 185 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3