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Protein

Calcium-transporting ATPase 2

Gene

PMC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports the calcium to the vacuole and participates in the control of the cytosolic free calcium.

Catalytic activityi

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei445 – 44514-aspartylphosphate intermediateBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium-transporting ATPase activity Source: SGD
  • metal ion binding Source: InterPro

GO - Biological processi

  • calcium ion transport Source: SGD
  • cellular calcium ion homeostasis Source: UniProtKB
  • transmembrane transport Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30530-MONOMER.
ReactomeiREACT_271569. Ion transport by P-type ATPases.
REACT_284367. Reduction of cytosolic Ca++ levels.

Protein family/group databases

TCDBi3.A.3.2.2. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-transporting ATPase 2 (EC:3.6.3.8)
Alternative name(s):
Vacuolar Ca(2+)-ATPase
Gene namesi
Name:PMC1
Ordered Locus Names:YGL006W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL006w.
EuPathDBiFungiDB:YGL006W.
SGDiS000002974. PMC1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 114114CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei115 – 13925HelicalSequence AnalysisAdd
BLAST
Topological domaini140 – 15213ExtracellularSequence AnalysisAdd
BLAST
Transmembranei153 – 17321HelicalSequence AnalysisAdd
BLAST
Topological domaini174 – 349176CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei350 – 36819HelicalSequence AnalysisAdd
BLAST
Topological domaini369 – 38820ExtracellularSequence AnalysisAdd
BLAST
Transmembranei389 – 40921HelicalSequence AnalysisAdd
BLAST
Topological domaini410 – 899490CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei900 – 92223HelicalSequence AnalysisAdd
BLAST
Topological domaini923 – 9297ExtracellularSequence Analysis
Transmembranei930 – 95021HelicalSequence AnalysisAdd
BLAST
Topological domaini951 – 97626CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei977 – 99822HelicalSequence AnalysisAdd
BLAST
Topological domaini999 – 101012ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1011 – 102919HelicalSequence AnalysisAdd
BLAST
Topological domaini1030 – 106536CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1066 – 108621HelicalSequence AnalysisAdd
BLAST
Topological domaini1087 – 109913ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1100 – 112021HelicalSequence AnalysisAdd
BLAST
Topological domaini1121 – 117353CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • fungal-type vacuole membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11731173Calcium-transporting ATPase 2PRO_0000046232Add
BLAST

Proteomic databases

MaxQBiP38929.
PaxDbiP38929.
PeptideAtlasiP38929.

Interactioni

Protein-protein interaction databases

BioGridi33239. 58 interactions.
DIPiDIP-5901N.
IntActiP38929. 29 interactions.
MINTiMINT-684286.

Structurei

3D structure databases

ProteinModelPortaliP38929.
SMRiP38929. Positions 89-971.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00510000046331.
HOGENOMiHOG000265623.
InParanoidiP38929.
KOiK01537.
OrthoDBiEOG7BS4JT.

Family and domain databases

Gene3Di1.20.1110.10. 1 hit.
2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38929-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRQDENSAL LANNENNKPS YTGNENGVYD NFKLSKSQLS DLHNPKSIRS
60 70 80 90 100
FVRLFGYESN SLFKYLKTDK NAGISLPEIS NYRKTNRYKN YGDNSLPERI
110 120 130 140 150
PKSFLQLVWA AFNDKTMQLL TVAAVVSFVL GLYELWMQPP QYDPEGNKIK
160 170 180 190 200
QVDWIEGVAI MIAVFVVVLV SAANDYQKEL QFAKLNKKKE NRKIIVIRND
210 220 230 240 250
QEILISIHHV LVGDVISLQT GDVVPADCVM ISGKCEADES SITGESNTIQ
260 270 280 290 300
KFPVDNSLRD FKKFNSIDSH NHSKPLDIGD VNEDGNKIAD CMLISGSRIL
310 320 330 340 350
SGLGRGVITS VGINSVYGQT MTSLNAEPES TPLQLHLSQL ADNISVYGCV
360 370 380 390 400
SAIILFLVLF TRYLFYIIPE DGRFHDLDPA QKGSKFMNIF ITSITVIVVA
410 420 430 440 450
VPEGLPLAVT LALAFATTRM TKDGNLVRVL RSCETMGSAT AVCSDKTGTL
460 470 480 490 500
TENVMTVVRG FPGNSKFDDS KSLPVSEQRK LNSKKVFEEN CSSSLRNDLL
510 520 530 540 550
ANIVLNSTAF ENRDYKKNDK NTNGSKNMSK NLSFLDKCKS RLSFFKKGNR
560 570 580 590 600
EDDEDQLFKN VNKGRQEPFI GSKTETALLS LARLSLGLQP GELQYLRDQP
610 620 630 640 650
MEKFNIEKVV QTIPFESSRK WAGLVVKYKE GKNKKPFYRF FIKGAAEIVS
660 670 680 690 700
KNCSYKRNSD DTLEEINEDN KKETDDEIKN LASDALRAIS VAHKDFCECD
710 720 730 740 750
SWPPEQLRDK DSPNIAALDL LFNSQKGLIL DGLLGIQDPL RAGVRESVQQ
760 770 780 790 800
CQRAGVTVRM VTGDNILTAK AIARNCAILS TDISSEAYSA MEGTEFRKLT
810 820 830 840 850
KNERIRILPN LRVLARSSPE DKRLLVETLK GMGDVVAVTG DGTNDAPALK
860 870 880 890 900
LADVGFSMGI SGTEVAREAS DIILMTDDFS AIVNAIKWGR CVSVSIKKFI
910 920 930 940 950
QFQLIVNITA VILTFVSSVA SSDETSVLTA VQLLWINLIM DTLAALALAT
960 970 980 990 1000
DKPDPNIMDR KPRGRSTSLI SVSTWKMILS QATLQLIVTF ILHFYGPELF
1010 1020 1030 1040 1050
FKKHEDEITS HQQQQLNAMT FNTFVWLQFF TMLVSRKLDE GDGISNWRGR
1060 1070 1080 1090 1100
ISAANLNFFQ DLGRNYYFLT IMAIIGSCQV LIMFFGGAPF SIARQTKSMW
1110 1120 1130 1140 1150
ITAVLCGMLS LIMGVLVRIC PDEVAVKVFP AAFVQRFKYV FGLEFLRKNH
1160 1170
TGKHDDEEAL LEESDSPEST AFY
Length:1,173
Mass (Da):130,861
Last modified:February 1, 1995 - v1
Checksum:i5BD9ECFF8508F396
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03060 Unassigned DNA. Translation: AAC48919.1.
Z72528 Genomic DNA. Translation: CAA96706.1.
BK006941 Genomic DNA. Translation: DAA08093.1.
PIRiS48877.
RefSeqiNP_011509.1. NM_001180871.1.

Genome annotation databases

EnsemblFungiiYGL006W; YGL006W; YGL006W.
GeneIDi852878.
KEGGisce:YGL006W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03060 Unassigned DNA. Translation: AAC48919.1.
Z72528 Genomic DNA. Translation: CAA96706.1.
BK006941 Genomic DNA. Translation: DAA08093.1.
PIRiS48877.
RefSeqiNP_011509.1. NM_001180871.1.

3D structure databases

ProteinModelPortaliP38929.
SMRiP38929. Positions 89-971.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33239. 58 interactions.
DIPiDIP-5901N.
IntActiP38929. 29 interactions.
MINTiMINT-684286.

Protein family/group databases

TCDBi3.A.3.2.2. the p-type atpase (p-atpase) superfamily.

Proteomic databases

MaxQBiP38929.
PaxDbiP38929.
PeptideAtlasiP38929.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL006W; YGL006W; YGL006W.
GeneIDi852878.
KEGGisce:YGL006W.

Organism-specific databases

CYGDiYGL006w.
EuPathDBiFungiDB:YGL006W.
SGDiS000002974. PMC1.

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00510000046331.
HOGENOMiHOG000265623.
InParanoidiP38929.
KOiK01537.
OrthoDBiEOG7BS4JT.

Enzyme and pathway databases

BioCyciYEAST:G3O-30530-MONOMER.
ReactomeiREACT_271569. Ion transport by P-type ATPases.
REACT_284367. Reduction of cytosolic Ca++ levels.

Miscellaneous databases

NextBioi972517.
PROiP38929.

Family and domain databases

Gene3Di1.20.1110.10. 1 hit.
2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Calcineurin-dependent growth control in Saccharomyces cerevisiae mutants lacking PMC1, a homolog of plasma membrane Ca2+ ATPases."
    Cunningham K.W., Fink G.R.
    J. Cell Biol. 124:351-363(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATC2_YEAST
AccessioniPrimary (citable) accession number: P38929
Secondary accession number(s): D6VUD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 145 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 98 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.