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P38929 (ATC2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-transporting ATPase 2

EC=3.6.3.8
Alternative name(s):
Vacuolar Ca(2+)-ATPase
Gene names
Name:PMC1
Ordered Locus Names:YGL006W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1173 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subcellular location

Vacuole membrane; Multi-pass membrane protein.

Miscellaneous

Present with 98 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11731173Calcium-transporting ATPase 2
PRO_0000046232

Regions

Topological domain1 – 114114Cytoplasmic Potential
Transmembrane115 – 13925Helical; Potential
Topological domain140 – 15213Extracellular Potential
Transmembrane153 – 17321Helical; Potential
Topological domain174 – 349176Cytoplasmic Potential
Transmembrane350 – 36819Helical; Potential
Topological domain369 – 38820Extracellular Potential
Transmembrane389 – 40921Helical; Potential
Topological domain410 – 899490Cytoplasmic Potential
Transmembrane900 – 92223Helical; Potential
Topological domain923 – 9297Extracellular Potential
Transmembrane930 – 95021Helical; Potential
Topological domain951 – 97626Cytoplasmic Potential
Transmembrane977 – 99822Helical; Potential
Topological domain999 – 101012Extracellular Potential
Transmembrane1011 – 102919Helical; Potential
Topological domain1030 – 106536Cytoplasmic Potential
Transmembrane1066 – 108621Helical; Potential
Topological domain1087 – 109913Extracellular Potential
Transmembrane1100 – 112021Helical; Potential
Topological domain1121 – 117353Cytoplasmic Potential

Sites

Active site44514-aspartylphosphate intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
P38929 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 5BD9ECFF8508F396

FASTA1,173130,861
        10         20         30         40         50         60 
MSRQDENSAL LANNENNKPS YTGNENGVYD NFKLSKSQLS DLHNPKSIRS FVRLFGYESN 

        70         80         90        100        110        120 
SLFKYLKTDK NAGISLPEIS NYRKTNRYKN YGDNSLPERI PKSFLQLVWA AFNDKTMQLL 

       130        140        150        160        170        180 
TVAAVVSFVL GLYELWMQPP QYDPEGNKIK QVDWIEGVAI MIAVFVVVLV SAANDYQKEL 

       190        200        210        220        230        240 
QFAKLNKKKE NRKIIVIRND QEILISIHHV LVGDVISLQT GDVVPADCVM ISGKCEADES 

       250        260        270        280        290        300 
SITGESNTIQ KFPVDNSLRD FKKFNSIDSH NHSKPLDIGD VNEDGNKIAD CMLISGSRIL 

       310        320        330        340        350        360 
SGLGRGVITS VGINSVYGQT MTSLNAEPES TPLQLHLSQL ADNISVYGCV SAIILFLVLF 

       370        380        390        400        410        420 
TRYLFYIIPE DGRFHDLDPA QKGSKFMNIF ITSITVIVVA VPEGLPLAVT LALAFATTRM 

       430        440        450        460        470        480 
TKDGNLVRVL RSCETMGSAT AVCSDKTGTL TENVMTVVRG FPGNSKFDDS KSLPVSEQRK 

       490        500        510        520        530        540 
LNSKKVFEEN CSSSLRNDLL ANIVLNSTAF ENRDYKKNDK NTNGSKNMSK NLSFLDKCKS 

       550        560        570        580        590        600 
RLSFFKKGNR EDDEDQLFKN VNKGRQEPFI GSKTETALLS LARLSLGLQP GELQYLRDQP 

       610        620        630        640        650        660 
MEKFNIEKVV QTIPFESSRK WAGLVVKYKE GKNKKPFYRF FIKGAAEIVS KNCSYKRNSD 

       670        680        690        700        710        720 
DTLEEINEDN KKETDDEIKN LASDALRAIS VAHKDFCECD SWPPEQLRDK DSPNIAALDL 

       730        740        750        760        770        780 
LFNSQKGLIL DGLLGIQDPL RAGVRESVQQ CQRAGVTVRM VTGDNILTAK AIARNCAILS 

       790        800        810        820        830        840 
TDISSEAYSA MEGTEFRKLT KNERIRILPN LRVLARSSPE DKRLLVETLK GMGDVVAVTG 

       850        860        870        880        890        900 
DGTNDAPALK LADVGFSMGI SGTEVAREAS DIILMTDDFS AIVNAIKWGR CVSVSIKKFI 

       910        920        930        940        950        960 
QFQLIVNITA VILTFVSSVA SSDETSVLTA VQLLWINLIM DTLAALALAT DKPDPNIMDR 

       970        980        990       1000       1010       1020 
KPRGRSTSLI SVSTWKMILS QATLQLIVTF ILHFYGPELF FKKHEDEITS HQQQQLNAMT 

      1030       1040       1050       1060       1070       1080 
FNTFVWLQFF TMLVSRKLDE GDGISNWRGR ISAANLNFFQ DLGRNYYFLT IMAIIGSCQV 

      1090       1100       1110       1120       1130       1140 
LIMFFGGAPF SIARQTKSMW ITAVLCGMLS LIMGVLVRIC PDEVAVKVFP AAFVQRFKYV 

      1150       1160       1170 
FGLEFLRKNH TGKHDDEEAL LEESDSPEST AFY 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03060 Unassigned DNA. Translation: AAC48919.1.
Z72528 Genomic DNA. Translation: CAA96706.1.
BK006941 Genomic DNA. Translation: DAA08093.1.
PIRS48877.
RefSeqNP_011509.1. NM_001180871.1.

3D structure databases

ProteinModelPortalP38929.
SMRP38929. Positions 89-971.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33239. 55 interactions.
DIPDIP-5901N.
IntActP38929. 29 interactions.
MINTMINT-684286.
STRING4932.YGL006W.

Protein family/group databases

TCDB3.A.3.2.2. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbP38929.
PeptideAtlasP38929.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL006W; YGL006W; YGL006W.
GeneID852878.
KEGGsce:YGL006W.

Organism-specific databases

CYGDYGL006w.
SGDS000002974. PMC1.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00510000046331.
HOGENOMHOG000265623.
KOK01537.
OrthoDBEOG7BS4JT.

Enzyme and pathway databases

BioCycYEAST:G3O-30530-MONOMER.

Gene expression databases

GenevestigatorP38929.

Family and domain databases

Gene3D1.20.1110.10. 1 hit.
2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
InterProIPR006408. ATPase_P-typ_Ca-transp_plasma.
IPR006068. 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.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972517.

Entry information

Entry nameATC2_YEAST
AccessionPrimary (citable) accession number: P38929
Secondary accession number(s): D6VUD2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families