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P13586 (ATC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 150. 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 1

EC=3.6.3.8
Alternative name(s):
Bypass SOD defects protein 1
Golgi Ca(2+)-ATPase
Gene names
Name:PMR1
Synonyms:BSD1, SCC1
Ordered Locus Names:YGL167C
ORF Names:G1666
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length950 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Has a role in the secretory pathway.

Catalytic activity

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

Subcellular location

Golgi apparatus membrane; Multi-pass membrane protein.

Miscellaneous

Present with 6900 molecules/cell in log phase SD medium.

Sequence similarities

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

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentGolgi apparatus
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transmembrane transport

Inferred from direct assay PubMed 10545175. Source: GOC

calcium ion transport

Inferred from direct assay PubMed 10545175. Source: SGD

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 23569283. Source: UniProtKB

exocytosis

Inferred from genetic interaction PubMed 1379856. Source: SGD

manganese ion transmembrane transport

Inferred from direct assay PubMed 10801856. Source: GOC

manganese ion transport

Inferred from direct assay PubMed 10801856. Source: SGD

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 23569283. Source: UniProtKB

Golgi membrane

Inferred from direct assay PubMed 24124599PubMed 9092527. Source: SGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from direct assay PubMed 10545175. Source: SGD

calcium-transporting ATPase activity

Inferred from direct assay PubMed 10545175. Source: SGD

manganese-transporting ATPase activity

Inferred from direct assay PubMed 10801856. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 950949Calcium-transporting ATPase 1
PRO_0000046231

Regions

Topological domain2 – 9291Cytoplasmic Potential
Transmembrane93 – 11119Helical; Potential
Topological domain112 – 1165Lumenal Potential
Transmembrane117 – 13317Helical; Potential
Topological domain134 – 288155Cytoplasmic Potential
Transmembrane289 – 30921Helical; Potential
Topological domain310 – 32314Lumenal Potential
Transmembrane324 – 34421Helical; Potential
Topological domain345 – 814470Cytoplasmic Potential
Transmembrane815 – 83521Helical; Potential
Topological domain836 – 8449Lumenal Potential
Transmembrane845 – 86218Helical; Potential
Topological domain863 – 88422Cytoplasmic Potential
Transmembrane885 – 90521Helical; Potential
Topological domain906 – 9094Lumenal Potential
Transmembrane910 – 93021Helical; Potential
Topological domain931 – 95020Cytoplasmic Potential

Sites

Active site37114-aspartylphosphate intermediate By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.9
Modified residue2271Phosphoserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
P13586 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 0A88271FBD6870B8

FASTA950104,571
        10         20         30         40         50         60 
MSDNPFNASL LDEDSNRERE ILDATAEALS KPSPSLEYCT LSVDEALEKL DTDKNGGLRS 

        70         80         90        100        110        120 
SNEANNRRSL YGPNEITVED DESLFKKFLS NFIEDRMILL LIGSAVVSLF MGNIDDAVSI 

       130        140        150        160        170        180 
TLAIFIVVTV GFVQEYRSEK SLEALNKLVP AECHLMRCGQ ESHVLASTLV PGDLVHFRIG 

       190        200        210        220        230        240 
DRIPADIRII EAIDLSIDES NLTGENEPVH KTSQTIEKSS FNDQPNSIVP ISERSCIAYM 

       250        260        270        280        290        300 
GTLVKEGHGK GIVVGTGTNT SFGAVFEMMN NIEKPKTPLQ LTMDKLGKDL SLVSFIVIGM 

       310        320        330        340        350        360 
ICLVGIIQGR SWLEMFQISV SLAVAAIPEG LPIIVTVTLA LGVLRMAKRK AIVRRLPSVE 

       370        380        390        400        410        420 
TLGSVNVICS DKTGTLTSNH MTVSKLWCLD SMSNKLNVLS LDKNKKTKNS NGNLKNYLTE 

       430        440        450        460        470        480 
DVRETLTIGN LCNNASFSQE HAIFLGNPTD VALLEQLANF EMPDIRNTVQ KVQELPFNSK 

       490        500        510        520        530        540 
RKLMATKILN PVDNKCTVYV KGAFERILEY STSYLKSKGK KTEKLTEAQK ATINECANSM 

       550        560        570        580        590        600 
ASEGLRVFGF AKLTLSDSST PLTEDLIKDL TFTGLIGMND PPRPNVKFAI EQLLQGGVHI 

       610        620        630        640        650        660 
IMITGDSENT AVNIAKQIGI PVIDPKLSVL SGDKLDEMSD DQLANVIDHV NIFARATPEH 

       670        680        690        700        710        720 
KLNIVRALRK RGDVVAMTGD GVNDAPALKL SDIGVSMGRI GTDVAKEASD MVLTDDDFST 

       730        740        750        760        770        780 
ILTAIEEGKG IFNNIQNFLT FQLSTSVAAL SLVALSTAFK LPNPLNAMQI LWINILMDGP 

       790        800        810        820        830        840 
PAQSLGVEPV DHEVMKKPPR KRTDKILTHD VMKRLLTTAA CIIVGTVYIF VKEMAEDGKV 

       850        860        870        880        890        900 
TARDTTMTFT CFVFFDMFNA LACRHNTKSI FEIGFFTNKM FNYAVGLSLL GQMCAIYIPF 

       910        920        930        940        950 
FQSIFKTEKL GISDILLLLL ISSSVFIVDE LRKLWTRKKN EEDSTYFSNV 

« Hide

References

« Hide 'large scale' references
[1]"The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family."
Rudolph H.K., Antebi A., Fink G.R., Buckley C.M., Dorman T.E., Levitre J., Davidow L.S., Mao J.-I., Moir D.T.
Cell 58:133-145(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A putative helicase, the SUA5, PMR1, tRNALys1 genes and four open reading frames have been detected in the DNA sequence of an 8.8 kb fragment of the left arm of chromosome VII of Saccharomyces cerevisiae."
Klima R., Coglievina M., Zaccaria P., Bertani I., Bruschi C.V.
Yeast 12:1033-1040(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"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.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Isolation and characterization of SUA5, a novel gene required for normal growth in Saccharomyces cerevisiae."
Na J.G., Pinto I., Hampsey M.
Genetics 131:791-801(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 863-950.
[6]"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].
[7]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[8]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25488 Genomic DNA. Translation: AAA34884.1.
X85757 Genomic DNA. Translation: CAA59762.1.
Z72690 Genomic DNA. Translation: CAA96880.1.
X64319 Genomic DNA. Translation: CAA45599.1.
BK006941 Genomic DNA. Translation: DAA07946.1.
PIRPWBYR1. A30990.
RefSeqNP_011348.1. NM_001181032.1.

3D structure databases

ProteinModelPortalP13586.
SMRP13586. Positions 31-937.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33087. 515 interactions.
DIPDIP-7899N.
IntActP13586. 16 interactions.
MINTMINT-2781235.
STRING4932.YGL167C.

Protein family/group databases

TCDB3.A.3.2.3. the p-type atpase (p-atpase) superfamily.

Proteomic databases

MaxQBP13586.
PaxDbP13586.
PeptideAtlasP13586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL167C; YGL167C; YGL167C.
GeneID852709.
KEGGsce:YGL167C.

Organism-specific databases

CYGDYGL167c.
SGDS000003135. PMR1.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00560000076887.
HOGENOMHOG000265621.
KOK01537.
OMAIIQGRSW.
OrthoDBEOG7BS4JT.

Enzyme and pathway databases

BioCycYEAST:G3O-30655-MONOMER.

Gene expression databases

GenevestigatorP13586.

Family and domain databases

Gene3D1.20.1110.10. 3 hits.
InterProIPR006413. ATPase_P-typ_Ca-transp_PMR1.
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.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972070.

Entry information

Entry nameATC1_YEAST
AccessionPrimary (citable) accession number: P13586
Secondary accession number(s): D6VTY5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 14, 2014
This is version 150 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