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Protein

Calcium-transporting ATPase 1

Gene

PMR1

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

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei371 – 37114-aspartylphosphate intermediateBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium ion binding Source: SGD
  3. calcium-transporting ATPase activity Source: SGD
  4. manganese-transporting ATPase activity Source: SGD

GO - Biological processi

  1. calcium ion transmembrane transport Source: GOC
  2. calcium ion transport Source: SGD
  3. cellular calcium ion homeostasis Source: UniProtKB
  4. exocytosis Source: SGD
  5. manganese ion transmembrane transport Source: GOC
  6. manganese ion 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-30655-MONOMER.
ReactomeiREACT_96459. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.2.3. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-transporting ATPase 1 (EC:3.6.3.8)
Alternative name(s):
Bypass SOD defects protein 1
Golgi Ca(2+)-ATPase
Gene namesi
Name:PMR1
Synonyms:BSD1, SCC1
Ordered Locus Names:YGL167C
ORF Names:G1666
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL167c.
SGDiS000003135. PMR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 9291CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei93 – 11119HelicalSequence AnalysisAdd
BLAST
Topological domaini112 – 1165LumenalSequence Analysis
Transmembranei117 – 13317HelicalSequence AnalysisAdd
BLAST
Topological domaini134 – 288155CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei289 – 30921HelicalSequence AnalysisAdd
BLAST
Topological domaini310 – 32314LumenalSequence AnalysisAdd
BLAST
Transmembranei324 – 34421HelicalSequence AnalysisAdd
BLAST
Topological domaini345 – 814470CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei815 – 83521HelicalSequence AnalysisAdd
BLAST
Topological domaini836 – 8449LumenalSequence Analysis
Transmembranei845 – 86218HelicalSequence AnalysisAdd
BLAST
Topological domaini863 – 88422CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei885 – 90521HelicalSequence AnalysisAdd
BLAST
Topological domaini906 – 9094LumenalSequence Analysis
Transmembranei910 – 93021HelicalSequence AnalysisAdd
BLAST
Topological domaini931 – 95020CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. Golgi membrane Source: SGD
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 950949Calcium-transporting ATPase 1PRO_0000046231Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei227 – 2271Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP13586.
PaxDbiP13586.
PeptideAtlasiP13586.

Expressioni

Gene expression databases

GenevestigatoriP13586.

Interactioni

Protein-protein interaction databases

BioGridi33087. 517 interactions.
DIPiDIP-7899N.
IntActiP13586. 16 interactions.
MINTiMINT-2781235.
STRINGi4932.YGL167C.

Structurei

3D structure databases

ProteinModelPortaliP13586.
SMRiP13586. Positions 31-937.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOGENOMiHOG000265621.
InParanoidiP13586.
KOiK01537.
OMAiDIRITHA.
OrthoDBiEOG7BS4JT.

Family and domain databases

Gene3Di1.20.1110.10. 3 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.
IPR006413. P-type_ATPase_IIA_PMR1.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF217. PTHR24093:SF217. 1 hit.
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.
PR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13586-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDNPFNASL LDEDSNRERE ILDATAEALS KPSPSLEYCT LSVDEALEKL
60 70 80 90 100
DTDKNGGLRS SNEANNRRSL YGPNEITVED DESLFKKFLS NFIEDRMILL
110 120 130 140 150
LIGSAVVSLF MGNIDDAVSI TLAIFIVVTV GFVQEYRSEK SLEALNKLVP
160 170 180 190 200
AECHLMRCGQ ESHVLASTLV PGDLVHFRIG DRIPADIRII EAIDLSIDES
210 220 230 240 250
NLTGENEPVH KTSQTIEKSS FNDQPNSIVP ISERSCIAYM GTLVKEGHGK
260 270 280 290 300
GIVVGTGTNT SFGAVFEMMN NIEKPKTPLQ LTMDKLGKDL SLVSFIVIGM
310 320 330 340 350
ICLVGIIQGR SWLEMFQISV SLAVAAIPEG LPIIVTVTLA LGVLRMAKRK
360 370 380 390 400
AIVRRLPSVE TLGSVNVICS DKTGTLTSNH MTVSKLWCLD SMSNKLNVLS
410 420 430 440 450
LDKNKKTKNS NGNLKNYLTE DVRETLTIGN LCNNASFSQE HAIFLGNPTD
460 470 480 490 500
VALLEQLANF EMPDIRNTVQ KVQELPFNSK RKLMATKILN PVDNKCTVYV
510 520 530 540 550
KGAFERILEY STSYLKSKGK KTEKLTEAQK ATINECANSM ASEGLRVFGF
560 570 580 590 600
AKLTLSDSST PLTEDLIKDL TFTGLIGMND PPRPNVKFAI EQLLQGGVHI
610 620 630 640 650
IMITGDSENT AVNIAKQIGI PVIDPKLSVL SGDKLDEMSD DQLANVIDHV
660 670 680 690 700
NIFARATPEH KLNIVRALRK RGDVVAMTGD GVNDAPALKL SDIGVSMGRI
710 720 730 740 750
GTDVAKEASD MVLTDDDFST ILTAIEEGKG IFNNIQNFLT FQLSTSVAAL
760 770 780 790 800
SLVALSTAFK LPNPLNAMQI LWINILMDGP PAQSLGVEPV DHEVMKKPPR
810 820 830 840 850
KRTDKILTHD VMKRLLTTAA CIIVGTVYIF VKEMAEDGKV TARDTTMTFT
860 870 880 890 900
CFVFFDMFNA LACRHNTKSI FEIGFFTNKM FNYAVGLSLL GQMCAIYIPF
910 920 930 940 950
FQSIFKTEKL GISDILLLLL ISSSVFIVDE LRKLWTRKKN EEDSTYFSNV
Length:950
Mass (Da):104,571
Last modified:January 1, 1990 - v1
Checksum:i0A88271FBD6870B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA30990. PWBYR1.
RefSeqiNP_011348.1. NM_001181032.1.

Genome annotation databases

EnsemblFungiiYGL167C; YGL167C; YGL167C.
GeneIDi852709.
KEGGisce:YGL167C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA30990. PWBYR1.
RefSeqiNP_011348.1. NM_001181032.1.

3D structure databases

ProteinModelPortaliP13586.
SMRiP13586. Positions 31-937.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33087. 517 interactions.
DIPiDIP-7899N.
IntActiP13586. 16 interactions.
MINTiMINT-2781235.
STRINGi4932.YGL167C.

Protein family/group databases

TCDBi3.A.3.2.3. the p-type atpase (p-atpase) superfamily.

Proteomic databases

MaxQBiP13586.
PaxDbiP13586.
PeptideAtlasiP13586.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL167C; YGL167C; YGL167C.
GeneIDi852709.
KEGGisce:YGL167C.

Organism-specific databases

CYGDiYGL167c.
SGDiS000003135. PMR1.

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOGENOMiHOG000265621.
InParanoidiP13586.
KOiK01537.
OMAiDIRITHA.
OrthoDBiEOG7BS4JT.

Enzyme and pathway databases

BioCyciYEAST:G3O-30655-MONOMER.
ReactomeiREACT_96459. Ion transport by P-type ATPases.

Miscellaneous databases

NextBioi972070.

Gene expression databases

GenevestigatoriP13586.

Family and domain databases

Gene3Di1.20.1110.10. 3 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.
IPR006413. P-type_ATPase_IIA_PMR1.
IPR001757. P_typ_ATPase.
[Graphical view]
PANTHERiPTHR24093:SF217. PTHR24093:SF217. 1 hit.
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.
PR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01522. ATPase-IIA2_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATC1_YEAST
AccessioniPrimary (citable) accession number: P13586
Secondary accession number(s): D6VTY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: January 7, 2015
This is version 154 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 6900 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.