P13586 (ATC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	950 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.6
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. [View classification]

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Golgi apparatus Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Magnesium Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from direct assay. Source: SGD calcium-transporting ATPase activity Inferred from mutant phenotype. Source: SGD manganese-transporting ATPase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 950	950	Calcium-transporting ATPase 1		PRO_0000046231
Regions
	Topological domain	1 – 92	92	Cytoplasmic Potential
	Transmembrane	93 – 111	19	Helical; Potential
	Topological domain	112 – 116	5	Lumenal Potential
	Transmembrane	117 – 133	17	Helical; Potential
	Topological domain	134 – 288	155	Cytoplasmic Potential
	Transmembrane	289 – 309	21	Helical; Potential
	Topological domain	310 – 323	14	Lumenal Potential
	Transmembrane	324 – 344	21	Helical; Potential
	Topological domain	345 – 814	470	Cytoplasmic Potential
	Transmembrane	815 – 835	21	Helical; Potential
	Topological domain	836 – 844	9	Lumenal Potential
	Transmembrane	845 – 862	18	Helical; Potential
	Topological domain	863 – 884	22	Cytoplasmic Potential
	Transmembrane	885 – 905	21	Helical; Potential
	Topological domain	906 – 909	4	Lumenal Potential
	Transmembrane	910 – 930	21	Helical; Potential
	Topological domain	931 – 950	20	Cytoplasmic Potential
Sites
	Active site	371	1	4-aspartylphosphate intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13586 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 0A88271FBD6870B8	FASTA	950	104,571
	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

References

	« Hide 'large scale' referencesShow '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: 2526682] [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: 8896267] [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: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 1325384] [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: 14562106] [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: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: ATCC 208353 / W303-1A.
+	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.
PIR	PWBYR1. A30990.
RefSeq	NP_011348.1. NM_001181032.1.
3D structure databases
ProteinModelPortal	P13586.
SMR	P13586. Positions 36-941.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-7899N.
IntAct	P13586. 26 interactions.
MINT	MINT-2781235.
STRING	P13586.
Protein family/group databases
TCDB	3.A.3.2.3. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PeptideAtlas	P13586.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL167C; YGL167C; YGL167C.
GeneID	852709.
KEGG	sce:YGL167C.
NMPDR	fig|4932.3.peg.2452.
Organism-specific databases
CYGD	YGL167c.
SGD	S000003135. PMR1.
Phylogenomic databases
eggNOG	fuNOG04517.
GeneTree	EFGT00050000000742.
HOGENOM	HBG456486.
OMA	LMPPECH.
OrthoDB	EOG498Z7V.
Gene expression databases
ArrayExpress	P13586.
Genevestigator	P13586.
GermOnline	YGL167C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR006413. ATPase_P-typ_Ca-transp_PMR1. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR000695. ATPase_P-typ_H-transp. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KO	K01537.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01522. ATPase-IIA2_Ca. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972070.

Entry information

Entry name

ATC1_YEAST

Accession

Primary (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:	January 25, 2012
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program