ATC1_YEAST
ID ATC1_YEAST Reviewed; 950 AA.
AC P13586; D6VTY5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Calcium-transporting ATPase 1;
DE EC=7.2.2.10;
DE AltName: Full=Bypass SOD defects protein 1;
DE AltName: Full=Golgi Ca(2+)-ATPase;
GN Name=PMR1; Synonyms=BSD1, SCC1; OrderedLocusNames=YGL167C; ORFNames=G1666;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2526682; DOI=10.1016/0092-8674(89)90410-8;
RA Rudolph H.K., Antebi A., Fink G.R., Buckley C.M., Dorman T.E., Levitre J.,
RA Davidow L.S., Mao J.-I., Moir D.T.;
RT "The yeast secretory pathway is perturbed by mutations in PMR1, a member of
RT a Ca2+ ATPase family.";
RL Cell 58:133-145(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896267;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1033::aid-yea983>3.0.co;2-v;
RA Klima R., Coglievina M., Zaccaria P., Bertani I., Bruschi C.V.;
RT "A putative helicase, the SUA5, PMR1, tRNALys1 genes and four open reading
RT frames have been detected in the DNA sequence of an 8.8 kb fragment of the
RT left arm of chromosome VII of Saccharomyces cerevisiae.";
RL Yeast 12:1033-1040(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 863-950.
RX PubMed=1325384; DOI=10.1093/genetics/131.4.791;
RA Na J.G., Pinto I., Hampsey M.;
RT "Isolation and characterization of SUA5, a novel gene required for normal
RT growth in Saccharomyces cerevisiae.";
RL Genetics 131:791-801(1992).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of calcium. Has a role in the secretory
CC pathway.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein.
CC -!- MISCELLANEOUS: Present with 6900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000305}.
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DR EMBL; M25488; AAA34884.1; -; Genomic_DNA.
DR EMBL; X85757; CAA59762.1; -; Genomic_DNA.
DR EMBL; Z72690; CAA96880.1; -; Genomic_DNA.
DR EMBL; X64319; CAA45599.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07946.1; -; Genomic_DNA.
DR PIR; A30990; PWBYR1.
DR RefSeq; NP_011348.1; NM_001181032.1.
DR AlphaFoldDB; P13586; -.
DR SMR; P13586; -.
DR BioGRID; 33087; 836.
DR DIP; DIP-7899N; -.
DR IntAct; P13586; 19.
DR MINT; P13586; -.
DR STRING; 4932.YGL167C; -.
DR TCDB; 3.A.3.2.3; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P13586; -.
DR MaxQB; P13586; -.
DR PaxDb; P13586; -.
DR PRIDE; P13586; -.
DR EnsemblFungi; YGL167C_mRNA; YGL167C; YGL167C.
DR GeneID; 852709; -.
DR KEGG; sce:YGL167C; -.
DR SGD; S000003135; PMR1.
DR VEuPathDB; FungiDB:YGL167C; -.
DR eggNOG; KOG0202; Eukaryota.
DR GeneTree; ENSGT00940000168572; -.
DR HOGENOM; CLU_002360_3_0_1; -.
DR InParanoid; P13586; -.
DR OMA; GVHRMAK; -.
DR BioCyc; YEAST:G3O-30655-MON; -.
DR BRENDA; 7.2.2.10; 984.
DR BRENDA; 7.2.2.22; 984.
DR Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR PRO; PR:P13586; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P13586; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IDA:SGD.
DR GO; GO:0005388; F:P-type calcium transporter activity; IDA:SGD.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0140613; F:P-type manganese transporter activity; IDA:SGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IDA:SGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IMP:SGD.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0006828; P:manganese ion transport; IDA:SGD.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006413; P-type_ATPase_IIA_PMR1.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01522; ATPase-IIA2_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Calcium; Calcium transport; Golgi apparatus;
KW Ion transport; Magnesium; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..950
FT /note="Calcium-transporting ATPase 1"
FT /id="PRO_0000046231"
FT TOPO_DOM 2..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..116
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..323
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..814
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 815..835
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 836..844
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 863..884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..909
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 910..930
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 931..950
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 371
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 950 AA; 104571 MW; 0A88271FBD6870B8 CRC64;
MSDNPFNASL LDEDSNRERE ILDATAEALS KPSPSLEYCT LSVDEALEKL DTDKNGGLRS
SNEANNRRSL YGPNEITVED DESLFKKFLS NFIEDRMILL LIGSAVVSLF MGNIDDAVSI
TLAIFIVVTV GFVQEYRSEK SLEALNKLVP AECHLMRCGQ ESHVLASTLV PGDLVHFRIG
DRIPADIRII EAIDLSIDES NLTGENEPVH KTSQTIEKSS FNDQPNSIVP ISERSCIAYM
GTLVKEGHGK GIVVGTGTNT SFGAVFEMMN NIEKPKTPLQ LTMDKLGKDL SLVSFIVIGM
ICLVGIIQGR SWLEMFQISV SLAVAAIPEG LPIIVTVTLA LGVLRMAKRK AIVRRLPSVE
TLGSVNVICS DKTGTLTSNH MTVSKLWCLD SMSNKLNVLS LDKNKKTKNS NGNLKNYLTE
DVRETLTIGN LCNNASFSQE HAIFLGNPTD VALLEQLANF EMPDIRNTVQ KVQELPFNSK
RKLMATKILN PVDNKCTVYV KGAFERILEY STSYLKSKGK KTEKLTEAQK ATINECANSM
ASEGLRVFGF AKLTLSDSST PLTEDLIKDL TFTGLIGMND PPRPNVKFAI EQLLQGGVHI
IMITGDSENT AVNIAKQIGI PVIDPKLSVL SGDKLDEMSD DQLANVIDHV NIFARATPEH
KLNIVRALRK RGDVVAMTGD GVNDAPALKL SDIGVSMGRI GTDVAKEASD MVLTDDDFST
ILTAIEEGKG IFNNIQNFLT FQLSTSVAAL SLVALSTAFK LPNPLNAMQI LWINILMDGP
PAQSLGVEPV DHEVMKKPPR KRTDKILTHD VMKRLLTTAA CIIVGTVYIF VKEMAEDGKV
TARDTTMTFT CFVFFDMFNA LACRHNTKSI FEIGFFTNKM FNYAVGLSLL GQMCAIYIPF
FQSIFKTEKL GISDILLLLL ISSSVFIVDE LRKLWTRKKN EEDSTYFSNV
