ID   ATC2_YEAST              Reviewed;        1173 AA.
AC   P38929; D6VUD2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Calcium-transporting ATPase 2;
DE            EC=7.2.2.10;
DE   AltName: Full=Vacuolar Ca(2+)-ATPase;
GN   Name=PMC1; OrderedLocusNames=YGL006W;
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.
RX   PubMed=7507493; DOI=10.1083/jcb.124.3.351;
RA   Cunningham K.W., Fink G.R.;
RT   "Calcineurin-dependent growth control in Saccharomyces cerevisiae mutants
RT   lacking PMC1, a homolog of plasma membrane Ca2+ ATPases.";
RL   J. Cell Biol. 124:351-363(1994).
RN   [2]
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   [3]
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   [4]
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).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the transport of calcium. Transports the calcium to
CC       the vacuole and participates in the control of the cytosolic free
CC       calcium.
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   -!- INTERACTION:
CC       P38929; P38310: FTH1; NbExp=3; IntAct=EBI-3097, EBI-20959;
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC   -!- MISCELLANEOUS: Present with 98 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; U03060; AAC48919.1; -; Unassigned_DNA.
DR   EMBL; Z72528; CAA96706.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08093.1; -; Genomic_DNA.
DR   PIR; S48877; S48877.
DR   RefSeq; NP_011509.1; NM_001180871.1.
DR   AlphaFoldDB; P38929; -.
DR   SMR; P38929; -.
DR   BioGRID; 33239; 97.
DR   DIP; DIP-5901N; -.
DR   IntAct; P38929; 39.
DR   MINT; P38929; -.
DR   STRING; 4932.YGL006W; -.
DR   TCDB; 3.A.3.2.2; the p-type atpase (p-atpase) superfamily.
DR   iPTMnet; P38929; -.
DR   MaxQB; P38929; -.
DR   PaxDb; 4932-YGL006W; -.
DR   PeptideAtlas; P38929; -.
DR   EnsemblFungi; YGL006W_mRNA; YGL006W; YGL006W.
DR   GeneID; 852878; -.
DR   KEGG; sce:YGL006W; -.
DR   AGR; SGD:S000002974; -.
DR   SGD; S000002974; PMC1.
DR   VEuPathDB; FungiDB:YGL006W; -.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_2_1; -.
DR   InParanoid; P38929; -.
DR   OMA; QWGYSIV; -.
DR   OrthoDB; 847at2759; -.
DR   BioCyc; YEAST:G3O-30530-MONOMER; -.
DR   Reactome; R-SCE-418359; Reduction of cytosolic Ca++ levels.
DR   Reactome; R-SCE-5578775; Ion homeostasis.
DR   Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR   BioGRID-ORCS; 852878; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38929; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P38929; Protein.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IMP:SGD.
DR   GO; GO:0006816; P:calcium ion transport; IMP:SGD.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR   CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Calcium transport; Ion transport; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Translocase; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..1173
FT                   /note="Calcium-transporting ATPase 2"
FT                   /id="PRO_0000046232"
FT   TOPO_DOM        1..114
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        115..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        140..152
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        174..349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        350..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        369..388
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        410..899
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        900..922
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        923..929
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        930..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        951..976
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        977..998
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        999..1010
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1011..1029
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        1030..1065
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1066..1086
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        1087..1099
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1100..1120
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        1121..1173
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        445
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         398
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         403
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         445
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         447
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         447
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         643
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         762..764
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         816
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         822
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         841
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         844
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         907
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         937
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         941
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         941
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
SQ   SEQUENCE   1173 AA;  130861 MW;  5BD9ECFF8508F396 CRC64;
     MSRQDENSAL LANNENNKPS YTGNENGVYD NFKLSKSQLS DLHNPKSIRS FVRLFGYESN
     SLFKYLKTDK NAGISLPEIS NYRKTNRYKN YGDNSLPERI PKSFLQLVWA AFNDKTMQLL
     TVAAVVSFVL GLYELWMQPP QYDPEGNKIK QVDWIEGVAI MIAVFVVVLV SAANDYQKEL
     QFAKLNKKKE NRKIIVIRND QEILISIHHV LVGDVISLQT GDVVPADCVM ISGKCEADES
     SITGESNTIQ KFPVDNSLRD FKKFNSIDSH NHSKPLDIGD VNEDGNKIAD CMLISGSRIL
     SGLGRGVITS VGINSVYGQT MTSLNAEPES TPLQLHLSQL ADNISVYGCV SAIILFLVLF
     TRYLFYIIPE DGRFHDLDPA QKGSKFMNIF ITSITVIVVA VPEGLPLAVT LALAFATTRM
     TKDGNLVRVL RSCETMGSAT AVCSDKTGTL TENVMTVVRG FPGNSKFDDS KSLPVSEQRK
     LNSKKVFEEN CSSSLRNDLL ANIVLNSTAF ENRDYKKNDK NTNGSKNMSK NLSFLDKCKS
     RLSFFKKGNR EDDEDQLFKN VNKGRQEPFI GSKTETALLS LARLSLGLQP GELQYLRDQP
     MEKFNIEKVV QTIPFESSRK WAGLVVKYKE GKNKKPFYRF FIKGAAEIVS KNCSYKRNSD
     DTLEEINEDN KKETDDEIKN LASDALRAIS VAHKDFCECD SWPPEQLRDK DSPNIAALDL
     LFNSQKGLIL DGLLGIQDPL RAGVRESVQQ CQRAGVTVRM VTGDNILTAK AIARNCAILS
     TDISSEAYSA MEGTEFRKLT KNERIRILPN LRVLARSSPE DKRLLVETLK GMGDVVAVTG
     DGTNDAPALK LADVGFSMGI SGTEVAREAS DIILMTDDFS AIVNAIKWGR CVSVSIKKFI
     QFQLIVNITA VILTFVSSVA SSDETSVLTA VQLLWINLIM DTLAALALAT DKPDPNIMDR
     KPRGRSTSLI SVSTWKMILS QATLQLIVTF ILHFYGPELF FKKHEDEITS HQQQQLNAMT
     FNTFVWLQFF TMLVSRKLDE GDGISNWRGR ISAANLNFFQ DLGRNYYFLT IMAIIGSCQV
     LIMFFGGAPF SIARQTKSMW ITAVLCGMLS LIMGVLVRIC PDEVAVKVFP AAFVQRFKYV
     FGLEFLRKNH TGKHDDEEAL LEESDSPEST AFY
//