ATC2_YEAST
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 03-AUG-2022, entry version 196.
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; 90.
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; P38929; -.
DR PRIDE; P38929; -.
DR EnsemblFungi; YGL006W_mRNA; YGL006W; YGL006W.
DR GeneID; 852878; -.
DR KEGG; sce:YGL006W; -.
DR SGD; S000002974; PMC1.
DR VEuPathDB; FungiDB:YGL006W; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; P38929; -.
DR OMA; KTAHVGF; -.
DR BioCyc; YEAST:G3O-30530-MON; -.
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 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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
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:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IMP: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; IPR006408; P-type_ATPase_IIB.
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 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; TIGR01517; ATPase-IIB_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
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
