ID   PMA2_YEAST              Reviewed;         947 AA.
AC   P19657; D6W3X8;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   27-MAR-2024, entry version 205.
DE   RecName: Full=Plasma membrane ATPase 2;
DE            EC=7.1.2.1;
DE   AltName: Full=Proton pump 2;
GN   Name=PMA2; OrderedLocusNames=YPL036W;
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=2904437; DOI=10.1016/s0021-9258(19)77659-5;
RA   Schlesser A., Ulaszewski S., Ghislain M., Goffeau A.;
RT   "A second transport ATPase gene in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 263:19480-19487(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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   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).
CC   -!- FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen
CC       ion pump. The proton gradient it generates drives the active transport
CC       of nutrients by H(+)-symport. The resulting external acidification
CC       and/or internal alkinization may mediate growth responses.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- MISCELLANEOUS: There are two plasma membrane ATPases in yeast. This is
CC       the minor isoform.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIA subfamily. {ECO:0000305}.
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DR   EMBL; J04421; AAA83387.1; -; Genomic_DNA.
DR   EMBL; U44030; AAB68184.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11394.1; -; Genomic_DNA.
DR   PIR; S62039; PXBY2P.
DR   RefSeq; NP_015289.1; NM_001183850.1.
DR   AlphaFoldDB; P19657; -.
DR   SMR; P19657; -.
DR   BioGRID; 36143; 493.
DR   DIP; DIP-4036N; -.
DR   IntAct; P19657; 4.
DR   MINT; P19657; -.
DR   STRING; 4932.YPL036W; -.
DR   iPTMnet; P19657; -.
DR   MaxQB; P19657; -.
DR   PaxDb; 4932-YPL036W; -.
DR   PeptideAtlas; P19657; -.
DR   EnsemblFungi; YPL036W_mRNA; YPL036W; YPL036W.
DR   GeneID; 856071; -.
DR   KEGG; sce:YPL036W; -.
DR   AGR; SGD:S000005957; -.
DR   SGD; S000005957; PMA2.
DR   VEuPathDB; FungiDB:YPL036W; -.
DR   eggNOG; KOG0205; Eukaryota.
DR   GeneTree; ENSGT00940000176570; -.
DR   HOGENOM; CLU_002360_6_0_1; -.
DR   InParanoid; P19657; -.
DR   OMA; APLWVFK; -.
DR   OrthoDB; 1058547at2759; -.
DR   BioCyc; YEAST:G3O-33950-MONOMER; -.
DR   BioGRID-ORCS; 856071; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P19657; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P19657; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
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:0008553; F:P-type proton-exporting transporter activity; IDA:SGD.
DR   GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR   GO; GO:1902600; P:proton transmembrane transport; IDA:SGD.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   CDD; cd02076; P-type_ATPase_H; 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; 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; IPR006534; P-type_ATPase_IIIA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01647; ATPase-IIIA_H; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF26; PLASMA MEMBRANE ATPASE 1-RELATED; 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   PRINTS; PR00120; HATPASE.
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   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Hydrogen ion transport; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..947
FT                   /note="Plasma membrane ATPase 2"
FT                   /id="PRO_0000046272"
FT   TOPO_DOM        1..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..169
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..189
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..320
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..342
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        343..353
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..376
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        377..748
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        749..767
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        768..783
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        784..803
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        804..853
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        854..874
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        875..886
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        887..903
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        904..947
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        407
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         663
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         667
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        944
FT                   /note="E -> D (in Ref. 1; AAA83387)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   947 AA;  102172 MW;  24CF0D3EAFD1E9D5 CRC64;
     MSSTEAKQYK EKPSKEYLHA SDGDDPANNS AASSSSSSST STSASSSAAA VPRKAAAASA
     ADDSDSDEDI DQLIDELQSN YGEGDESGEE EVRTDGVHAG QRVVPEKDLS TDPAYGLTSD
     EVARRRKKYG LNQMAEENES LIVKFLMFFV GPIQFVMEAA AILAAGLSDW VDVGVICALL
     LLNASVGFIQ EFQAGSIVDE LKKTLANTAT VIRDGQLIEI PANEVVPGEI LQLESGTIAP
     ADGRIVTEDC FLQIDQSAIT GESLAAEKHY GDEVFSSSTV KTGEAFMVVT ATGDNTFVGR
     AAALVGQASG VEGHFTEVLN GIGIILLVLV IATLLLVWTA CFYRTVGIVS ILRYTLGITI
     IGVPVGLPAV VTTTMAVGAA YLAKKQAIVQ KLSAIESLAG VEILCSDKTG TLTKNKLSLH
     EPYTVEGVSP DDLMLTACLA ASRKKKGLDA IDKAFLKSLI EYPKAKDALT KYKVLEFHPF
     DPVSKKVTAV VESPEGERIV CVKGAPLFVL KTVEEDHPIP EDVHENYENK VAELASRGFR
     ALGVARKRGE GHWEILGVMP CMDPPRDDTA QTINEARNLG LRIKMLTGDA VGIAKETCRQ
     LGLGTNIYNA ERLGLGGGGD MPGSELADFV ENADGFAEVF PQHKYRVVEI LQNRGYLVAM
     TGDGVNDAPS LKKADTGIAV EGATDAARSA ADIVFLAPGL SAIIDALKTS RQIFHRMYSY
     VVYRIALSLH LEIFLGLWIA ILNNSLDINL IVFIAIFADV ATLTIAYDNA PYAPEPVKWN
     LPRLWGMSII LGIVLAIGSW ITLTTMFLPN GGIIQNFGAM NGVMFLQISL TENWLIFVTR
     AAGPFWSSIP SWQLAGAVFA VDIIATMFTL FGWWSENWTD IVSVVRVWIW SIGIFCVLGG
     FYYIMSTSQA FDRLMNGKSL KEKKSTRSVE DFMAAMQRVS TQHEKSS
//