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
//
