ID C7GU18_YEAS2 Unreviewed; 947 AA.
AC C7GU18;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN Name=PMA2 {ECO:0000313|EMBL:EEU05689.1};
GN ORFNames=C1Q_03899 {ECO:0000313|EMBL:EEU05689.1};
OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=574961 {ECO:0000313|EMBL:EEU05689.1, ECO:0000313|Proteomes:UP000008073};
RN [1] {ECO:0000313|EMBL:EEU05689.1, ECO:0000313|Proteomes:UP000008073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAY291 {ECO:0000313|EMBL:EEU05689.1,
RC ECO:0000313|Proteomes:UP000008073};
RX PubMed=19812109; DOI=10.1101/gr.091777.109;
RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.,
RA Missawa S.K., Galzerani F., Costa G.G., Vidal R.O., Noronha M.F.,
RA Dominska M., Andrietta M.G., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA Tavares F.C., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA Pereira G.A.;
RT "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT bioethanol production.";
RL Genome Res. 19:2258-2270(2009).
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 {ECO:0000256|ARBA:ARBA00003417}.
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 Evidence={ECO:0000256|RuleBase:RU362083};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362083};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362083}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000256|ARBA:ARBA00008804,
CC ECO:0000256|RuleBase:RU362083}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEU05689.1}.
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DR EMBL; ACFL01000283; EEU05689.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GU18; -.
DR Proteomes; UP000008073; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
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; SFLDS00003; Haloacid_Dehalogenase; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362083};
KW Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
KW Ion transport {ECO:0000256|RuleBase:RU362083};
KW Magnesium {ECO:0000256|RuleBase:RU362083};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362083};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362083};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362083};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362083};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362083}; Transport {ECO:0000256|RuleBase:RU362083}.
FT TRANSMEM 141..164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 170..189
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 358..383
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 721..742
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 748..767
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 788..808
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 820..842
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 854..875
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 887..905
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 96..169
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
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"
SQ SEQUENCE 947 AA; 102220 MW; 43481EB3A216E8FA CRC64;
MSSTEAKQYK EKPSKEYLHA SDGDDPANNS AASSSSSSST STSASSSAAA VPRKAAAASA
ADDSDSDEDI DQLIDELQSN YGEGDESGEE EVRTDGVHAG QRVVPEKDLS TDPAYGLTSD
EVARRRKKYG LNQMAEENES LIVKFLMFFV GPIQFVMEAA AILAAGLSDW VDFGVICALL
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
//
