ID   PMA2_SCHPO              Reviewed;        1010 AA.
AC   P28876;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   04-NOV-2026, entry version 184.
DE   RecName: Full=Plasma membrane ATPase 2;
DE            EC=7.1.2.1 {ECO:0000305|PubMed:1833395};
DE   AltName: Full=Proton pump 2;
GN   Name=pma2; ORFNames=SPCC1020.01c, SPCC1393.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=1833395; DOI=10.1016/s0021-9258(18)55265-0;
RA   Ghislain M., Goffeau A.;
RT   "The pma1 and pma2 H(+)-ATPases from Schizosaccharomyces pombe are
RT   functionally interchangeable.";
RL   J. Biol. Chem. 266:18276-18279(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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:0000305|PubMed:1833395}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + H(+)(in) = ADP + phosphate + 2 H(+)(out);
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:0000305|PubMed:1833395};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20853;
CC         Evidence={ECO:0000305|PubMed:1833395};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- PTM: In addition to transient phosphorylation of the active site Asp
CC       residue, this protein, but not the product of the pma1 locus, is
CC       phosphorylated efficiently in isolated plasma membrane.
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; M60471; AAA35325.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAA18989.2; -; Genomic_DNA.
DR   PIR; A40945; PXZP2P.
DR   RefSeq; NP_587959.2; NM_001022950.2.
DR   AlphaFoldDB; P28876; -.
DR   SMR; P28876; -.
DR   BioGRID; 275585; 6.
DR   FunCoup; P28876; 187.
DR   STRING; 284812.P28876; -.
DR   iPTMnet; P28876; -.
DR   PaxDb; 284812-P28876; -.
DR   GeneID; 2539012; -.
DR   KEGG; spo:2539012; -.
DR   PomBase; SPCC1020.01c; pma2.
DR   VEuPathDB; FungiDB:SPCC1020.01c; -.
DR   eggNOG; KOG0205; Eukaryota.
DR   HOGENOM; CLU_002360_6_0_1; -.
DR   InParanoid; P28876; -.
DR   OMA; ADAEWVH; -.
DR   PhylomeDB; P28876; -.
DR   PRO; PR:P28876; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0051286; C:cell tip; HDA:PomBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008553; F:P-type proton-exporting transporter activity; IMP:PomBase.
DR   GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR   GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   CDD; cd02076; P-type_ATPase_H; 1.
DR   FunFam; 2.70.150.10:FF:000011; Plasma membrane ATPase; 1.
DR   FunFam; 3.40.1110.10:FF:000005; Plasma membrane ATPase; 1.
DR   FunFam; 3.40.50.1000:FF:000008; Plasma membrane ATPase; 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; IPR059000; ATPase_P-type_domA.
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; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 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; 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   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Hydrogen ion transport; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..1010
FT                   /note="Plasma membrane ATPase 2"
FT                   /id="PRO_0000046270"
FT   TOPO_DOM        1..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..226
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..246
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..399
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        400..410
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..433
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        434..805
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        806..824
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        825..840
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        841..860
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        861..912
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        913..933
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        934..946
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        947..963
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        964..1010
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..14
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..52
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..151
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        464
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         720
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         724
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1010 AA;  110128 MW;  2C629A45125B4DC3 CRC64;
     MQRNNGEGRP EGMHRISRFL HGNPFKNNAS PQDDSTTRTE VYEEGGVEDS AVDYDNASGN
     AAPRLTAAPN THAQQANLQS GNTSITHETQ STSRGQEATT SPSLSASHEK PARPQTGEGS
     DNEDEDEDID ALIEDLYSQD QEEEQVEEEE SPGPAGAAKV VPEELLETDP KYGLTESEVE
     ERKKKYGLNQ MKEEKTNNIK KFLSFFVGPI QFVMELAAAL AAGLRDWVDF GVICALLLLN
     ATVGFVQEYQ AGSIVDELKK TMALKASVLR DGRVKEIEAS EIVPGDILHL DEGTICPADG
     RLITKDCFLQ VDQSAITGES LAVDKHQNDT MYSSSTVKRG EAFMVVTATA DSTFVGRAAS
     LVGAAGQSQG HFTEVLNGIG TILLVLVILT LLCIYTAAFY RSVRLAALLE YTLAITIIGV
     PVGLPAVVTT TMAVGAAYLA KKKAIVQKLS AIESLAGVEI LCSDKTGTLT KNRLSLGEPY
     CVEGVSPDDL MLTACLASSR KKKGLDAIDK AFLKALRNYP KAKDQLSKYK VLDFHPFDPV
     SKKITAYVEA PDGQRITCVK GAPLWVFKTV QDDHEVPEAI TDAYREQVND MASRGFRSLG
     VARKADGKQW EILGIMPCSD PPRHDTARTI HEAIGLGLRI KMLTGDAVGI AKETARQLGM
     GTNVYNAERL GLSGGGDMPG SEVNDFVEAA DGFAEVFPQH KYAVVDILQQ RGYLVAMTGD
     GVNDAPSLKK ADAGIAVEGA SDAARSAADI VFLAPGLSAI IDALKTSRQI FHRMYAYVVY
     RIALSLHLEI FLGLWLIIRN QLLNLELIVF IAIFADVATL AIAYDNAPYA MKPVKWNLPR
     LWGLATIVGI LLAIGTWIVN TTMIAQGQNR GIVQNFGVQD EVLFLQISLT ENWLIFITRC
     SGPFWSSFPS WQLSGAVLVV DILATLFCIF GWFKGGHQTS IVAVIRIWMY SFGIFCLIAG
     VYYILSESSS FDRWMHGKHK ERGTTRKLED FVMQLQRTST HHEAEGKVTS
//