PMA1_SCHPO
ID PMA1_SCHPO Reviewed; 919 AA.
AC P09627;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Plasma membrane ATPase 1;
DE EC=7.1.2.1 {ECO:0000305|PubMed:2891694};
DE AltName: Full=Proton pump 1;
GN Name=pma1; ORFNames=SPAC1071.10c;
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=2891694; DOI=10.1016/s0021-9258(18)45416-6;
RA Ghislain M., Schlesser A., Goffeau A.;
RT "Mutation of a conserved glycine residue modifies the vanadate sensitivity
RT of the plasma membrane H+-ATPase from Schizosaccharomyces pombe.";
RL J. Biol. Chem. 262:17549-17555(1987).
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-494 AND SER-899, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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:2891694}.
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:0000305|PubMed:2891694};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20853;
CC Evidence={ECO:0000305|PubMed:2891694};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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; J03498; AAA35324.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB59886.1; -; Genomic_DNA.
DR PIR; A28454; PXZP1P.
DR RefSeq; NP_594360.1; NM_001019781.2.
DR AlphaFoldDB; P09627; -.
DR SMR; P09627; -.
DR BioGRID; 279117; 11.
DR DIP; DIP-59125N; -.
DR IntAct; P09627; 1.
DR STRING; 4896.SPAC1071.10c.1; -.
DR iPTMnet; P09627; -.
DR MaxQB; P09627; -.
DR PaxDb; P09627; -.
DR PRIDE; P09627; -.
DR EnsemblFungi; SPAC1071.10c.1; SPAC1071.10c.1:pep; SPAC1071.10c.
DR GeneID; 2542664; -.
DR KEGG; spo:SPAC1071.10c; -.
DR PomBase; SPAC1071.10c; pma1.
DR VEuPathDB; FungiDB:SPAC1071.10c; -.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_0_1; -.
DR InParanoid; P09627; -.
DR OMA; FTIFGWF; -.
DR PhylomeDB; P09627; -.
DR PRO; PR:P09627; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IDA:PomBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IMP:PomBase.
DR GO; GO:1901691; F:proton binding; IDA:PomBase.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0120029; P:proton export across plasma membrane; IMP:PomBase.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:PomBase.
DR CDD; cd02076; P-type_ATPase_H; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
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; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
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..919
FT /note="Plasma membrane ATPase 1"
FT /id="PRO_0000046269"
FT TOPO_DOM 1..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..158
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..311
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..322
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..345
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..717
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..736
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..752
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..772
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..824
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 825..845
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 846..858
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..875
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 876..919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 376
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 632
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 636
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 919 AA; 99884 MW; 0AE31B92ED607CC7 CRC64;
MADNAGEYHD AEKHAPEQQA PPPQQPAHAA APAQDDEPDD DIDALIEELF SEDVQEEQED
NDDAPAAGEA KAVPEELLQT DMNTGLTMSE VEERRKKYGL NQMKEELENP FLKFIMFFVG
PIQFVMEMAA ALAAGLRDWV DFGVICALLM LNAVVGFVQE YQAGSIVDEL KKSLALKAVV
IREGQVHELE ANEVVPGDIL KLDEGTIICA DGRVVTPDVH LQVDQSAITG ESLAVDKHYG
DPTFASSGVK RGEGLMVVTA TGDSTFVGRA ASLVNAAAGG TGHFTEVLNG IGTILLVLVL
LTLFCIYTAA FYRSVRLARL LEYTLAITII GVPVGLPAVV TTTMAVGAAY LAEKQAIVQK
LSAIESLAGV EVLCSDKTGT LTKNKLSLGE PFTVSGVSGD DLVLTACLAA SRKRKGLDAI
DKAFLKALKN YPGPRSMLTK YKVIEFQPFD PVSKKVTAYV QAPDGTRITC VKGAPLWVLK
TVEEDHPIPE DVLSAYKDKV GDLASRGYRS LGVARKIEGQ HWEIMGIMPC SDPPRHDTAR
TISEAKRLGL RVKMLTGDAV DIAKETARQL GMGTNIYNAE RLGLTGGGNM PGSEVYDFVE
AADGFGEVFP QHKYAVVDIL QQRGYLVAMT GDGVNDAPSL KKADTGIAVE GATDAARSAA
DIVFLAPGLS AIIDALKTSR QIFHRMYSYV VYRIALSLHL EIFLGLWLII RNQLLNLELV
VFIAIFADVA TLAIAYDNAP YSMKPVKWNL PRLWGLSTVI GIVLAIGTWI TNTTMIAQGQ
NRGIVQNFGV QDEVLFLEIS LTENWLIFVT RCNGPFWSSI PSWQLSGAVL AVDILATMFC
IFGWFKGGHQ TSIVAVLRIW MYSFGIFCIM AGTYYILSES AGFDRMMNGK PKESRNQRSI
EDLVVALQRT STRHEKGDA
