PMA2_SCHPO
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 03-AUG-2022, entry version 167.
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 + 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: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; CAA18989.1; -; 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 STRING; 4896.SPCC1020.01c.1; -.
DR MaxQB; P28876; -.
DR PaxDb; P28876; -.
DR PRIDE; P28876; -.
DR EnsemblFungi; SPCC1020.01c.1; SPCC1020.01c.1:pep; SPCC1020.01c.
DR GeneID; 2539012; -.
DR KEGG; spo:SPCC1020.01c; -.
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; YCIGVEI; -.
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:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0034220; P:ion transmembrane transport; IBA:GO_Central.
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 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..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 63..110
FT /note="Polar 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
