PMA1_ORYSJ
ID PMA1_ORYSJ Reviewed; 951 AA.
AC Q7XPY2; B7EQF8; Q0J9F5; Q8RW28;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Plasma membrane ATPase;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump;
GN OrderedLocusNames=Os04g0656100, LOC_Os04g56160; ORFNames=OSJNBa0071I13.11;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11935018; DOI=10.1126/science.1068275;
RA Goff S.A., Ricke D., Lan T.H., Presting G., Wang R., Dunn M.,
RA Glazebrook J., Sessions A., Oeller P., Varma H., Hadley D., Hutchison D.,
RA Martin C., Katagiri F., Lange B.M., Moughamer T., Xia Y., Budworth P.,
RA Zhong J., Miguel T., Paszkowski U., Zhang S., Colbert M., Sun W.L.,
RA Chen L., Cooper B., Park S., Wood T.C., Mao L., Quail P., Wing R., Dean R.,
RA Yu Y., Zharkikh A., Shen R., Sahasrabudhe S., Thomas A., Cannings R.,
RA Gutin A., Pruss D., Reid J., Tavtigian S., Mitchell J., Eldredge G.,
RA Scholl T., Miller R.M., Bhatnagar S., Adey N., Rubano T., Tusneem N.,
RA Robinson R., Feldhaus J., Macalma T., Oliphant A., Briggs S.;
RT "A draft sequence of the rice genome (Oryza sativa L. ssp. japonica).";
RL Science 296:92-100(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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 (By
CC similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG94605.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD29313.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ440218; CAD29313.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL606685; CAE03410.3; -; Genomic_DNA.
DR EMBL; AP008210; BAF16032.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91406.1; -; Genomic_DNA.
DR EMBL; AK100435; BAG94605.1; ALT_INIT; mRNA.
DR RefSeq; XP_015635425.1; XM_015779939.1.
DR AlphaFoldDB; Q7XPY2; -.
DR SMR; Q7XPY2; -.
DR STRING; 4530.OS04T0656100-01; -.
DR CarbonylDB; Q7XPY2; -.
DR PaxDb; Q7XPY2; -.
DR PRIDE; Q7XPY2; -.
DR EnsemblPlants; Os04t0656100-01; Os04t0656100-01; Os04g0656100.
DR GeneID; 4337257; -.
DR Gramene; Os04t0656100-01; Os04t0656100-01; Os04g0656100.
DR KEGG; osa:4337257; -.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; Q7XPY2; -.
DR OMA; CFSILAF; -.
DR OrthoDB; 188115at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q7XPY2; baseline and differential.
DR Genevisible; Q7XPY2; OS.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IBA:GO_Central.
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 2: Evidence at transcript 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..951
FT /note="Plasma membrane ATPase"
FT /id="PRO_0000247644"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..805
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..834
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 329
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 366
FT /note="S -> F (in Ref. 1; CAD29313)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="N -> T (in Ref. 1; CAD29313)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="R -> G (in Ref. 1; CAD29313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 951 AA; 104819 MW; 0E904CFD1B06DBA3 CRC64;
MGGLEEIKNE AVDLENIPIE EVFEQLKCTR EGLSSEEGNR RIEMFGPNKL EEKKESKILK
FLGFMWNPLS WVMEMAAIMA IALANGGGKP PDWEDFVGII VLLVINSTIS FIEENNAGNA
AAALMANLAP KTKVLRDGRW GEQEAAILVP GDIISIKLGD IVPADARLLE GDPLKIDQSA
LTGESLPVTK NPGDEVFSGS TCKQGEIEAV VIATGVHTFF GKAAHLVDST NQVGHFQTVL
TAIGNFCICS IAVGIVIEII VMFPIQHRAY RSGIENLLVL LIGGIPIAMP TVLSVTMAIG
SHKLSQQGAI TKRMTAIEEM AGMDVLCSDK TGTLTLNKLS VDKNLVEVFT KGVDKDHVLL
LAARASRTEN QDAIDAAMVG MLADPKEARA GIREVHFLPF NPVDKRTALT YIDADGNWHR
ASKGAPEQIL TLCNCKEDVK RKVHAVIDKY AERGLRSLAV ARQEVPEKSK ESAGGPWQFV
GLLPLFDPPR HDSAETIRKA LHLGVNVKMI TGDQLAIGKE TGRRLGMGTN MYPSSALLGQ
NKDASLEALP VDELIEKADG FAGVFPEHKY EIVKRLQEKK HIVGMTGDGV NDAPALKKAD
IGIAVADATD AARSASDIVL TEPGLSVIIS AVLTSRCIFQ RMKNYTIYAV SITIRIVLGF
LLIALIWKYD FSPFMVLIIA ILNDGTIMTI SKDRVKPSPL PDSWKLKEIF ATGIVLGSYL
ALMTVIFFWA MHKTDFFTDK FGVRSIRNSE HEMMSALYLQ VSIVSQALIF VTRSRSWSFI
ERPGLLLVTA FMLAQLVATF LAVYANWGFA RIKGIGWGWA GVIWLYSIVF YFPLDIFKFF
IRFVLSGRAW DNLLENKIAF TTKKDYGREE REAQWATAQR TLHGLQPPEV ASNTLFNDKS
SYRELSEIAE QAKRRAEIAR LRELNTLKGH VESVVKLKGL DIDTIQQNYT V
