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Plasma membrane ATPase (EC 3.6.3.6)

 A0A1P8AYX4_ARATH        Unreviewed;       885 AA.
A0A1P8AYX4;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
22-NOV-2017, entry version 8.
RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
EC=3.6.3.6 {ECO:0000256|RuleBase:RU362083};
Name=HA1 {ECO:0000313|EMBL:ANM61856.1};
Synonyms=AHA1 {ECO:0000313|EMBL:ANM61856.1},
H(+)-ATPase 1 {ECO:0000313|EMBL:ANM61856.1},
OPEN STOMATA 2 {ECO:0000313|EMBL:ANM61856.1},
OST2 {ECO:0000313|EMBL:ANM61856.1},
PLASMA MEMBRANE PROTON ATPASE {ECO:0000313|EMBL:ANM61856.1},
PMA {ECO:0000313|EMBL:ANM61856.1};
OrderedLocusNames=At2g18960 {ECO:0000313|EMBL:ANM61856.1};
ORFNames=F19F24.16 {ECO:0000313|EMBL:ANM61856.1},
F19F24_16 {ECO:0000313|EMBL:ANM61856.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000313|EMBL:ANM61856.1, ECO:0000313|Proteomes:UP000006548};
[1] {ECO:0000313|EMBL:ANM61856.1, ECO:0000313|Proteomes:UP000006548}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S., Shea T.P., Benito M.I., Town C.D.,
Fujii C.Y., Mason T., Bowman C.L., Barnstead M., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J., Ronning C.M., Koo H.L., Moffat K.S.,
Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2] {ECO:0000213|PubMed:14506206}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=14506206; DOI=10.1074/mcp.T300006-MCP200;
Nuhse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Large-scale analysis of in vivo phosphorylated membrane proteins by
immobilized metal ion affinity chromatography and mass spectrometry.";
Mol. Cell. Proteomics 2:1234-1243(2003).
[3] {ECO:0000213|PubMed:17586839}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17586839; DOI=10.1074/mcp.M700164-MCP200;
Niittyla T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
"Temporal analysis of sucrose-induced phosphorylation changes in
plasma membrane proteins of Arabidopsis.";
Mol. Cell. Proteomics 6:1711-1726(2007).
[4] {ECO:0000213|PubMed:18433157}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[5] {ECO:0000213|PubMed:19245862}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[6] {ECO:0000213|PubMed:19376835}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[7] {ECO:0000313|EMBL:ANM61856.1}
NUCLEOTIDE SEQUENCE.
TAIR;
Swarbreck D., Lamesch P., Wilks C., Huala E.;
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000313|EMBL:ANM61856.1, ECO:0000313|Proteomes:UP000006548}
GENOME REANNOTATION.
STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
Lavstsen T., Jespersen J.S.;
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
H(+)(Out). {ECO:0000256|RuleBase:RU362083}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIIA subfamily.
{ECO:0000256|RuleBase:RU362083}.
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EMBL; CP002685; ANM61856.1; -; Genomic_DNA.
EMBL; CP002685; ANM61857.1; -; Genomic_DNA.
RefSeq; NP_001324051.1; NM_001335617.1.
RefSeq; NP_001324052.1; NM_001335616.1.
UniGene; At.24695; -.
EnsemblPlants; AT2G18960.2; AT2G18960.2; AT2G18960.
EnsemblPlants; AT2G18960.3; AT2G18960.3; AT2G18960.
GeneID; 816413; -.
Gramene; AT2G18960.2; AT2G18960.2; AT2G18960.
Gramene; AT2G18960.3; AT2G18960.3; AT2G18960.
Proteomes; UP000006548; Chromosome 2.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:UniProtKB-EC.
GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd02076; P-type_ATPase_H; 1.
Gene3D; 3.40.1110.10; -; 1.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006534; P-type_ATPase_IIIA.
InterPro; IPR001757; P_typ_ATPase.
PRINTS; PR00120; HATPASE.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding {ECO:0000256|RuleBase:RU362083};
Complete proteome {ECO:0000313|Proteomes:UP000006548};
Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
Hydrolase {ECO:0000256|RuleBase:RU362083};
Ion transport {ECO:0000256|RuleBase:RU362083};
Membrane {ECO:0000256|RuleBase:RU362083};
Nucleotide-binding {ECO:0000256|RuleBase:RU362083};
Reference proteome {ECO:0000313|Proteomes:UP000006548};
Signal {ECO:0000256|SAM:SignalP};
Transmembrane {ECO:0000256|RuleBase:RU362083};
Transmembrane helix {ECO:0000256|RuleBase:RU362083};
Transport {ECO:0000256|RuleBase:RU362083}.
SIGNAL 1 22 {ECO:0000256|SAM:SignalP}.
CHAIN 23 885 Plasma membrane ATPase.
{ECO:0000256|SAM:SignalP}.
/FTId=PRO_5011179167.
TRANSMEM 179 201 Helical. {ECO:0000256|RuleBase:RU362083}.
TRANSMEM 213 235 Helical. {ECO:0000256|RuleBase:RU362083}.
TRANSMEM 581 603 Helical. {ECO:0000256|RuleBase:RU362083}.
TRANSMEM 609 626 Helical. {ECO:0000256|RuleBase:RU362083}.
TRANSMEM 646 667 Helical. {ECO:0000256|RuleBase:RU362083}.
TRANSMEM 689 708 Helical. {ECO:0000256|RuleBase:RU362083}.
TRANSMEM 720 740 Helical. {ECO:0000256|RuleBase:RU362083}.
TRANSMEM 752 769 Helical. {ECO:0000256|RuleBase:RU362083}.
SEQUENCE 885 AA; 96858 MW; C38C181BE17E3CDF CRC64;
MWNPLSWVME AAALMAIALA NGDNRPPDWQ DFVGIICLLV INSTISFIEE NNAGNAAAAL
MAGLAPKTKV LRDGKWSEQE AAILVPGDIV SIKLGDIIPA DARLLEGDPL KVDQSALTGE
SLPVTKHPGQ EVFSGSTCKQ GEIEAVVIAT GVHTFFGKAA HLVDSTNQVG HFQKVLTSIG
NFCICSIAIG IAIEIVVMYP IQHRKYRDGI DNLLVLLIGG IPIAMPTVLS VTMAIGSHRL
SQQGAITKRM TAIEEMAGMD VLCSDKTGTL TLNKLSVDKN LVEVFCKGVE KDQVLLFAAM
ASRVENQDAI DAAMVGMLAD PKEARAGIRE VHFLPFNPVD KRTALTYIDS DGNWHRVSKG
APEQILDLAN ARPDLRKKVL SCIDKYAERG LRSLAVARQV VPEKTKESPG GPWEFVGLLP
LFDPPRHDSA ETIRRALNLG VNVKMITGDQ LAIGKETGRR LGMGTNMYPS AALLGTDKDS
NIASIPVEEL IEKADGFAGV FPEHKYEIVK KLQERKHIVG MTGDGVNDAP ALKKADIGIA
VADATDAARG ASDIVLTEPG LSVIISAVLT SRAIFQRMKN YTIYAVSITI RIVFGFMLIA
LIWEFDFSAF MVLIIAILND GTIMTISKDR VKPSPTPDSW KLKEIFATGI VLGGYQAIMS
VIFFWAAHKT DFFSDKFGVR SIRDNNDELM GAVYLQVSII SQALIFVTRS RSWSFVERPG
ALLMIAFVIA QLVATLIAVY ADWTFAKVKG IGWGWAGVIW IYSIVTYFPQ DILKFAIRYI
LSGKAWASLF DNRTAFTTKK DYGIGEREAQ WAQAQRTLHG LQPKEDVNIF PEKGSYRELS
EIAEQAKRRA EIARLRELHT LKGHVESVAK LKGLDIDTAG HHYTV


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