PMA7_ARATH
ID PMA7_ARATH Reviewed; 961 AA.
AC Q9LY32;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=ATPase 7, plasma membrane-type;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 7;
GN Name=AHA7; OrderedLocusNames=At3g60330; ORFNames=F27H5_120;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: The plasma membrane H(+) ATPase of plants and fungi generates
CC a proton gradient that drives the active transport of nutrients by
CC H(+)-symport. The resulting external acidification and/or internal
CC alkinization may mediate growth responses (By similarity).
CC {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 -!- SUBUNIT: Binds to 14-3-3 proteins. The binding is induced by
CC phosphorylation of Thr-960. Binding to 14-3-3 proteins activates the
CC H(+)-ATPase (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL163852; CAB87870.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80046.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80047.1; -; Genomic_DNA.
DR PIR; T49228; T49228.
DR RefSeq; NP_001190141.1; NM_001203212.1.
DR RefSeq; NP_191592.5; NM_115897.5.
DR AlphaFoldDB; Q9LY32; -.
DR SMR; Q9LY32; -.
DR BioGRID; 10518; 7.
DR IntAct; Q9LY32; 3.
DR STRING; 3702.AT3G60330.2; -.
DR TCDB; 3.A.3.3.12; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q9LY32; -.
DR PaxDb; Q9LY32; -.
DR PRIDE; Q9LY32; -.
DR ProteomicsDB; 236648; -.
DR EnsemblPlants; AT3G60330.1; AT3G60330.1; AT3G60330.
DR EnsemblPlants; AT3G60330.2; AT3G60330.2; AT3G60330.
DR GeneID; 825204; -.
DR Gramene; AT3G60330.1; AT3G60330.1; AT3G60330.
DR Gramene; AT3G60330.2; AT3G60330.2; AT3G60330.
DR KEGG; ath:AT3G60330; -.
DR Araport; AT3G60330; -.
DR TAIR; locus:2081932; AT3G60330.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; Q9LY32; -.
DR OMA; YCIGVEI; -.
DR OrthoDB; 188115at2759; -.
DR PhylomeDB; Q9LY32; -.
DR BioCyc; ARA:AT3G60330-MON; -.
DR PRO; PR:Q9LY32; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY32; baseline and differential.
DR Genevisible; Q9LY32; AT.
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 3: Inferred from homology;
KW ATP-binding; Hydrogen ion transport; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..961
FT /note="ATPase 7, plasma membrane-type"
FT /id="PRO_0000046280"
FT TOPO_DOM 1..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..294
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..665
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666..670
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..693
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..764
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..785
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 786..797
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 798..818
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 819..826
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..961
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 959..961
FT /note="Interaction with 14-3-3 proteins"
FT /evidence="ECO:0000250"
FT ACT_SITE 332
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 MOD_RES 894
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20649"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 942
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 960
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20649"
SQ SEQUENCE 961 AA; 105520 MW; BF8F9C5BC234A4F8 CRC64;
MTDIEALKAI TTESIDLENV PVEEVFQHLK CTKEGLTSNE VQERLTLFGY NKLEEKKESK
ILKFLGFMWN PLSWVMEAAA LMAIGLAHGG GKPADYHDFV GIVVLLLINS TISFVEENNA
GNAAAALMAQ LAPKAKAVRD GKWNEIDAAE LVPGDIVSIK LGDIIPADAR LLEGDPLKID
QATLTGESLP VTKNPGASVY SGSTCKQGEI EAVVIATGVH TFFGKAAHLV DSTTHVGHFQ
KVLTAIGNFC ICSIAVGMAI EIVVIYGLQK RGYRVGIDNL LVLLIGGIPI AMPTVLSVTM
AIGAHRLAQQ GAITKRMTAI EEMAGMDVLC SDKTGTLTLN KLSVDKNLIE VFKRGIDRDM
AVLMAARAAR LENQDAIDTA IVSMLSDPKE ARAGIKELHF LPFSPANRRT ALTYLDGEGK
MHRVSKGAPE EILDMAHNKL EIKEKVHATI DKFAERGLRS LGLAYQEVPD GDVKGEGGPW
DFVALLPLFD PPRHDSAQTI ERALHLGVSV KMITGDQLAI AKETGRRLGM GTNMYPSSSL
LSDNNTEGVS VDELIENADG FAGVFPEHKY EIVKRLQSRK HICGMTGDGV NDAPALKKAD
IGIAVDDATD AARGASDIVL TEPGLSVIIS AVLTSRAIFQ RMKNYTIYAV SITIRIVMGF
MLLCVFWEFD FPPFMVLVIA ILNDGTIMTI SKDRVKPSPT PDCWKLKEIF ATGVVLGAYL
AIMTVVFFWA AYETNFFHNI FHVRNFNQHH FKMKDKKVAA HLNEQMASAV YLQVSTISQA
LIFVTRSRSW SFVERPGFLL VIAFLIAQLV ASVISAMANW PFAGIRSIGW GWTGVIWIFN
IVTYMLLDPI KFLVRYALSG KSWDRMVEGR TALTGKKNFG QEERMAAWAT EKRTQHGLET
GQKPVYERNS ATELNNMAEE AKRRAEIARM RELQTLKGKV ESAAKLKGYD LEDPNSNNYT
I
