PMA8_ARATH
ID PMA8_ARATH Reviewed; 948 AA.
AC Q9M2A0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=ATPase 8, plasma membrane-type;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 8;
GN Name=AHA8; OrderedLocusNames=At3g42640; ORFNames=T12K4_90;
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-947. 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}.
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DR EMBL; AL138640; CAB86447.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77743.1; -; Genomic_DNA.
DR PIR; T47322; T47322.
DR RefSeq; NP_189850.1; NM_114131.3.
DR AlphaFoldDB; Q9M2A0; -.
DR SMR; Q9M2A0; -.
DR BioGRID; 8606; 20.
DR IntAct; Q9M2A0; 19.
DR STRING; 3702.AT3G42640.1; -.
DR iPTMnet; Q9M2A0; -.
DR PaxDb; Q9M2A0; -.
DR PRIDE; Q9M2A0; -.
DR ProteomicsDB; 234783; -.
DR EnsemblPlants; AT3G42640.1; AT3G42640.1; AT3G42640.
DR GeneID; 823281; -.
DR Gramene; AT3G42640.1; AT3G42640.1; AT3G42640.
DR KEGG; ath:AT3G42640; -.
DR Araport; AT3G42640; -.
DR TAIR; locus:2096549; AT3G42640.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; Q9M2A0; -.
DR OMA; VWTLLQC; -.
DR OrthoDB; 188115at2759; -.
DR PhylomeDB; Q9M2A0; -.
DR BioCyc; ARA:AT3G42640-MON; -.
DR PRO; PR:Q9M2A0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2A0; baseline and differential.
DR Genevisible; Q9M2A0; AT.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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..948
FT /note="ATPase 8, plasma membrane-type"
FT /id="PRO_0000046281"
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..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..668
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..673
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..696
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 697..712
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..733
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 734..754
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..787
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 788..808
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 809..816
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 817..837
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 838..948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 946..948
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 591
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 595
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 884
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20649"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 947
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20649"
SQ SEQUENCE 948 AA; 104131 MW; A45CA0F478F7576B CRC64;
MATEFSWDEI KKENVDLERI PVEEVFEQLK CSKEGLSSDE GAKRLEIFGA NKLEEKSENK
FLKFLGFMWN PLSWVMESAA IMAIVLANGG GKAPDWQDFI GIMVLLIINS TISFIEENNA
GNAAAALMAN LAPKTKVLRD GKWGEQEASI LVPGDLISIK LGDIVPADAR LLEGDPLKID
QSALTGESLP TTKHPGDEVF SGSTCKQGEI EAVVIATGVH TFFGKAAHLV DSTNNVGHFQ
KVLTSIGNFC ICSIGLGMLI EILIMYPIQH RTYRDGIDNL LVLLIGGIPI AMPTVLSVTM
AIGSHRLSQQ GAITKRMTAI EEMAGMDVLC SDKTGTLTLN KLSVDKSLIE VFPKNMDSDS
VVLMAARASR IENQDAIDAS IVGMLGDPKE ARAGITEVHF LPFNPVDKRT AITYIDESGD
WHRSSKGAPE QIIELCNLQG ETKRKAHEVI DGFAERGLRS LGVAQQTVPE KTKESDGSPW
EFVGLLPLFD PPRHDSAETI RRALELGVNV KMITGDQLAI GIETGRRLGM GTNMYPSTSL
LGNSKDESLV GIPIDELIEK ADGFAGVFPE HKYEIVKKLQ ERKHICGMTG DGVNDAPALK
KADIGIAVAD ATDAARSASD IVLTEPGLSV IISAVLTSRA IFQRMKNYTI YAVSITIRIV
LGFMLVALIW RFDFAPFMVL IIAILNDGTI MTISKDRVKP SPVPDSWKLN EIFATGVVLG
TYMALTTVLF FWLAHDTDFF SKTFGVRSIQ GNEEELMAAL YLQVSIISQA LIFVTRSRSW
SFVERPGFLL LIAFVIAQLV ATLIAVYANW GFARIVGCGW GWAGGIWVYS IITYIPLDIL
KFIIRYALTG KAWDNMINQK TAFTTKKDYG KGEREAQWAL AQRTLHGLPP PEAMFNDNKN
ELSEIAEQAK RRAEVARLRE LHTLKGHVES VVKLKGLDID TIQQHYTV
