PMA11_ARATH
ID PMA11_ARATH Reviewed; 956 AA.
AC Q9LV11;
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 11, plasma membrane-type;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 11;
GN Name=AHA11; OrderedLocusNames=At5g62670; ORFNames=MRG21.9;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-889, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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-955. 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; AB020751; BAA97214.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97641.1; -; Genomic_DNA.
DR EMBL; AY125493; AAM78085.1; -; mRNA.
DR RefSeq; NP_201073.1; NM_125662.4.
DR AlphaFoldDB; Q9LV11; -.
DR SMR; Q9LV11; -.
DR BioGRID; 21631; 6.
DR STRING; 3702.AT5G62670.1; -.
DR iPTMnet; Q9LV11; -.
DR PaxDb; Q9LV11; -.
DR PRIDE; Q9LV11; -.
DR ProteomicsDB; 226182; -.
DR EnsemblPlants; AT5G62670.1; AT5G62670.1; AT5G62670.
DR GeneID; 836388; -.
DR Gramene; AT5G62670.1; AT5G62670.1; AT5G62670.
DR KEGG; ath:AT5G62670; -.
DR Araport; AT5G62670; -.
DR TAIR; locus:2172244; AT5G62670.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; Q9LV11; -.
DR OMA; GVDINWM; -.
DR OrthoDB; 188115at2759; -.
DR PhylomeDB; Q9LV11; -.
DR BioCyc; ARA:AT5G62670-MON; -.
DR PRO; PR:Q9LV11; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LV11; baseline and differential.
DR Genevisible; Q9LV11; 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:0003729; F:mRNA binding; IDA:TAIR.
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 1: Evidence at protein level;
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..956
FT /note="ATPase 11, plasma membrane-type"
FT /id="PRO_0000046284"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..85
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..295
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..669
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..674
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..697
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..759
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..792
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 793..813
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 814..821
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 843..956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 954..956
FT /note="Interaction with 14-3-3 proteins"
FT /evidence="ECO:0000250"
FT ACT_SITE 333
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 596
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 889
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 955
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20649"
SQ SEQUENCE 956 AA; 105123 MW; CA59212B16B9C5BD CRC64;
MGDKEEVLEA VLKETVDLEN VPIEEVFESL RCSREGLTTE AADERLALFG HNKLEEKKES
KFLKFLGFMW NPLSWVMEAA AIMAIALANG GGKPPDWQDF VGIITLLVIN STISFIEENN
AGNAAAALMA RLAPKAKVLR DGRWGEQDAA ILVPGDIISI KLGDIVPADA RLLEGDPLKI
DQSSLTGESL PVTKGPGDGV YSGSTCKQGE LEAVVIATGV HTFFGKAAHL VDTTNHVGHF
QQVLTAIGNF CICSIAVGMI IEIVVMYPIQ HRAYRPGIDN LLVLLIGGIP IAMPTVLSVT
MAIGSHRLSQ QGAITKRMTA IEEMAGMDVL CSDKTGTLTL NKLTVDKNLI EVFTKGVDAD
TVVLMAAQAS RLENQDAIDA AIVGMLADPK EARAGVREVH FLPFNPTDKR TALTYIDSDG
KMHRVSKGAP EQILNLAHNR AEIERRVHAV IDKFAERGLR SLAVAYQEVP EGTKESAGGP
WQFMGLMPLF DPPRHDSAET IRRALNLGVN VKMITGDQLA IGKETGRRLG MGTNMYPSSA
LLGQHKDESI GALPIDDLIE KADGFAGVFP EHKYEIVKRL QARKHICGMT GDGVNDAPAL
KKADIGIAVA DATDAARSAS DIVLTEPGLS VIISAVLTSR AIFQRMKNYT IYAVSITIRI
VLGFMLLALI WKFDFPPFMV LIIAILNDGT IMTISKDRVK PSPLPDSWKL SEIFATGVVF
GSYMAMMTVI FFWAAYKTDF FPRTFGVSTL EKTAHDDFRK LASAIYLQVS IISQALIFVT
RSRSWSYVER PGMLLVVAFI LAQLVATLIA VYANWSFAAI EGIGWGWAGV IWLYNIVFYI
PLDIIKFLIR YALSGRAWDL VIEQRVAFTR QKDFGKEQRE LQWAHAQRTL HGLQAPDAKM
FPERTHFNEL SQMAEEAKRR AEIARLRELH TLKGHVESVV RLKGLDIETI QQAYTV
