PMA3_ARATH
ID PMA3_ARATH Reviewed; 949 AA.
AC P20431;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=ATPase 3, plasma membrane-type;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 3;
GN Name=AHA3; OrderedLocusNames=At5g57350; ORFNames=MJB24.16;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2524481; DOI=10.1016/s0021-9258(18)81827-0;
RA Pardo J.M., Serrano R.;
RT "Structure of a plasma membrane H+-ATPase gene from the plant Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 264:8557-8562(1989).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC STRAIN=cv. Columbia;
RX PubMed=1844877; DOI=10.1111/j.1365-313x.1991.00121.x;
RA Dewitt N.D., Harper J.F., Sussman M.R.;
RT "Evidence for a plasma membrane proton pump in phloem cells of higher
RT plants.";
RL Plant J. 1:121-128(1991).
RN [7]
RP PHOSPHORYLATION AT THR-948, INTERACTION WITH 14-3-3 PROTEINS, AND
RP MUTAGENESIS OF TYR-947; THR-948 AND VAL-949.
RX PubMed=10593986; DOI=10.1074/jbc.274.51.36774;
RA Fuglsang A.T., Visconti S., Drumm K., Jahn T., Stensballe A., Mattei B.,
RA Jensen O.N., Aducci P., Palmgren M.G.;
RT "Binding of 14-3-3 protein to the plasma membrane H(+)-ATPase AHA2 involves
RT the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation
RT of Thr(947).";
RL J. Biol. Chem. 274:36774-36780(1999).
RN [8]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-882, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-882, 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.
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-948. Binding to 14-3-3 proteins activates the
CC H(+)-ATPase.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15308754};
CC Multi-pass membrane protein {ECO:0000305|PubMed:15308754}.
CC -!- TISSUE SPECIFICITY: Found predominantly in phloem cells of leaves,
CC stems, roots and flowers.
CC -!- PTM: Phosphorylation level varies significantly during early response
CC to bacterial elicitor (e.g. fusicoccin FC).
CC {ECO:0000269|PubMed:10593986}.
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; J04737; AAA32750.1; -; Genomic_DNA.
DR EMBL; AB019233; BAB09963.1; -; Genomic_DNA.
DR EMBL; AB016891; BAB09963.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED96889.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96890.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69534.1; -; Genomic_DNA.
DR EMBL; AY072153; AAL59975.1; -; mRNA.
DR EMBL; X60115; CAA42714.1; -; Genomic_DNA.
DR PIR; A33698; PXMUP3.
DR RefSeq; NP_001190559.1; NM_001203630.1.
DR RefSeq; NP_001331204.1; NM_001345259.1.
DR RefSeq; NP_200545.1; NM_125118.3.
DR AlphaFoldDB; P20431; -.
DR SMR; P20431; -.
DR BioGRID; 21085; 5.
DR STRING; 3702.AT5G57350.1; -.
DR iPTMnet; P20431; -.
DR PaxDb; P20431; -.
DR PRIDE; P20431; -.
DR ProteomicsDB; 234981; -.
DR EnsemblPlants; AT5G57350.1; AT5G57350.1; AT5G57350.
DR EnsemblPlants; AT5G57350.2; AT5G57350.2; AT5G57350.
DR EnsemblPlants; AT5G57350.4; AT5G57350.4; AT5G57350.
DR GeneID; 835841; -.
DR Gramene; AT5G57350.1; AT5G57350.1; AT5G57350.
DR Gramene; AT5G57350.2; AT5G57350.2; AT5G57350.
DR Gramene; AT5G57350.4; AT5G57350.4; AT5G57350.
DR KEGG; ath:AT5G57350; -.
DR Araport; AT5G57350; -.
DR TAIR; locus:2165600; AT5G57350.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; P20431; -.
DR OMA; HKDENMA; -.
DR OrthoDB; 188115at2759; -.
DR PhylomeDB; P20431; -.
DR BioCyc; ARA:AT5G57350-MON; -.
DR PRO; PR:P20431; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P20431; baseline and differential.
DR Genevisible; P20431; AT.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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; 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..949
FT /note="ATPase 3, plasma membrane-type"
FT /id="PRO_0000046276"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..82
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..94
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..292
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..644
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..666
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..671
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..694
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 695..710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 711..731
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..752
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..773
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 774..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..806
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 807..814
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 815..835
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 836..949
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 947..949
FT /note="Interaction with 14-3-3 proteins"
FT ACT_SITE 330
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 589
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 593
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 882
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 948
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10593986"
FT MUTAGEN 947
FT /note="Y->A: Impaired fusicoccin- (FC) dependent activation
FT by 14-3-3 protein."
FT /evidence="ECO:0000269|PubMed:10593986"
FT MUTAGEN 948
FT /note="T->A: Impaired fusicoccin- (FC) dependent activation
FT by 14-3-3 protein."
FT /evidence="ECO:0000269|PubMed:10593986"
FT MUTAGEN 949
FT /note="V->A: Impaired fusicoccin- (FC) dependent activation
FT by 14-3-3 protein."
FT /evidence="ECO:0000269|PubMed:10593986"
SQ SEQUENCE 949 AA; 104450 MW; 3F88C87D849A4001 CRC64;
MASGLEDIVN ENVDLEKIPI EEVFQQLKCS REGLSGAEGE NRLQIFGPNK LEEKKESKLL
KFLGFMWNPL SWVMEAAAIM AIALANGGGK PPDWQDFVGI VCLLVINSTI SFVEENNAGN
AAAALMAGLA PKTKVLRDGK WSEQEASILV PGDIVSIKLG DIIPADARLL EGDPLKVDQS
ALTGESLPAT KGPGEEVFSG STCKQGEIEA VVIATGVHTF FGKAAHLVDS TNQVGHFQKV
LTAIGNFCIC SIAVGIAIEI VVMYPIQRRH YRDGIDNLLV LLIGGIPIAM PTVLSVTMAI
GSHKLSQQGA ITKRMTAIEE MAGMDVLCSD KTGTLTLNKL SVDKNLIEVY CKGVEKDEVL
LFAARASRVE NQDAIDAAMV GMLADPKEAR AGIREIHFLP FNPVDKRTAL TFIDSNGNWH
RVSKGAPEQI LDLCNARADL RKRVHSTIDK YAERGLRSLA VSRQTVPEKT KESSGSPWEF
VGVLPLFDPP RHDSAETIRR ALDLGVNVKM ITGDQLAIAK ETGRRLGMGS NMYPSSSLLG
KHKDEAMAHI PVEDLIEKAD GFAGVFPEHK YEIVKKLQER KHICGMTGDG VNDAPALKKA
DIGIAVADAT DAARGASDIV LTEPGLSVII SAVLTSRAIF QRMKNYTIYA VSITIRIVFG
FMLIALIWKF DFSPFMVLII AILNDGTIMT ISKDRVKPSP TPDSWKLKEI FATGVVLGGY
MAIMTVVFFW AAYKTDFFPR TFHVRDLRGS EHEMMSALYL QVSIVSQALI FVTRSRSWSF
TERPGYFLLI AFWVAQLIAT AIAVYGNWEF ARIKGIGWGW AGVIWLYSIV FYFPLDIMKF
AIRYILAGTA WKNIIDNRTA FTTKQNYGIE EREAQWAHAQ RTLHGLQNTE TANVVPERGG
YRELSEIANQ AKRRAEIARL RELHTLKGHV ESVVKLKGLD IETAGHYTV
