ID PMA5_ARATH Reviewed; 949 AA.
AC Q9SJB3; F4IPQ2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 183.
DE RecName: Full=ATPase 5, plasma membrane-type;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 5;
GN Name=AHA5; OrderedLocusNames=At2g24520; ORFNames=F25P17.18;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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 TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia GL1;
RX PubMed=15821287; DOI=10.1093/pcp/pci104;
RA Ueno K., Kinoshita T., Inoue S., Emi T., Shimazaki K.;
RT "Biochemical characterization of plasma membrane H+-ATPase activation in
RT guard cell protoplasts of Arabidopsis thaliana in response to blue light.";
RL Plant Cell Physiol. 46:955-963(2005).
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-948. Binding to 14-3-3 proteins activates the
CC H(+)-ATPase (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in guard cells and leaves.
CC {ECO:0000269|PubMed:15821287}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD23893.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEC07588.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006954; AAD23893.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07588.1; ALT_SEQ; Genomic_DNA.
DR PIR; F84637; F84637.
DR RefSeq; NP_001318282.1; NM_001335933.1.
DR RefSeq; NP_180028.1; NM_128013.2.
DR AlphaFoldDB; Q9SJB3; -.
DR SMR; Q9SJB3; -.
DR STRING; 3702.Q9SJB3; -.
DR iPTMnet; Q9SJB3; -.
DR PaxDb; 3702-AT2G24520-1; -.
DR PeptideAtlas; Q9SJB3; -.
DR GeneID; 816988; -.
DR KEGG; ath:AT2G24520; -.
DR Araport; AT2G24520; -.
DR TAIR; AT2G24520; HA5.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; Q9SJB3; -.
DR PhylomeDB; Q9SJB3; -.
DR PRO; PR:Q9SJB3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJB3; baseline and differential.
DR Genevisible; Q9SJB3; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR CDD; cd02076; P-type_ATPase_H; 1.
DR Gene3D; 6.10.140.890; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01647; ATPase-IIIA_H; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF31; PLASMA MEMBRANE ATPASE-RELATED; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Hydrogen ion transport; Ion transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT CHAIN 2..949
FT /note="ATPase 5, plasma membrane-type"
FT /id="PRO_0000046278"
FT TOPO_DOM 2..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..81
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..93
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..291
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..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..751
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..805
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 806..813
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..834
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 835..949
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 947..949
FT /note="Interaction with 14-3-3 proteins"
FT /evidence="ECO:0000250"
FT ACT_SITE 329
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 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 881
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20431"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 948
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20431"
FT CONFLICT 1
FT /note="M -> G (in Ref. 1; AAD23893 and 2; AEC07588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 949 AA; 104739 MW; 2D042497CD564C10 CRC64;
MSELDHIKNE SVDLVRIPME EVFEELKCTK QGLTANEASH RLDVFGPNKL EEKKESKLLK
FLGFMWNPLS WVMEVAALMA IALANGGGRP PDWQDFVGIV CLLLINSTIS FIEENNAGNA
AAALMAGLAP KTKVLRDNQW SEQEASILVP GDVISIKLGD IIPADARLLD GDPLKIDQSS
LTGESIPVTK NPSDEVFSGS ICKQGEIEAI VIATGVHTFF GKAAHLVDNT NQIGHFQKVL
TSIGNFCICS IALGIIVELL VMYPIQRRRY RDGIDNLLVL LIGGIPIAMP SVLSVTMATG
SHRLFQQGAI TKRMTAIEEM AGMDVLCCDK TGTLTLNKLT VDKNLVEVFA KGVGKEHVFL
LAARASRIEN QDAIDAAIVG MLADPKEARA GVREVHFFPF NPVDKRTALT YVDSDGNWHR
ASKGAPEQIL NLCNCKEDVR RKVHGVIDKF AERGLRSLAV ARQEVLEKKK DAPGGPWQLV
GLLPLFDPPR HDSAETIRRA LNLGVNVKMI TGDQLAIGKE TGRRLGMGTN MYPSSALLGQ
VKDSSLGALP VDELIEKADG FAGVFPEHKY EIVHRLQQRN HICGMTGDGV NDAPALKKAD
IGIAVVDATD AARGASDIVL TEPGLSVIIS AVLTSRAIFQ RMKNYTIYAV SITIRIVFGF
MFIALIWQFD FSPFMVLIIA ILNDGTIMTI SKDRMKPSPQ PDSWKLRDIF STGVVLGGYQ
ALMTVVFFWV MKDSDFFSNY FGVRPLSQRP EQMMAALYLQ VSIISQALIF VTRSRSWSYA
ECPGLLLLGA FVIAQLVATF IAVYANWSFA RIEGAGWGWA GVIWLYSFLT YIPLDLLKFG
IRYVLSGKAW LNLLENKTAF TTKKDYGKEE REAQWAAAQR TLHGLQPAEK NNIFNEKNSY
SELSQIAEQA KRRAEVVRLR EINTLKGHVE SVVKLKGLDI DTIQQHYTV
//
