PMA4_ARATH
ID PMA4_ARATH Reviewed; 960 AA.
AC Q9SU58; Q8GXR3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=ATPase 4, plasma membrane-type;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 4;
GN Name=AHA4; OrderedLocusNames=At3g47950; ORFNames=T17F15.180;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP SUBCELLULAR LOCATION.
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).
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-959. Binding to 14-3-3 proteins activates the
CC H(+)-ATPase (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15308754};
CC Multi-pass membrane protein {ECO:0000305|PubMed:15308754}.
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=CAB41144.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049658; CAB41144.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78350.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63639.1; -; Genomic_DNA.
DR EMBL; AK118088; BAC42716.1; -; mRNA.
DR PIR; T06688; T06688.
DR RefSeq; NP_001325714.1; NM_001339341.1.
DR RefSeq; NP_190378.2; NM_114664.4.
DR AlphaFoldDB; Q9SU58; -.
DR SMR; Q9SU58; -.
DR BioGRID; 9270; 4.
DR STRING; 3702.AT3G47950.1; -.
DR iPTMnet; Q9SU58; -.
DR PaxDb; Q9SU58; -.
DR PRIDE; Q9SU58; -.
DR ProteomicsDB; 226184; -.
DR EnsemblPlants; AT3G47950.1; AT3G47950.1; AT3G47950.
DR EnsemblPlants; AT3G47950.2; AT3G47950.2; AT3G47950.
DR GeneID; 823950; -.
DR Gramene; AT3G47950.1; AT3G47950.1; AT3G47950.
DR Gramene; AT3G47950.2; AT3G47950.2; AT3G47950.
DR KEGG; ath:AT3G47950; -.
DR Araport; AT3G47950; -.
DR TAIR; locus:2097895; AT3G47950.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; Q9SU58; -.
DR OMA; NDELICW; -.
DR OrthoDB; 188115at2759; -.
DR PhylomeDB; Q9SU58; -.
DR BioCyc; ARA:AT3G47950-MON; -.
DR PRO; PR:Q9SU58; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SU58; baseline and differential.
DR Genevisible; Q9SU58; 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; ISS:TAIR.
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 GO; GO:0009651; P:response to salt stress; IMP:TAIR.
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 2: Evidence at transcript 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..960
FT /note="ATPase 4, plasma membrane-type"
FT /id="PRO_0000046277"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..89
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..299
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..673
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 674..678
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..701
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 702..717
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 739..763
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 764..784
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 785..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 797..817
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 818..825
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 826..846
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 847..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 958..960
FT /note="Interaction with 14-3-3 proteins"
FT /evidence="ECO:0000250"
FT ACT_SITE 337
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 596
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 600
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 893
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LV11"
FT MOD_RES 942
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 959
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20649"
SQ SEQUENCE 960 AA; 105718 MW; B2E9548A74606E39 CRC64;
MTTTVEDNRE VLEAVLKEAV DLENVPIEEV FENLRCSKEG LTTQAADERL ALFGHNKLEE
KKESKFLKFL GFMWNPLSWV MEAAAIMAIA LANGGGKPPD WQDFVGIITL LVINSTISFI
EENNAGNAAA ALMARLAPKA KVLRDGRWGE QDAAILVPGD IISIKLGDIV PADARLLEGD
PLKIDQSALT GESLPVTKSS GDGVYSGSTC KQGEIEAVVI ATGVHTFFGK AAHLVDTTNQ
IGHFQQVLTA IGNFCICSIA VGMLIEIVVM YPIQHRAYRP GIDNLLVLLI GGIPIAMPTV
LSVTMAIGSH RLSQQGAITK RMTAIEEMAG MDVLCSDKTG TLTLNKLTVD KNLIEVFMKG
VDADTVVLMA ARASRLENQD AIDAAIVGML ADPKDARAGI QEVHFLPFNP TDKRTALTYI
DNEGNTHRVS KGAPEQILNL AHNKSEIERR VHAVIDKFAE RGLRSLAVAY QDVPEGRKDS
AGGPWQFVGL MPLFDPPRHD SAETIRRALN LGVSVKMITG DQLAIGKETG RRLGMGTNMY
PSSALLGQNK DESIVALPVD ELIEKADGFA GVFPEHKYEI VKRLQARKHI CGMTGDGVND
APALKKADIG IAVADATDAA RSASDIVLTE PGLSVIISAV LTSRAIFQRM KNYTIYAVSI
TIRIVLGFML LALIWQFDFP PFMVLIIAIL NDGTIMTISK DRVKPSPLPD SWKLSEIFAT
GVVFGSYMAM MTVIFFWVSY KTDFFPRTFG VATLEKTAHD DFRKLASAIY LQVSIISQAL
IFVTRSRSWS FVERPGIFLM IAFILAQLVA TLIAVYANWS FAAIEGIGWG WAGVIWLYNI
IFYIPLDFIK FFIRYALSGR AWDLVIEQRV AFTRQKDFGK EQRELQWAHA QRTLHGLQAP
DTKMFTDRTH VSELNQMAEE AKRRAEIARL RELHTLKGHV ESVVRLKGLD IETIQQAYTV
