PMAX_ARATH
ID PMAX_ARATH Reviewed; 813 AA.
AC Q9T0E0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Putative ATPase, plasma membrane-like;
GN OrderedLocusNames=At4g11730; ORFNames=T5C23.160;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000305}.
CC -!- CAUTION: This protein is not an active H(+)-ATPase in its current form
CC as there is a deletion in a conserved domain crucial for P-type ATPase
CC function. {ECO:0000305}.
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DR EMBL; AL049500; CAB39944.1; -; Genomic_DNA.
DR EMBL; AL161532; CAB78216.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83042.1; -; Genomic_DNA.
DR PIR; T04220; T04220.
DR RefSeq; NP_192910.1; NM_117242.1.
DR AlphaFoldDB; Q9T0E0; -.
DR SMR; Q9T0E0; -.
DR STRING; 3702.AT4G11730.1; -.
DR PaxDb; Q9T0E0; -.
DR PRIDE; Q9T0E0; -.
DR EnsemblPlants; AT4G11730.1; AT4G11730.1; AT4G11730.
DR GeneID; 826778; -.
DR Gramene; AT4G11730.1; AT4G11730.1; AT4G11730.
DR KEGG; ath:AT4G11730; -.
DR Araport; AT4G11730; -.
DR TAIR; locus:2139782; AT4G11730.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; Q9T0E0; -.
DR OrthoDB; 1340643at2759; -.
DR PhylomeDB; Q9T0E0; -.
DR BioCyc; ARA:AT4G11730-MON; -.
DR PRO; PR:Q9T0E0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T0E0; baseline and differential.
DR Genevisible; Q9T0E0; 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:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 2.
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; IPR001757; P_typ_ATPase.
DR Pfam; PF00690; Cation_ATPase_N; 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; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..813
FT /note="Putative ATPase, plasma membrane-like"
FT /id="PRO_0000046285"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..86
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..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..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..293
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..577
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..582
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..605
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..664
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 665..685
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 686..697
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..726
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 727..747
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 748..813
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 331
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000255"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 504
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
SQ SEQUENCE 813 AA; 90439 MW; 30EB9D1CB01B92B9 CRC64;
MATGDSLEDI KIEIDDDLEK IPIEEVFKKL RCSREGLSGA EGKERLKIFG PNKLENKKKE
HITLRFFALM FKPLSWVIQA AAIMAMLFAN GDGRQLFLGI VCLLIVNTII CYLKEDDAAN
VVAMARAGLS PKTKVLRDGK WSEQEASILV PGDIVSIKPG DIIPCDARLL EGDTLKVDQS
ALTGEFGPIT KGPGEEVFSG TTCKQGEMEA VVIATGVHTF SGTTAHLVDN RTNKVGHFRK
VVTEIENLCV ISIAIGISIE VIVMYWIQRR NFSDVINNLL VLVIGGIPLA MPTVLYVIMV
TGSLRLYRTG TITQRITAIE DMAAIDVLCS DKTGTLTLNK LSVDKNLIKV YSKDVEKEQV
LLLAARASRI ENRDGIDAAM VGSLADPKEA RAGIREVHFN LVDKRTALTY IDGNGDWHRV
SKGTPEQILD LCNARDDLRK SVHSAIRNYA ERGLKSFAIS WFRNTNCNTV FFFPYQLCSE
HKYHIVNKLQ ERHICGLIGD GVDDVPSLKK ADVGIAVANA TEAARAASDI VLTEPGLSVI
IDAVLASRAI LQQMKHYTIY AVSITIRVVF GFMFIALIWK FDFSPFMVLA IALLNEETTK
AITMDNVTNP SPTPDSLKLK EIFATGVVYG SYMALITVVF FWAAYRTDIF PRTFHVRDLR
GNEAEMMCAL YLQVSIMSQA LFFVIQSRSW FFVERPGELL FLSFVTVQTI ATTLAVYASW
ETARIEGIGW SWAGVIWLYN IIFFFPLDIM KFGIRYILTG KAQSLFDNMV HLVLNSYAKL
SNGIYNHTQA DHTYSLLEVS TPPSQDLRGV GWV
