PMA9_ARATH
ID PMA9_ARATH Reviewed; 954 AA.
AC Q42556; Q9M8N3; Q9SAJ1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=ATPase 9, plasma membrane-type;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 9;
GN Name=AHA9; OrderedLocusNames=At1g80660; ORFNames=F23A5.1, T21F11.1;
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=8180619; DOI=10.1111/j.1365-313x.1994.00311.x;
RA Houlne G., Boutry M.;
RT "Identification of an Arabidopsis thaliana gene encoding a plasma membrane
RT H(+)-ATPase whose expression is restricted to anther tissue.";
RL Plant J. 5:311-317(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Goodman H.M., Gallant P., Keifer-Higgins S., Rubenfield M., Church G.M.;
RT "A 37.5 Kb sequence from Arabidopsis thaliana chromosome I.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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).
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-953. Binding to 14-3-3 proteins activates the
CC H(+)-ATPase (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q42556-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Anther specific.
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=AAA98916.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X73676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U53501; AAA98916.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011713; AAF14653.1; -; Genomic_DNA.
DR EMBL; AC018849; AAF27113.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36433.1; -; Genomic_DNA.
DR PIR; H96838; H96838.
DR PIR; S60301; S60301.
DR RefSeq; NP_178181.1; NM_106714.2. [Q42556-1]
DR AlphaFoldDB; Q42556; -.
DR SMR; Q42556; -.
DR BioGRID; 29623; 2.
DR STRING; 3702.AT1G80660.1; -.
DR iPTMnet; Q42556; -.
DR PaxDb; Q42556; -.
DR PRIDE; Q42556; -.
DR EnsemblPlants; AT1G80660.1; AT1G80660.1; AT1G80660. [Q42556-1]
DR GeneID; 844405; -.
DR Gramene; AT1G80660.1; AT1G80660.1; AT1G80660. [Q42556-1]
DR KEGG; ath:AT1G80660; -.
DR Araport; AT1G80660; -.
DR TAIR; locus:2025727; AT1G80660.
DR eggNOG; KOG0205; Eukaryota.
DR InParanoid; Q42556; -.
DR PhylomeDB; Q42556; -.
DR BioCyc; ARA:AT1G80660-MON; -.
DR PRO; PR:Q42556; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42556; baseline and differential.
DR Genevisible; Q42556; AT.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; ISS: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; 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 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 Alternative splicing; ATP-binding; 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..954
FT /note="ATPase 9, plasma membrane-type"
FT /id="PRO_0000046282"
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..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..296
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..670
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..675
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..698
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 699..714
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..756
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 757..777
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 778..789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..818
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..839
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 840..954
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 952..954
FT /note="Interaction with 14-3-3 proteins"
FT /evidence="ECO:0000250"
FT ACT_SITE 334
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 593
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 886
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20649"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 953
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20649"
SQ SEQUENCE 954 AA; 105208 MW; 34DFCB96F45E5F18 CRC64;
MAGNKDSSWD DIKNEGIDLE KIPIEEVLTQ LRCTREGLTS DEGQTRLEIF GPNKLEEKKE
NKVLKFLGFM WNPLSWVMEL AAIMAIALAN GGGRPPDWQD FVGITVLLII NSTISFIEEN
NAGNAAAALM AGLAPKTKVL RDGKWSEQEA AILVPGDIIS IKLGDIVPAD GRLLDGDPLK
IDQSALTGES LPVTKHPGQE VYSGSTCKQG ELEAVVIATG VHTFFGKAAH LVDSTNQEGH
FQKVLTAIGN FCICSIAIGM LIEIVVMYPI QKRAYRDGID NLLVLLIGGI PIAMPTVLSV
TMAIGSHRLS QQGAITKRMT AIEEMAGMDV LCSDKTGTLT LNKLTVDKSM VEVFVKDLDK
DQLLVNAARA SRVENQDAID ACIVGMLGDP REAREGITEV HFFPFNPVDK RTAITYIDAN
GNWHRVSKGA PEQIIELCNL REDASKRAHD IIDKFADRGL RSLAVGRQTV SEKDKNSPGE
PWQFLGLLPL FDPPRHDSAE TIRRALDLGV NVKMITGDQL AIGKETGRRL GMGTNMYPSS
ALLGQDKDES IASLPVDELI EKADGFAGVF PEHKYEIVKR LQEMKHICGM TGDGVNDAPA
LKRADIGIAV ADATDAARSA SDIVLTEPGL SVIVSAVLTS RAIFQRMKNY TIYAVSITIR
IVMGFMLLAL IWKFDFSPFM VLIVAILNDG TIMTISKDRV KPSPLPDSWK LKEIFATGVV
LGTYLAVMTV VFFWAAESTD FFSAKFGVRS ISGNPHELTA AVYLQVSIVS QALIFVTRSR
SWSYVERPGF WLISAFFMAQ LIATLIAVYA NWNFARIRGI GWGWAGVIWL YSIVFYIPLD
ILKFIIRYSL SGRAWDNVIE NKTAFTSKKD YGKGEREAQW AQAQRTLHGL QPAQTSDMFN
DKSTYRELSE IADQAKRRAE VARLRERHTL KGHVESVVKQ KGLDIEAIQQ HYTL
