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Database: UniProt
Entry: PMA6_ARATH
LinkDB: PMA6_ARATH
Original site: PMA6_ARATH 
ID   PMA6_ARATH              Reviewed;         949 AA.
AC   Q9SH76; Q84WR5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=ATPase 6, plasma membrane-type;
DE            EC=7.1.2.1;
DE   AltName: Full=Proton pump 6;
GN   Name=AHA6; OrderedLocusNames=At2g07560; ORFNames=F9A16.7;
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.
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] OF 616-949.
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   [4]
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.
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}.
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DR   EMBL; AC007662; AAD32758.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06056.1; -; Genomic_DNA.
DR   EMBL; BT002855; AAO22672.1; -; mRNA.
DR   PIR; G84486; G84486.
DR   RefSeq; NP_178762.1; NM_126721.3.
DR   AlphaFoldDB; Q9SH76; -.
DR   SMR; Q9SH76; -.
DR   BioGRID; 719; 2.
DR   IntAct; Q9SH76; 1.
DR   STRING; 3702.Q9SH76; -.
DR   TCDB; 3.A.3.3.8; the p-type atpase (p-atpase) superfamily.
DR   iPTMnet; Q9SH76; -.
DR   PaxDb; 3702-AT2G07560-1; -.
DR   ProteomicsDB; 226278; -.
DR   EnsemblPlants; AT2G07560.1; AT2G07560.1; AT2G07560.
DR   GeneID; 815329; -.
DR   Gramene; AT2G07560.1; AT2G07560.1; AT2G07560.
DR   KEGG; ath:AT2G07560; -.
DR   Araport; AT2G07560; -.
DR   TAIR; AT2G07560; HA6.
DR   eggNOG; KOG0205; Eukaryota.
DR   HOGENOM; CLU_002360_6_4_1; -.
DR   InParanoid; Q9SH76; -.
DR   OMA; IELCNMG; -.
DR   OrthoDB; 46741at2759; -.
DR   PhylomeDB; Q9SH76; -.
DR   BioCyc; ARA:AT2G07560-MONOMER; -.
DR   PRO; PR:Q9SH76; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SH76; baseline and differential.
DR   Genevisible; Q9SH76; AT.
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: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:SF147; ATPASE 6, PLASMA MEMBRANE-TYPE; 1.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 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   ATP-binding; Hydrogen ion transport; Ion transport; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..949
FT                   /note="ATPase 6, plasma membrane-type"
FT                   /id="PRO_0000046279"
FT   TOPO_DOM        1..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..84
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..96
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..246
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        268..276
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..294
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..645
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        646..667
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        668..672
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        673..695
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        696..711
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        712..732
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        733..753
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        754..774
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        775..786
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        787..807
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        808..815
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        816..836
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        837..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        332
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         590
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         594
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         883
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P20431"
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"
SQ   SEQUENCE   949 AA;  105012 MW;  25C076607DB214EF CRC64;
     MAADISWDEI KKENVDLEKI PVDEVFQQLK CSREGLSSEE GRNRLQIFGA NKLEEKVENK
     FLKFLGFMWN PLSWVMEAAA IMAIVLANGG GRPPDWQDFV GITCLLIINS TISFIEENNA
     GNAAAALMAN LAPKTKVLRD GRWGEQEAAI LVPGDLISIK LGDIVPADAR LLEGDPLKID
     QSALTGESLP ATKHQGDEVF SGSTCKQGEI EAVVIATGVH TFFGKAAHLV DSTNNVGHFQ
     KVLTAIGNFC ICSIGIGMLI EIIIMYPIQH RKYRDGIDNL LVLLIGGIPI AMPTVLSVTM
     AIGSHRLSQQ GAITKRMTAI EEMAGMDVLC SDKTGTLTLN KLTVDKNLIE VFSKDVDKDY
     VILLSARASR VENQDAIDTS IVNMLGDPKE ARAGITEVHF LPFNPVEKRT AITYIDTNGE
     WHRCSKGAPE QIIELCDLKG ETKRRAHEII DKFAERGLRS LGVARQRVPE KDKESAGTPW
     EFVGLLPLFD PPRHDSAETI RRALDLGVNV KMITGDQLAI GKETGRRLGM GTNMYPSSSL
     LENKDDTTGG VPVDELIEKA DGFAGVFPEH KYEIVRKLQE RKHIVGMTGD GVNDAPALKK
     ADIGIAVDDA TDAARSASDI VLTEPGLSVI VSAVLTSRAI FQRMKNYTIY AVSITIRIVL
     GFMLVALIWE FDFSPFMVLI IAILNDGTIM TISKDRVKPS PIPDSWKLKE IFATGVVLGT
     YMALVTVVFF WLAHDTTFFS DKFGVRSLQG KDEELIAVLY LQVSIISQAL IFVTRSRSWS
     FVERPGLLLL IAFFVAQLIA TLIATYAHWE FARIKGCGWG WCGVIWIYSI VTYIPLDILK
     FITRYTLSGK AWNNMIENRT AFTTKKDYGR GEREAQWALA QRTLHGLKPP ESMFEDTATY
     TELSEIAEQA KKRAEVARLR EVHTLKGHVE SVVKLKGLDI DNLNQHYTV
//
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