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 03-AUG-2022, entry version 175.
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).
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 -!- 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.AT2G07560.1; -.
DR TCDB; 3.A.3.3.8; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q9SH76; -.
DR PaxDb; Q9SH76; -.
DR PRIDE; Q9SH76; -.
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; locus:2053343; AT2G07560.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; Q9SH76; -.
DR OMA; SAGDPWE; -.
DR OrthoDB; 188115at2759; -.
DR PhylomeDB; Q9SH76; -.
DR BioCyc; ARA:AT2G07560-MON; -.
DR PRO; PR:Q9SH76; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SH76; baseline and differential.
DR Genevisible; Q9SH76; 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: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 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