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Database: UniProt
Entry: F4HU00_ARATH
LinkDB: F4HU00_ARATH
Original site: F4HU00_ARATH 
ID   F4HU00_ARATH            Unreviewed;       825 AA.
AC   F4HU00;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 2.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE            EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN   Name=HA9 {ECO:0000313|EMBL:AEE36434.2, ECO:0000313|TAIR:AT1G80660};
GN   Synonyms=AHA9 {ECO:0000313|EMBL:AEE36434.2}, H(+)-ATPase 9
GN   {ECO:0000313|EMBL:AEE36434.2};
GN   OrderedLocusNames=At1g80660 {ECO:0000313|Araport:AT1G80660,
GN   ECO:0000313|EMBL:AEE36434.2};
GN   ORFNames=F23A5.1 {ECO:0000313|EMBL:AEE36434.2}, F23A5_1
GN   {ECO:0000313|EMBL:AEE36434.2};
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 {ECO:0000313|EMBL:AEE36434.2, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:AEE36434.2, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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., 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., 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   [2] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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   -!- 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         Evidence={ECO:0000256|ARBA:ARBA00001250,
CC         ECO:0000256|RuleBase:RU362083};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362083};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU362083}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIA subfamily. {ECO:0000256|ARBA:ARBA00008804,
CC       ECO:0000256|RuleBase:RU362083}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362083}.
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DR   EMBL; CP002684; AEE36434.2; -; Genomic_DNA.
DR   RefSeq; NP_001319430.1; NM_001334999.1.
DR   AlphaFoldDB; F4HU00; -.
DR   SMR; F4HU00; -.
DR   EnsemblPlants; AT1G80660.2; AT1G80660.2; AT1G80660.
DR   GeneID; 844405; -.
DR   Gramene; AT1G80660.2; AT1G80660.2; AT1G80660.
DR   Araport; AT1G80660; -.
DR   TAIR; AT1G80660; HA9.
DR   HOGENOM; CLU_002360_6_4_1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4HU00; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
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; 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:SF145; ATPASE 9, PLASMA MEMBRANE-TYPE; 1.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 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   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|RuleBase:RU362083};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
KW   Ion transport {ECO:0000256|RuleBase:RU362083};
KW   Magnesium {ECO:0000256|RuleBase:RU362083};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362083};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362083};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F4HU00,
KW   ECO:0007829|ProteomicsDB:F4HU00};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362083};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362083};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362083}; Transport {ECO:0000256|RuleBase:RU362083}.
FT   TRANSMEM        115..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        153..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        521..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        586..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        660..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        693..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
SQ   SEQUENCE   825 AA;  90978 MW;  8FD50A77CED00880 CRC64;
     MAGLAPKTKV LRDGKWSEQE AAILVPGDII SIKLGDIVPA DGRLLDGDPL KIDQSALTGE
     SLPVTKHPGQ EVYSGSTCKQ GELEAVVIAT GVHTFFGKAA HLVDSTNQEG HFQKVLTAIG
     NFCICSIAIG MLIEIVVMYP IQKRAYRDGI DNLLVLLIGG IPIAMPTVLS VTMAIGSHRL
     SQQGAITKRM TAIEEMAGMD VLCSDKTGTL TLNKLTVDKS MVEVFVKDLD KDQLLVNAAR
     ASRVENQDAI DACIVGMLGD PREAREGITE VHFFPFNPVD KRTAITYIDA NGNWHRVSKG
     APEQIIELCN LREDASKRAH DIIDKFADRG LRSLAVGRQT VSEKDKNSPG EPWQFLGLLP
     LFDPPRHDSA ETIRRALDLG VNVKMITGDQ LAIGKETGRR LGMGTNMYPS SALLGQDKDE
     SIASLPVDEL IEKADGFAGV FPEHKYEIVK RLQEMKHICG MTGDGVNDAP ALKRADIGIA
     VADATDAARS ASDIVLTEPG LSVIVSAVLT SRAIFQRMKN YTIYAVSITI RIVMGFMLLA
     LIWKFDFSPF MVLIVAILND GTIMTISKDR VKPSPLPDSW KLKEIFATGV VLGTYLAVMT
     VVFFWAAEST DFFSAKFGVR SISGNPHELT AAVYLQVSIV SQALIFVTRS RSWSYVERPG
     FWLISAFFMA QLIATLIAVY ANWNFARIRG IGWGWAGVIW LYSIVFYIPL DILKFIIRYS
     LSGRAWDNVI ENKTAFTSKK DYGKGEREAQ WAQAQRTLHG LQPAQTSDMF NDKSTYRELS
     EIADQAKRRA EVARLRERHT LKGHVESVVK QKGLDIEAIQ QHYTL
//
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