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Database: UniProt
Entry: A0A2I4HDZ0_JUGRE
LinkDB: A0A2I4HDZ0_JUGRE
Original site: A0A2I4HDZ0_JUGRE 
ID   A0A2I4HDZ0_JUGRE        Unreviewed;       954 AA.
AC   A0A2I4HDZ0;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE            EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN   Name=LOC109016418 {ECO:0000313|RefSeq:XP_018845641.1};
GN   ORFNames=F2P56_026057 {ECO:0000313|EMBL:KAF5456590.1}, F2P56_026058
GN   {ECO:0000313|EMBL:KAF5456591.1};
OS   Juglans regia (English walnut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Juglandaceae; Juglans.
OX   NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018845641.1};
RN   [1] {ECO:0000313|EMBL:KAF5456590.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5456590.1};
RA   Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA   Stevens K., Paul R., Butterfield T., Britton M., Reagan R., Chakraborty S.,
RA   Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R., Pratt K.,
RA   Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M., Salzberg S.L.,
RA   Wegrzyn J.L., Langley C.H., Neale D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAF5456590.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5456590.1};
RA   Marrano A., Britton M., Zimin A.V., Zaini P.A., Workman R., Puiu D.,
RA   Bianco L., Allen B.J., Troggio M., Leslie C.A., Timp W., Dendekar A.,
RA   Salzberg S.L., Neale D.B.;
RT   "Walnut 2.0.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:XP_018845641.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaves {ECO:0000313|RefSeq:XP_018845641.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   EMBL; LIHL02000011; KAF5456590.1; -; Genomic_DNA.
DR   EMBL; LIHL02000011; KAF5456591.1; -; Genomic_DNA.
DR   RefSeq; XP_018845641.1; XM_018990096.2.
DR   RefSeq; XP_018854375.1; XM_018998830.1.
DR   STRING; 51240.A0A2I4HDZ0; -.
DR   EnsemblPlants; Jr11_27970_p1; cds.Jr11_27970_p1; Jr11_27970.
DR   EnsemblPlants; Jr11_27980_p1; cds.Jr11_27980_p1; Jr11_27980.
DR   GeneID; 109016418; -.
DR   Gramene; Jr11_27970_p1; cds.Jr11_27970_p1; Jr11_27970.
DR   Gramene; Jr11_27980_p1; cds.Jr11_27980_p1; Jr11_27980.
DR   KEGG; jre:109016418; -.
DR   OrthoDB; 46741at2759; -.
DR   Proteomes; UP000235220; Chromosome 11.
DR   Proteomes; UP000619265; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
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; 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; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF31; PLASMA MEMBRANE ATPASE-RELATED; 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; SFLDS00003; Haloacid_Dehalogenase; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362083};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235220};
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        66..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        101..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        244..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        282..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        650..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        676..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        715..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        758..777
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        789..810
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        822..839
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   DOMAIN          18..90
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   954 AA;  105131 MW;  A84EE9D177C249B1 CRC64;
     MASDKGISLE EIKNESVDLE RIPIEEVFEQ LKCSREGLTS EEGANRLQVF GPNKLEEKKE
     SKVLKFLGFM WNPLSWVMEA AAIMAIALAN GGGRPPDWQD FVGIVVLLVI NSTISFIEEN
     NAGNAAAALM AGLAPKTKVL RDGRWSEQDA SILVPGDIIS IKLGDIIPAD ARLLEGDPLK
     IDQSALTGES LPVTKNPSDE VFSGSTCKQG EIEAVVIATG VHTFFGKAAH LVDSTNQVGH
     FQKVLTAIGN FCICSIAVGI AVELIVMYPI QHREYRDGID NLLVLLIGGI PIAMPTVLSV
     TMAIGSHRLS QQGAITKRMT AIEEMAGMDV LCSDKTGTLT LNKLTVDRNL IEVFAKGVEK
     EHVMLLAARA SRTENQDAID AAIVGMLADP KEARAGVKEI HFFPFNPVDK RTALTYIDES
     GNWHRASKGA PEQIINLCNC KEDVRKRVHA VIDKFAERGL RSLAVARQEI PEKTKDSPGA
     PWQFVGLLPL FDPPRHDSAE TIRRALNLGV NVKMITGDQL AIGKETGRRL GMGTNMYPSS
     SLLGQNKDAS IAALPVDELI EKADGFAGVF PEHKYEIVKK LQERKHICGM TGDGVNDAPA
     LKKADIGIAV ADATDAARGA SDIVLTEPGL SVIISAVLTS RAIFQRMKNY TIYAVSITIR
     IVFGFMFIAL IWKFDFAPFM VLIIAILNDG TIMTISKDRV KPSPQPDSWK LKEIFATGIV
     LGGYLALMTV IFFWVMKDTD FFSDKFHVRS LRHNDKEMMA ALYLQVSIIS QALIFVTRSR
     SWSFIERPGL LLLTAFVLAQ LVATFIAVYA DWGFARIKGA GWGWAGVVWL YSIVTYFPLD
     CLKFAIRYIQ SGKAWDNLLE NKTAFTTKKD YGKEEREAQW ATAQRTLHGL QPPETSNVFS
     DKSSYRELSE IAEQAKRRAE VARLRELHTL KGHVESVVKL KGLDIDTIQQ HYTV
//
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