ID A5C9X8_VITVI Unreviewed; 954 AA.
AC A5C9X8;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=VITISV_014422 {ECO:0000313|EMBL:CAN64375.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CAN64375.1};
RN [1] {ECO:0000313|EMBL:CAN64375.1}
RP NUCLEOTIDE SEQUENCE.
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT vinifera L.): coping with a highly heterozygous genome.";
RL PLoS ONE 2:e1326-e1326(2007).
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; AM487422; CAN64375.1; -; Genomic_DNA.
DR ExpressionAtlas; A5C9X8; 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; 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:SF124; ATPASE 2, 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; 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|ARBA:ARBA00022781,
KW 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 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..672
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 715..736
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 756..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..846
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; 105163 MW; AB9951AA9FB5EDD8 CRC64;
MGGDKSISLE EIKNETVDLE KIPIEEVFEQ LKCTKEGLTS QEGEARLQIF GPNKLEEKKE
SKFLKFLGFM WNPLSWVMEA AALMAIVLAN GDGQPPDWQD FVGIVCLLVI NSTISFIEEN
NAGNAAAALM AGLAPKTKVL RDGRWSEQDA AILVPGDIIS IKLGDIIPAD ARLLEGDPLK
VDQSALTGES LPVTKHPSDE VFSGSTCKQG EIEAVVIATG VHTFFGKAAH LVDSTNQVGH
FQKVLTAIGN FCICSIAVGM LVEIIVMYPI QHRKYRDGID NLLVLLIGGI PIAMPTVLSV
TMAIGSHRLS QQGAITKRMT AIEEMAGMDV LCSDKTGTLT LNKLSVDRNL VEVFAKGVDK
EHVLLLAARA SRTENQDAID AAIVGMLADP KEARAGIREV HFLPFNPVDK RTALTYIDAD
GKWHRASKGA PEQILDLCKC KEDVKKKAHS IIDKFAERGL RSLAVGRQEV PEKSKESLGS
PWQFVGLLPL FDPPRHDSAE TIRRALNLGV NVKMITGDQL AIAKETGRRL GMGTNMYPSA
SLLGQDKDAS IAALPVEELI EKADGFAGVF PEHKYEIVKK LQERKHICGM TGDGVNDAPA
LKKADIGIAV ADATDAARGA SDIVLTEPGL SVIISAVLTS RAIFQRMKNY TIYAVSITIR
IVFGFLFIAL IWKFDFSPFM VLIIAILNDG TIMTISKDRV KPSPLPDSWK LREIFATGVV
LGGYLALMTV IFFWVMKDTD FFPDKFGVKS IRDSPHEMMA ALYLQVSVVS QALIFVTRSR
SWSFVERPGL LLVTAFIIAQ LVATLIAVYA NWGFARIKGM GWGWAGVVWI YSVVFYVPLD
FIKFFIRYIL SGKAWLNLLE NKTAFTTKKD YGKEEREAQW ALAQRTLHGL QPPETSNLFX
DKNSYRELSE IAEQAKRRAE VARLRELHTL KGHVESVVKL KGLDIDTIQQ HYTV
//