ID A0A2K2DKX0_BRADI Unreviewed; 856 AA.
AC A0A2K2DKX0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=100837629 {ECO:0000313|EnsemblPlants:PNT74929};
GN ORFNames=BRADI_1g24630v3 {ECO:0000313|EMBL:PNT74929.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:PNT74929.1};
RN [1] {ECO:0000313|EMBL:PNT74929.1, ECO:0000313|EnsemblPlants:PNT74929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT74929.1,
RC ECO:0000313|EnsemblPlants:PNT74929};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:PNT74929.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT74929.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:PNT74929}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:PNT74929};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362033}.
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DR EMBL; CM000880; PNT74929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K2DKX0; -.
DR EnsemblPlants; PNT74929; PNT74929; BRADI_1g24630v3.
DR Gramene; PNT74929; PNT74929; BRADI_1g24630v3.
DR Proteomes; UP000008810; Chromosome 1.
DR ExpressionAtlas; A0A2K2DKX0; baseline.
DR GO; GO:0016020; C: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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF19; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 570..591
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 675..693
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 741..762
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 530..769
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 856 AA; 95821 MW; 3470F2ED3E4659D5 CRC64;
MSRGVPEPKL TAMDAMIDKL TGAIFLFQLA VVVVLGSAGN VWKDTEARKQ WYVKYDDDEP
WYQILVIPLR FELLCSIMIP ISIKVSLDFV KSLYAKFIDW DEEMYDKETD TPAHAANTAI
SEDLGQVEYI LTDKTGTLTE NKMIFRRCCI GGTLYGNESG DALKDVELLN AVANNSPHVI
KFLTVMALCN TVIPIKSPSG QISYKAQSQD EDALVNAASN LHMVLVSKNG NNAEIHFNRR
VVQYEILDVL EFTSDRKRMS VLISDSESGK IFLLSKGADE AILPLAYSGQ QIKTFIDAVD
KYAQLGLRTL CLAWRELGLQ EYLEWSRLFK EANSALIDRE WKVAEVCQKL EHTLDILGIS
AIEDRLQAGV PETIEILRQS GINFWMLTGD KQSTAIQIAL LCNLISSEPK GQLLYINGKT
EDEVARSLER VLLTMRITSS EPKELAFVVD GWALEIILTR YKEAFTELAV LSKTAICCRV
TPSQKAQLVK LLKSCDYRTL AIGDGGNDVR MIQQAHIGVG ISGREGLQAA RAADYSIGKF
RFLKRLILVH GRYSYNRTAF LSQYSFYKSL LICFIQILFS FVSGIAGTSL FNSVSLMAYN
VFYTSIPVLT TVLDKDLSER TVTQNPEILL YCQAGRLLNP STFAGWFGRS LYHAIVVFLI
TIHVYANEKS EMEELSMVAL SGSIWLQAFV VTLEMNSFTF VQFLGIWGNF AAFYIINFGI
SSIPSAGMYT IMFRLCRQPS YWITMLLISG VGMGPVLALK YFRYTYSPSA INILQKAERS
RGPMYTLVNL ESQLRLDNNA TDSISSMPVK KSSVYEPLLS DSPMASRRSV ASSSFDIFQP
AQSRVPASYP RNIKAS
//
