ID A0A0D3G261_9ORYZ Unreviewed; 1208 AA.
AC A0A0D3G261;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART05G00020.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART05G00020.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART05G00020.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART05G00020.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) 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}.
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DR AlphaFoldDB; A0A0D3G261; -.
DR STRING; 65489.A0A0D3G261; -.
DR PaxDb; 65489-OBART05G00020-1; -.
DR EnsemblPlants; OBART05G00020.1; OBART05G00020.1; OBART05G00020.
DR Gramene; OBART05G00020.1; OBART05G00020.1; OBART05G00020.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR Proteomes; UP000026960; Chromosome 5.
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 CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 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; 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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
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; 2.
DR PANTHER; PTHR24092:SF175; PHOSPHOLIPID-TRANSPORTING ATPASE 9-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
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 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:UP000026960};
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 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 312..334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 363..388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 930..947
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 959..979
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1009..1030
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1042..1061
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1073..1096
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1116..1136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 64..114
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 895..1145
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1187..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 134382 MW; B7FBB90120712355 CRC64;
MMATGGGDGR RRGRRRSKMR LSRLYSFACG RRPTAVDDES SSRIGGPGFT RVVNANGGGG
IPEYGYRSNS VSTTKYNVVT FVPKSLLEQF RRVANIYFLI SACLTYTNLA PYTSASAVAP
LVLVLLATMV KEAIEDWRRK QQDTEVNNRK TKVLQDGAFH STKWMNLQVG DIVKVEKDEF
FPADLILLSS SYEDAICYVE TMNLDGETNL KLKQSLEASS GLQEDDSFNS FRAVIRCEDP
NPHLYSFVGN IEIEEQQYPL SPQQILLRDS KLRNTEYVYG VVIFTGHDTK VMQNAMKAPS
KRSKIERKMD RIIYLLLSAL VLISVIGSVF FGIATRDDLQ DGRPKRWYLR PDDSTIYFKP
TKAAISAILH FFTAMMLYGN FIPISLYISI EIVKLLQALF INQDIHMYHE ETDTPAHART
SNLNEELGQV DTILTDKTGT LTCNSMEFIK CSIAGIAYGR GITEVERAMA KRKGSPLIAD
MASNTQGSQA AIKGFNFTDE RVMNGNWVSQ PHSGVIQMFF RLLAVCHTCI PEVDEESGTI
SYEAESPDEA AFVVAARELG FTFYQRTQTG VFLHELDPSS GKQVDRSYKL LHVLEFNSAR
KRMSVIVRNE EGKIFLFSKG ADSVMFERLS SSDCAYREVT QDHINEYADA GLRTLVLAYR
QLDEAEYANF DRKFTAAKNS VSADRDEMIE EAADLLERKL ILLGATAVED KLQKGVPECI
DKLAQAGIKI WVLTGDKMET AINIGYACSL LRQGMTQITI TLEQPDIIAL EKGGGDKAAV
AKASKENVVK QINEGKKRID GSVVGEAFAL IIDGKSLTYA LEEDAKGALM DLAVGCKSVI
CCRSSPKQKA LVTRLVKEST GKVSLAIGDG ANDVGMIQEA DIGVGISGAE GMQAVMASDV
SIAQFRFLER LLLVHGHWCY SRISAMICYF FYKNITFGVT LFLYEAYTSF SGQTFYNDWA
LSTYNVFFTS LPVIAMGVFD QDVSARFCLR YPMLYQEGPQ NLLFRWSRLL GWMAYGVASG
VIIFFLTSAA LQHQAFRRGG EVVDLAILSG TAYTCVVWAV NAQMTVTANY FTLVQHACIW
GSVALWYVFL LAYGAITPAF STNYFMLFTD GLAAAPSYWV VTLLVPAAAL LPYFTYSAAK
TRFFPDYHNK IQWLQHRGSN ADDPEFGHAL RQFSVRSTGV GVSARRDARD LHLPPPSQSH
SHSQTTST
//
