ID A0A0E0AUX4_9ORYZ Unreviewed; 1102 AA.
AC A0A0E0AUX4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM08G14180.3};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM08G14180.3}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM08G14180.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0E0AUX4; -.
DR EnsemblPlants; OGLUM08G14180.3; OGLUM08G14180.3; OGLUM08G14180.
DR Gramene; OGLUM08G14180.3; OGLUM08G14180.3; OGLUM08G14180.
DR HOGENOM; CLU_000846_5_2_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
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; 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:SF165; PHOSPHOLIPID-TRANSPORTING ATPASE 8-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_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:UP000026961};
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 312..333
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 362..387
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 957..980
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 992..1015
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1022..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1061..1081
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 890..1091
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 122330 MW; 911272A70E86B4FB CRC64;
MRPPAASAAD ERPLVELTPA AATAPAPAVS SAPGFTRAVR CSGAGCSSSS SSSSSSSDEG
GGGVYPGNAI STTKYTAASF VPKSLFEQFR RAANCFFLVV ACVSFSPLAP YRAVSVLLPL
VVVVGAAMAK EAVEDWRRKQ QDIEVNSRKV EVYDGTQSFH QTEWKKLQVG DIVKVKKDEF
FPADLVLLSS SYEDGICYVE TMNLDGETNL KRKQSLDVTA GLNEDHSFHT FKAFIQCEDP
NEKLYSFLGT LHYNGQQYPL SPQQILLRDS KLRNTNQIYG IVIFTGHDTK VMQNAMEPPS
KRSSVERRMD KIIYLLFVIL FAIASFGSVM FGIRTRAELS AGNYAWYLRP DNSTMYFDPN
RATLAAICHF LTSLMLYVCL VPISLYISIE IVKVLQSTFI NQDQNMYCEE SDKPARARTS
NLNEELGQVH TILSDKTGTL TCNSMEFLKC SIAGVAYGNR PIEVQMPYGG IEEECVDIGQ
KGAVKSVRPV KGFNFTDDRL MNGQWSKECH QDVIEMFFRV LAVCHTAIPV ADRTSGRMSY
EAESPDEGAL VAAARELGFE FYHRSQTSIS VHEYDPVFGR KVDRTYKLLN TLEFSSARKR
MSVIVRTEEG RLFLFCKGAD SVILERLSKD NSKACLTNTK CHIDEYSEAG LRTLALAYRE
LTEDEYVAWN MEYSAAKNSV HNDHDVAVEK ASENIEKDLV LLGATAVEDR LQKGVPECIH
KLAQAGIKIW ILTGDKLETA VNIGYACNLL RKGMEEVYIT LDNPGTNVPE EHSGESSGMA
PYEQIGRKLE DARRQILQKG TSAPFALIID GNALTHALMG GLKTTFLDLA VDCVSVLCCR
ISPKQKALIT RLVKNRIRKT TLAIGDGAND VGMLQEADIG VGISGAEGMQ AHAMFSAQPG
YNDWFISFYN VAFTSLPVIA LGVFDKDVSS RVCLEVPSLH QDGVNNLFFS WSRILSWMLN
GVCCSIIIYF GALHAVLIQA VRQDGHVAGF DILGVTMYSC VVWTVNCQLA LYISYFTWIQ
HFVIWGSILI WYTFLVIYGS FPPTISTSAY HVFWEACASS PLYWLSTLVI VVTALIPYFL
YKITQSLFYP QHCDQAQRPN SK
//
