ID A0A0E0C0P9_9ORYZ Unreviewed; 1386 AA.
AC A0A0E0C0P9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-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 meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI01G11120.1};
RN [1] {ECO:0000313|EnsemblPlants:OMERI01G11120.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI01G11120.1};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI01G11120.1}
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}.
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DR STRING; 40149.A0A0E0C0P9; -.
DR EnsemblPlants; OMERI01G11120.1; OMERI01G11120.1; OMERI01G11120.
DR Gramene; OMERI01G11120.1; OMERI01G11120.1; OMERI01G11120.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_3_4_1; -.
DR Proteomes; UP000008021; Chromosome 1.
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:SF207; PHOSPHOLIPID-TRANSPORTING ATPASE; 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 PRINTS; PR00121; NAKATPASE.
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:UP000008021};
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 143..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 946..967
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 973..994
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1015..1037
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1049..1069
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1081..1103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1109..1131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 83..142
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 906..1146
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 153276 MW; 0809FD8F9F9A618A CRC64;
MASERPLLDA SPRPPQQPPA SSLLPPPQPE PPLRADRLAF SLEVPDPFRR EPDPSSAASQ
REVVGEEEEG GGEEESRAVV VGEPSSSAAA GFAGNAVRTA KYSVLTFLPR NLFEQFRRLS
YVYFLAITVL NQLPQVAVFG RGASVLPLAF VLFVTAVKDA YEDLRRHRSD RQENNRLAKV
LLAPPAAGEF APKKWKHIRV GDVVRVASSE TLPADMVLLA TSDPSGVAHV QTVNLDGETN
LKTRYAKQET QVRFSQDGSV GGVLHCERPN RNIYGFQANL EIDGKRVSLG PSNIVLRGCE
LKNTTWAIGV VVYAGKETKV MLNSSGAPSK RSQLETQLNR ETVILSIMLI GMCTTASVLV
GIWILNHRGD LEFTQFFREK DYTTGKNYNY YGMGMQIFIT FLMAVIVYQV IIPISLYISM
ELVRLGQAYF MGADRDLYDE SSRSKFQCRA LNINEDLGQI KYVFSDKTGT LTENKMEFQC
ASIRGVDYSS GKDSCGYSVV VDDLLWTPKM AVKTDPRLLK LLRGGGTDEE TKLVLEFFLA
VAACNTIVPL VLDTRDSKQK LIDYQGESPD EQALVYAAAS YGIVLVERTS GYVVIDVLGD
RQRFDILGLH EFDSDRKRMS VIVGCPDKTV KLYVKGADSL LFGITKNSLD LDIVRATEAH
LHKYSSFGLR TLVIGMRELS QAEFEEWQLA YENASTSVLG RGNLLRSVAA NIENNIRILG
ATGIEDKLQD GVPEAIESLR QADIKVWILT GDKQETAISI GYSCKLLTND MTQIVINNNS
KESCKRSLEE ALATIKKLRI ASTGTQSPEL ASESAGVTLV LIIDGNSLVY ILETELQEEL
FKVARECSVV LCCRVAPLQK AGIVALIKNR TDDMTLAIGD GANDVSMIQM ADVGVGISGQ
EGRQAVMASD FAMGQFRFLV PLLLVHGHWN YQRMSYMILY NFYKNATFVL VLFWYVLYTA
FTLTTAITEW SSLLYTVLYT SLPTIIVGIL DKDLSKETLL AYPKLYGSGQ RDEKYNVNLF
VLNMLEALWQ SLVVFYMPYF AYRQSTIDMS SLGDLWALAP VIVVNMLLAM DIFRWNWIIH
AFVWGTIAAT TICLFVIDSI WFLPGYGAIF HIMGTGLFWL LLLIIVVAAM VPHFVIKAFT
EYFTPSDIQV AREIEKFENV NQVNRSEVPM TRQPGKQLHR GGTRGIGTTG VQIPGAGTIS
CGGHESGQGI PSFNPRTGCV EHCVAGMRAT LFHPRLQGST KAGPVGKGNA TPLQHPDLLF
GSFIIALSGI RFSEQLDTTT DDAHDFSSLL SPEAKGTRCF IFLQCCWKER RSMCNNLMVN
HIRNISRSYS IIARHHSLTV LRHMLISASS STNWDIPHSS TSGPISLAVP AEVPGLSLGL
PEKPAT
//
