ID A4RZ78_OSTLU Unreviewed; 1242 AA.
AC A4RZ78;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=OSTLU_49740 {ECO:0000313|EMBL:ABO96822.1};
OS Ostreococcus lucimarinus (strain CCE9901).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO96822.1, ECO:0000313|Proteomes:UP000001568};
RN [1] {ECO:0000313|EMBL:ABO96822.1, ECO:0000313|Proteomes:UP000001568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABO96822.1,
RC ECO:0000313|Proteomes:UP000001568};
RX PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA Van de Peer Y., Moreau H., Grigoriev I.V.;
RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT of plankton speciation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
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 EMBL; CP000586; ABO96822.1; -; Genomic_DNA.
DR RefSeq; XP_001418529.1; XM_001418492.1.
DR AlphaFoldDB; A4RZ78; -.
DR STRING; 436017.A4RZ78; -.
DR EnsemblPlants; ABO96822; ABO96822; OSTLU_49740.
DR GeneID; 5002417; -.
DR Gramene; ABO96822; ABO96822; OSTLU_49740.
DR KEGG; olu:OSTLU_49740; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR OMA; KANIAVW; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000001568; Chromosome 6.
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; 1.
DR PANTHER; PTHR24092:SF180; PHOSPHOLIPID-TRANSPORTING ATPASE 3; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001568};
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 291..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 342..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 899..919
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 931..951
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 984..1003
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1023..1043
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1050..1073
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1093..1113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 32..89
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 867..1119
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1131..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 645..672
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1211..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1242 AA; 139143 MW; 698DE1F136C891A4 CRC64;
MVERLRRKRA KPTARKLVLG AGEPNDGKDL AKEFKCKDNS ICTGKYNVVT FAPKGLYEQF
RRVANLYFLS VAVISLFPTV SPIQPYTTWT PLTMVIGLSL AKEAVEDYKR HVQDRVQNTS
TTERFNGESF ENCEWHDLKV GNIVRVVRDQ FFPCDLIMLD SSSDENACYV ETKNLDGETN
LKTKRSVDVA DLKFDRETFA KMSEGKTFIE CEHPNNSLYT YSGNLSIGAP LYPNGKKVSL
NPSNMLLRGS SLRNTEWIVG VCVYTGHDSK VMMNATDTPS KRSHLEKQMD GVVITMLIAL
FVMSTASAIY CSAWIGSGAK DHWYLAVHLQ DVTFNPDNRT SVGVIAFFTS YVLYGYLIPI
SLYVSLELVK VFQGFVFLNK DRAMYHEETD TPALARTTNL NEELGMVHTV LSDKTGTLTC
NTMEFFKCSI AGVAYGEGVT EIERAIMQRK GEPLPPKNGD AIEPSFNFRD KRLENGAWHK
RSDADICRGF FRVLGICQTV IPEGNPVPSE IVYQAESPDE LAFVVAAKRF GFFFKHRSAT
TITVEEEAFN DGRPGTEDVT YTILNTLEFT SARKRMSVIV KSKNDGRILL FTKGADNVIY
ERLSQNGNEF KDATQEHMDA WAKCGLRTLC LARRVINPSE YASWNEKFIE ASQALQNREE
KLEEVANLIE KDLTLLGSTA IEDKLQVGVP RTIEQLMKAN IAVWVLTGDK QDTAINIGQA
CSLITPQMKV RVINVEDLVK QENNGEIDSA TFQRLAMASV KQQIEAGLVD AEAAIQLDAD
VGMVIDGRSL TLALKPELAG SFLALGTKCS AVICCRVSPL QKALVTTLVK DSGRITLAIG
DGANDVGMIQ AAHIGVGISG QEGMQAVMAS DFAFAQFRFL ERLLLLHGRY NYKRIARMVT
YFFFKNIAFG LTIFIFNMHT KASGQTVYND WLMSSFNIFF TNFPVLALGI LDQDVKPQSS
MEVPELYRET QANSQFTSRR RLTWFAYGIY VAVVSFVMVF YGIHTGEADA ESGQPFGLWE
VGTTLYTALL IALNVQLGLL CNFWTLFHHV VIWGSILLWF ILNMALSETE VYYSTYSYKT
FLPITSQVMK YWLGFWPVAI ISIWPYIASI MFMRYFRPTL ADEVQDRDAA IRRSSGGKSE
KEGVEPRQKV DVELKSPRRS GTLHGVVVES LGIAPVKAEE IKAPKHRRKL SFADVWGKET
QFPDVPGGRR SSQDRTPTHS RGVSLESLSL PTLPEDRSAR DL
//
