ID A0A6I8VZA6_DROPS Unreviewed; 1550 AA.
AC A0A6I8VZA6;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC4802597 {ECO:0000313|RefSeq:XP_033236435.1};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_033236435.1};
RN [1] {ECO:0000313|RefSeq:XP_033236435.1}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_033236435.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_033236435.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_033236435.1; XM_033380544.1.
DR Proteomes; UP000001819; Chromosome 2.
DR ExpressionAtlas; A0A6I8VZA6; 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; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 3.
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:SF150; 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 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 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:UP000001819};
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 57..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 274..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 323..352
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1216..1236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1266..1285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1297..1315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1327..1350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1370..1393
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 17..82
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1152..1398
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 439..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1484..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1550 AA; 174200 MW; 90F1BA7DAE74893A CRC64;
MGTKTQPQQA KENERRIRAN DKEFNLQYKY HNNYIKTSKY SVFTFLPFNL LEQFQRLANF
YFLCLLVLQL IPAISSLTPV TTAIPLIGVL TLTAVKDAYD DIQRHLSDSQ VNNRKSKTLR
NGKLVDAKWS EVQVGDVIRL DNNQFVAADI LLLTTSEPNG LCFIETAELD GETNLKAKQC
LTETIELGDH HDALWNFNGE ILCERPNNLL NKFDGTLIWR NQRFALDNEK ILLRGCVLRN
TQWCYGVVVF AGVDTKLMQN SGKTQFKSTG VDRLLNFIII GIVLFLVSIC ALFAVGCAIW
EGLIGQHFQV YLPWEHIIPK DYIPSGATVI GLLVFFSYAI VLNTVVPISL YVSVEVIRFI
QSFLINWDEE MYYARTNTYA KARTTTLNEE LGQIQYIFSD KTGTLTQNIM TFNKCSINGR
TYGDVIDLRT GEPIEVTEQQ TIFHNSPRNP EEVPTGTATS TKQPPLILVH KAEVHAKKSS
VMVTAEGETQ LASSPSSDRA EMEHSAPLPA PQDPQRNRGR KQVRYSAPSR SQEEEPGGTI
PGRLPTPRGS SPSGYDSQRS SSRSSGGGLG VCFKRSGPGL MQRQLSSTNS SDKVKILHDN
EQTEPHMHHH NQHHHSQHHQ QPQHNGRLVK LKFKKSPSTT SLSVPFCHNH SATEELTLQA
PPTAQHQSTT HQNHHNESFA TNWSSSRQRV HALQCVDFSA NPHHESDFRW YDRTLLDAVR
SDEEHSHVFF RLLALCHTVM AETVEGKLEY QAQSPDEAAL VAAARNFGFV FRSRTPNSIT
IEVMGRKEEY ELLNILDFNN VRKRMSVILR RGNTVVLYCK GADNVIYDRL HGGQEDLKAR
TQDHLNKFAG EGLRTLVLAE RRLTEQYYKN WRTRQQEAAL AMDSREERLN EIYEEIESDM
QLVGVTAIED KLQDGVPKAI ANLQSAGIKI WVLTGDKQET AINIGYSCQL LTDELADVFI
VDGNSVEEVE KQLRQFKESI KIYNRFRPGG TEALYNSDSN MDPLSVTMTQ TSVFMHESSN
PPTPPPPPAI SVVTFSAECN DLFGDEKRSL DDGAASIVID ETTGFALVVN GHSLVHCLSP
ELEIKFLDIA SQCKAVICCR VTPLQKALVV ELIKRAKNAV TLAIGDGAND VSMIKAAHIG
VGISGQEGLQ AVLSSDYAIA QFRYLERLLL VHGRWSYYRM CKFLRYFFYK NFAFTLCHCW
YSLFCGFSAQ TVFDPMFISV YNLFYTSLPV LSLGIFEQDV SDKNSVEYPR LYTPGLRSEL
FNIREFIYSV LHGAFTSLVL FLIPYGVYKD GVSQNGYILS DHMTLGAVVA TILIVDNTAQ
ISLYTSYWTI VNHITIWGSL VWYFVLDYFY NYVIGGPYVG SLTQAIKDLT FWMTMLITVM
VLVAPVLAYK YYLLDVHPSL SDKIRQKSLK KIHSRASSDV RRTPSSRRGR RSVRSGYAFA
HQEGFGRLIT SGKIMHKMPQ DFAFPLGLGT KKTQALHNNL ASADQTKASN SSGHHMGNNN
NTNQRHNQNQ NHSSMADISA EGRAADAGGS GANDDISPRA PCQDLDTINL
//
