ID A0A484BCT3_DRONA Unreviewed; 1160 AA.
AC A0A484BCT3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=AWZ03_007775 {ECO:0000313|EMBL:TDG45820.1};
OS Drosophila navojoa (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG45820.1, ECO:0000313|Proteomes:UP000295192};
RN [1] {ECO:0000313|EMBL:TDG45820.1, ECO:0000313|Proteomes:UP000295192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG45820.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:TDG45820.1};
RX PubMed=30423125; DOI=.1093/jhered/esy059;
RA Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT the mojavensis Cluster.";
RL J. Hered. 110:118-123(2019).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDG45820.1}.
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DR EMBL; LSRL02000070; TDG45820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A484BCT3; -.
DR STRING; 7232.A0A484BCT3; -.
DR OMA; QALRCGR; -.
DR Proteomes; UP000295192; 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; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 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:SF91; 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 PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000295192};
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 163..187
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 921..941
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 953..973
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1003..1026
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1032..1053
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1060..1080
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1092..1119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 889..1133
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 383..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1160 AA; 130053 MW; 1466612398F4EA7F CRC64;
MTFIFETERY KKTKWQDLRV GDIVHLSNNE TVPADILLLR TSDPHGVCYI DTCDLDGETN
LKRREVVRGF TERQNVFVPS KFISCVEADA PTTKLYRFHG ALIHPTGERV PISTECLLLR
ESRLKNTDYI EGIVVYAGHE TKSMLNNSGP RYKRSQVEQQ MNIDVIWCVI ILLILCVVGA
IGCTMWLRSF ENFPVPYLPF VVDAAYEGML TFWTYIIILQ VMIPLSLYVT IELCKILQVY
HIHNNLELYD ADTNKQTECR AMNITEELGQ IQHIFSDKTG TLTENKMIFR RCVVNGTDYN
HPPSELEKLY AKPGAPAPPL IPNETLQDDM QRLAGVGNGA YLAPHAQCIQ EFLIVLAICN
TVIVSAAPHR DLMNASGIIE LHQNSSSPAT GPTPSTLKHL RPRNKLVTTT TTTTTIINGV
PQAGPMALPT DRYTRLAESR SVTPSPPPNL LFAMPAQGHQ PTLSPISSSP ESTPNSESPS
PPMKSKALSN SISPTGRAKA VINSKITSIA TFLNAKTHGK RMKIDQTKTQ TIYRTADGRP
LYEAESPDEL ALVNAAYSYD CCLLNRSPNH ILVSMPTAGA TLEYEILKIL PFDSSRKCMS
IVVRQTGTQE IVLYTKGADS SIMPVLAPCA PNSPEAILRE QTQQQLDRYA REGLRILVMA
KRTLNASDYT DWWARHQEIE MSLENRERRL RESFASLESN LTLLGATGIE DRLQDGVPET
IASLISAGIS VWVLTGDKPE TAINIAYSAK LFTQQMELIK LTARSRDAAE TAINFYLTEM
RNAKAVSSTG YSLAPRCKPR ALVVDGKTLT FILDPKSKLT LPFLKLAKGC ASVLCCRSTP
LQKAYLVKVV KEELNLRTLA IGDGANDVSM IQMADVGVGI SGQEGMQAVM ASDFTLSRFR
YLERLLLSHG YWCYDRLARM ILYFFYKNAA FVFLIFWYQL YCGFSGSVMM DQMYLMLYNL
LFTSLPPLAI GVYDNRVPED LLLKNPYLYK NGRLGLAYRP HDFWVILLDA LYQSLVIFFV
TLCAYAESEV GIWEFGTTIT ASCLFANLLH CCIEIRSWTV LHVLSIAISL GLFYLFSIVY
NSMCVNCFGL PSTYWVIFKC FASPVHWLVI MLSTVVAVLP RLVFRTVRTS MCPDDSTKVI
LQSKRERSRE SPIMGLRIRL
//
