ID A0A0A1U6Z5_ENTIV Unreviewed; 1080 AA.
AC A0A0A1U6Z5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=EIN_405090 {ECO:0000313|EMBL:ELP90095.1};
OS Entamoeba invadens IP1.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP90095.1, ECO:0000313|Proteomes:UP000014680};
RN [1] {ECO:0000313|EMBL:ELP90095.1, ECO:0000313|Proteomes:UP000014680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP1 {ECO:0000313|EMBL:ELP90095.1,
RC ECO:0000313|Proteomes:UP000014680};
RA Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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; KB206537; ELP90095.1; -; Genomic_DNA.
DR RefSeq; XP_004256866.1; XM_004256818.1.
DR AlphaFoldDB; A0A0A1U6Z5; -.
DR EnsemblProtists; ELP90095; ELP90095; EIN_405090.
DR GeneID; 14889129; -.
DR KEGG; eiv:EIN_405090; -.
DR VEuPathDB; AmoebaDB:EIN_405090; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000014680; 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:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 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 Hydrolase {ECO:0000313|EMBL:ELP90095.1};
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:UP000014680};
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 111..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 310..328
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 334..355
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 822..844
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 850..874
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 904..926
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 932..951
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 958..978
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 990..1013
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 56..113
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 792..1018
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1080 AA; 123688 MW; B0DB2F2F7C8378A8 CRC64;
MEKTDLSTDI PLVSSSDDDW LFPVDKRKWY EKIPFTHWYK KFYMPRTIKR TTVEIKKAPK
YVTNKIANTR YTWWNFLPMS LFNQFKYFYN LYFLLNASSQ LIPAFKVGMT FTYFAPLVFV
VALSICKDAV DEIRIKLRDI KLNNEEFEMV SQGQFIPVKS KDIKVGQLLR LKKGQRVPAD
LVILQSADDE GTCFIKTDQL DGETDWKFRK CIKEFQGLPI AELETSEFDL DTEAPHNAIY
SFIARVRKGY DTIPVSIDNT AWANTILVSE EIVGIVIYTG KETRSSMNRN DQRNVKVGRV
DMALNRVSKV LFCIMLALSL LMVCPDVFHG IFSFFTVVTV VRFMVLYSSI IPISIRVNLD
ISKLIYSFFI STDDKMEGAE VRNSSIPEEL GQVQFLLSDK TGTLTKNEMS FKVLSLGTQS
YSVDSAEEMK DELKEYLQTD NTQRVMKNSS TSKMAECIKA LALCHNVTPC VTASGERYYQ
ASSPDEVALV KFTEQVGVIL KEKTFAKMVL DVEGREERFE ILNMFPFSSS TKRMGVIVKS
DEGIVLYMKG ADSIMAQLID NIEWLGEECG NLAKDGLRTL VFGKKIIPSD VYEVFKKEYN
VASSMMIGRE EAVAKSVSKI EGHLHMLCIT GVEDELQDDV QQSLEMLKRA GIRTWMLTGD
KVETALCIAK STRLVSVDQE VREFFASSSL EAEALMEKYG GNINEEGLIV DGSTLSLVLK
ELPMRFIHFA LQAKSVICCR CMPTQKAEVV NLVKKSGIRT CAIGDGGNDV SMIQAADVGL
GIEGKEGKQA SMAADFSMKQ FSHVTRILLW HGRNSYIRSS DLALFIMHRG MIISIMQAIF
SAIFNFAPVA LFQGFLLMGY ATYYTMFPVL AIVLDERVNE QKVMEFPELY YQLQTKQRLS
MTSMLTWVSV SILQAVVIMF LCMFLFKETF LDIVSISFTA LILIELINVG FSIKRWNWLI
LSSELFSVTI YFLSFFFLKS YFDLHFVFSW QFWWKLFVIV VLTSIPFIAK FIYQIIFPPK
SLTVENRRWP VSFNTKCPKM PKIKMFKKYN KYFKWFNPLN WCACKKKNNQ GPYEQQMVDL
//