ID A0A183A616_9TREM Unreviewed; 1325 AA.
AC A0A183A616;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=ECPE_LOCUS2401 {ECO:0000313|EMBL:VDP66364.1};
OS Echinostoma caproni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC Echinostoma.
OX NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000240101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ECPE_0000240101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP66364.1, ECO:0000313|Proteomes:UP000272942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Egypt {ECO:0000313|EMBL:VDP66364.1,
RC ECO:0000313|Proteomes:UP000272942};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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|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|RuleBase:RU362033}.
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DR EMBL; UZAN01039590; VDP66364.1; -; Genomic_DNA.
DR WBParaSite; ECPE_0000240101-mRNA-1; ECPE_0000240101-mRNA-1; ECPE_0000240101.
DR Proteomes; UP000050740; Unplaced.
DR Proteomes; UP000272942; 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: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; 2.
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; IPR032631; P-type_ATPase_N.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR PANTHER; PTHR24092:SF212; 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 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:UP000272942};
KW Translocase {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 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 312..335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1088..1111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1138..1169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1189..1208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1215..1236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1256..1278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 33..86
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1027..1284
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 463..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 149521 MW; 66EB1642A096F949 CRC64;
MPKSSCVCSC RRKRREKETR IVYANHGPEY LIPEADRKVK FCNNAIISSR YTWYNFVPKN
LFEQFHNMAN VFFAMISILY VFASPTTSIW SNLGPLMAIL AIIMVKDGVE DILRHRRDRA
LNHIPVNVLE VNWTDETVKW TQKKAMNLSV GDVIKCDRGK AFPCDIVLLA SSNTTTEVNV
TTANLDGESN IKKYFAVGET QTIYHQVANP DWLAGPNGAL FSQLAKQLHV KVECQPPCAD
LTRFEGRMSS TLWDTEEPIP LTFPNLALRG AKLANTEFVL GLVVYTGKDT KLSLNGKQAK
RKYSSREARS NIILLSFIIA MIVISIIFGI VYTVWTSQNK ANMWYLSNAP QTSWEFVQNV
FRFIVIVNYL IPISIIFIIE FQQMYIAFTI SSDLQMHDPV EDQASKANSA QVADELGQVE
FLFSDKTGTL TQNVMQLRTC AVLHQNGTAD VYEFAHAQSE YSSIDGTRSP SRGRHSGATE
RESVFSSSSS SENEDDNDDA RYEGKRDSRS GGNGSSSTSK ESFRLNARAP KRNYLKPVVE
PNGTLEYILT LFTLCHTVEL DENQEEGQVM PKYEAASPDE KALVEGAAEH GVIFLQSKPI
EGQVNSKTYR IEYQRTDDLD HAPPGHSNST GSAKTIEYIV DAVLEFDSTR KRMTVMTRYP
DGTCHIHSKG AETSMLDAES CAESCGAIRT KAMHYVNEFA LDGLRTLVYG TRQVDRAEYD
RLLTELRRTR GLVGEQRLRA MREVYQAIES NLVPCAVTGV EDKLQVGVRE CLQSLRESGI
QIWILTGDKE ETAVTVSQSA GHFTPQMSLI RLTNCPDFHT AACWLFEQIE GLQTRFDLRL
TRRTHTQTTL VPQSTSRRSL ITPSIEEVGE VVLAAAECEE NATGSEDKGS ETKRRRLTRR
LLSFVRGGTW KKLRLPRRRH THRPGLAGEP IGLVIDGKTL NCVLHPTLRD AFLDLCMNVT
TVLCCRMTPL QKASIVQLVQ AGLARSSSGE GSTPVTAAVG DGGNDVAMLL QANIGVGLYG
KEGREAARAG DYSLPGFRYL HRLFLLHGHW AYHRLTFTMN LFYFKCTALV TTELLLQFYS
GFSQIANYGG ILFALFNLTM TSVACLLYGM FEQHLPEREL MLRPYLYRVI SRQANLRAWF
VILWIVEGLW FALITFFIVV CGLAGGMYYA PAIFMEPGVP PRAMYDFSLV GVANYVCIWI
AVNVRIAILT RHMNYMMVIG FLITLVNIGI LFLYQTTCGY ESLEYLAFVK LARSPAFWFS
LMLSVFIANF SSIIWRMASD TWWTSQIRLS EIPQRKMRKK RRRSPRFWFE SLVDGQRDYR
PMGNN
//
