ID A0A183I2L9_9BILA Unreviewed; 712 AA.
AC A0A183I2L9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=OFLC_LOCUS13981 {ECO:0000313|EMBL:VDP15180.1};
OS Onchocerca flexuosa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0001398201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:OFLC_0001398201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP15180.1, ECO:0000313|Proteomes:UP000267606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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|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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362033}.
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DR EMBL; UZAJ01040513; VDP15180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183I2L9; -.
DR STRING; 387005.A0A183I2L9; -.
DR WBParaSite; OFLC_0001398201-mRNA-1; OFLC_0001398201-mRNA-1; OFLC_0001398201.
DR Proteomes; UP000050787; Unplaced.
DR Proteomes; UP000267606; 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
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 PRINTS; PR00119; CATATPASE.
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 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 238..256
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 263..281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
SQ SEQUENCE 712 AA; 79497 MW; 56D599350951B6ED CRC64;
MRYSRGLGAA ETKIRLEESQ PLMSESVAST SRDDIFLLPL ASTSPSSTVN RFAGFFDTIM
FRDRELNSEK YEKLTPQGID YISSSNIKVG DLIIIQKDKR VPADVVFLRT TEKSGASFIR
TDQLDGETDW KLRIAIPVTQ NLALDQDIFD LNLEIYAEKP QKDIHDFVGT FKVSSEDSTQ
DGSLNVENVL WANTVLASGR VVGVVVYTGR ETRSVMNTTL PKSKVGLLDI EVNNLTKILF
LFVVVLASVM VAMKGLDKNW YRYLMRFVLL FSYIIPISLR VNLDMAKLFY SWQIGRDRHI
KDTVIRSSTI PEELGRISFL LSDKTGTLTM NEMRFKKIHL GTVAFSSDAF EDVSRHILSA
YSGKLGRHSF SSKLQTAVEA IALCHNVTPT EENGQISYQA ASPDEIALVR WSEQVGVRLA
QRDLTSMQLQ LSNGQTKSFQ ILHLFPFTSE TKRMGIIVKD ETSDEISLLM KGADTVMAGM
VQYNDWLEEE SSNMAREGLR TLVVAKKVLS MEQLADFEKH YHQAKMTVVD RSEHMAAVLR
RLETDLQLIC LTGVEDRLQD QVTTSLELLR NAGIKIWMLT GDKLETAICI AKSSGLFSKT
DNVHVFGQVQ TRIDAHNELN ALRRKNDVAL VLSGSALNVC LQYYEAEVAE LVCGCTAVVC
CRCSPEQKAQ LVNLLRKYRS PLRVAAIGDG GNDVSMIQAA HAGIGIDAHE GL
//
