ID A0A0B2V1A6_TOXCA Unreviewed; 1263 AA.
AC A0A0B2V1A6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=Atp8a1 {ECO:0000313|EMBL:KHN75244.1};
GN ORFNames=Tcan_13028 {ECO:0000313|EMBL:KHN75244.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN75244.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN75244.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN75244.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) 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: 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:KHN75244.1}.
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DR EMBL; JPKZ01002767; KHN75244.1; -; Genomic_DNA.
DR STRING; 6265.A0A0B2V1A6; -.
DR OMA; AFAMNKQ; -.
DR Proteomes; UP000031036; 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; 1.
DR PANTHER; PTHR24092:SF214; 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:UP000031036};
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 347..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 402..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 901..923
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 935..953
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 982..1005
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1017..1039
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1051..1071
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1091..1119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 47..100
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 870..1128
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1238..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 141784 MW; 2E3E0F97F741C072 CRC64;
MNERPSPLNR PTSIFSMPIS ETLRSCLRKR VDINDRVNVT IGTLIMHSTN RVSTTRYNFF
TFLPLFLYNE FKSFANIFFL CICIAQCIRE LNPFGTNTTI IPLVSILFIA AMKEMFEDIS
RKISDRKVNR QLMTAFAMNK QKTWGWTKVH WSQSRKISDR KVNRQLMTAF AMNKQKTWGW
TKVHWSQLKV GQVVKVQRDE GIPADLLLLS SSEPAGMAYI ETSNLDGESN LKIRQALPCT
AFATSDQNIE DLIASGSTVD CDPPSPMIYE FKGIINLKKS FATKSEHSNE FITYPLGTSQ
LLPRGCKLQN TDWVYGVVVY AGNHTKLMLN STRTTVKRSK VEKFTNSIMM IQFGFLVALV
LFNACAGASK IHSKYYYFPV TQSKSGLDCG QVWMRPHLSV SILGMIITYS GLIPISLLVT
LEMIALFQAY FIRQDLEMYD ENSDTRAEVR SSNLNSLLGQ VRYVVTDKTG TLTQNKMNFK
MCTIGGVKYG NKNSDQFDDP TLISDMQTNA KNNAAEIREF LTLLAVCHTV VPEKGKDGSL
VYHASSXXEA ALVTCARQLK FVFHTRTPFC VYINAMGKEE KYEVLNVLEF TSDRRRMGVI
VKSPAGNIKL YIKGADSVIL PRLSASADQR LIKTTTSHLI DFANCGYRTL CMAVAELSDR
EYMEWEPDYY RASIALDGRE KLIQEQAEKI ERNLRLLGAT GIDDKLQEGV KTTIANLALG
GMGVWVLTGD MLETAQNIGF SCGLIKPDIP TLVISENSAE KTRDRLRSYI NDVYSSHSSI
KIALIVSGQS LGHVLNDTID VEFFLLASRC SCVICCRCSP MQKAAVVKLI QKYCDGATLA
VGDGANDVAM IQAADVGVGI SGEEGMQASL AADYSIAQFR FLSRLLFVHG AISYHRTTKT
ILYFFYKTVC ESAIIFIYSH WALSSDTAVF DSWSIVFYNM FFSSWPPLAL GIWDRLFSFD
IMEQYPGLYV LSQREQTFNL KLFFSWVANG VLHAFVIFFV GYHTFKQDIM WSSGRIANIR
CFGTAMNIVI TFQALVLTVN VKAAIEMDSH TVMSLVACGG SLTMMFIYLF SYCLTSPHSP
VVVVDPEMAD IILDIFHSPV ILLSIVLSTV LAISFDVLFK VVQRLLYRNL KDEVLSKEFA
SGKKFDVLSQ PFFKVRDFMV RTSESALSLV NHPLKSHGYA FSQDEGTIVP QSDLVRIYDS
RIPKLAGSPM DGERSYRYSE MRSLSSIKSS PFIMNRLSTD NGSIESNNSS KTPSVSDEEE
SNN
//
