ID A0A4W6DN06_LATCA Unreviewed; 1104 AA.
AC A0A4W6DN06;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP8A2 {ECO:0000313|Ensembl:ENSLCAP00010026308.1};
OS Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010026308.1, ECO:0000313|Proteomes:UP000314980};
RN [1] {ECO:0000313|Proteomes:UP000314980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sai Rama Sridatta P.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLCAP00010026308.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 AlphaFoldDB; A0A4W6DN06; -.
DR Ensembl; ENSLCAT00010026865.1; ENSLCAP00010026308.1; ENSLCAG00010012233.1.
DR GeneTree; ENSGT00940000157332; -.
DR Proteomes; UP000314980; 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 CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 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; 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:SF98; PHOSPHOLIPID-TRANSPORTING ATPASE IB; 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; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362033};
KW Coiled coil {ECO:0000256|SAM:Coils};
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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000314980};
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 60..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 226..249
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 797..817
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 870..888
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 908..927
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 979..998
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1039..1057
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 20..66
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 758..1008
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT COILED 553..580
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1104 AA; 124364 MW; 6374D5EB1B7648D2 CRC64;
MQCMYLVHSH KRKHTHTDIT TKYGILTFLP RFLYEQIRRA ANAFFLFIAL MQQIPDVSPT
GRYTTLVPLI FILTVAGIKE IIEDYKRHKA DNTVNKKKTT GIVCVLVSCP SVNFPGLDLL
WLMFFQGLSL TAGFQTLEDL MALSGRLECE GPNRHLYDFT GTLRLENQNP APLGPDQVLL
RGAQLRNTQW VVGIVVYTGH DSKLMQNSTK APLKRSNVER VTNMQILVLF GILLVMALVS
SVGAAIWNRE HTEDACWYLS RAGDISTNFA YNLLTFIILY NNLIPISLLV TLEVVKFTQA
LFINWDVEMY YSETDTPAMA RTSNLNEELG QVKYLFSDKT GTLTCNVMHF KKCTIAGITY
GHFPDLDCDR SMEDFSNLPS SSNNSTEFDD PTLIQNIEKN HPTSPQICEF LTMMAVCHTV
VPEREGNQII YQASSPDEGA LVKGAKGLGF VFTARTPHSV IIEARGKEMS YELLNVLEFS
SNRKRMSVVV RTPNGRLRLY CKGADNVIFE RLTGASQYKE LTVAHLEQFA TEGLRTLCFA
YVDLEEDAYQ EWLKEYNQAS TVLKDRAQKL EECYELLEKN LMLLGATAIE DRLQAGVPET
IATLMRADIK IWVLTGDKQE TAINIGYSCR LVTHGMSLII VNEDSLDATR ATLTTHCSSL
GDSLRKENEL ALIIDGQTLK YALSFELRQA FLDLALSCKA VICCRVSPLQ KSEIVDMVKK
HVKAITLAIG DGANDVGMIQ TAHVGVGISG NEGMQATNSS DYSIAQFSYL EKLLLVHGAW
SYNRVTKCIL YCFYKNVVLY IIELWFAFVN GFSGQILFER WCIGLYNVIF TALPPFTLGI
FDRPCSQQNM LRFPQLYRIT QNAEGFNTKV FWGHCINALI HSIILFWFPL KMLEHDSPFN
NGQGNDYLFV GNMVYTYVVV TVCLKAGMET TAWTRFSHLA VWGSMVLWMV FFAVYSAIWP
TIPIAPDMLG QAGRVMQCWH FWLGLVLVPT ACLLKDFAWT ATRRTVRKSL LEEVQELEAR
AVDPGAAVLR DASGLKYIML HYIVKLFTFF FTSGFIISDL SSSLSSDGYA FSQEEHGVVS
QSQVVRSYDT TPQMNSLKKG GREA
//
