ID A0A4W5Q596_9TELE Unreviewed; 1122 AA.
AC A0A4W5Q596;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:ENSHHUP00000069070.1};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000069070.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000069070.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A4W5Q596; -.
DR Ensembl; ENSHHUT00000071385.1; ENSHHUP00000069070.1; ENSHHUG00000040450.1.
DR GeneTree; ENSGT00940000157332; -.
DR Proteomes; UP000314982; 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; 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: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; 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|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000314982};
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 295..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 340..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 855..875
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 928..946
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 966..985
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 997..1017
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 49..109
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 816..1036
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1122 AA; 125933 MW; 317874711D1CB0E0 CRC64;
MTENVPPTLS GCARTSCSSA GYRKADDEMS GTTSQADPID ATARTILLNQ PQNTKFCDNH
VSTTKYGVFT FLPRFLYEQI RRAANAFFLF IALMQQIPDV SPTGRYTTLV PLIFILTVAG
IKEIIEDYQR HKADNTVNNK KTTGIGRLCV AVGDIVKVTN GQHLPADMVI VSSSEPQAMC
YTETSNLDGE TNLKIRQGLT HTAGLQSLEE LMGLSGRLEC EEPNRHLYDF TGTLRLDNQN
AVPLGPDQVL LRGAQLRNTQ WVVGIIVYTG HDSKLMQNST KAPLKRSNVE RVTNVQILVL
FCILLVMALV SSIGASIWNK QHTEEACWYL SRAGDISTNF WYNLLTFIIL YNNLIPISLL
VTLEVVKFTQ ALFINWDEEM YYSETDTPAM ARTSNLNEEL GQVKYLFSDK TGTLTCNVMH
FKKCTIAGIT YGHFPDLDVD RSMEDFSLNS TEFDDPTLIQ NIEKNHPTSA QICEFLTMMA
VCHTVVPERE EDQLIYQASS PDEGALVKGA KGLGFVFTAR TPGSVIMEGE GEDLFFFYSN
RKRMSVVVRT PDGKLRLYCK GADNVIFERL TDASQYKELT IAHLEQFATE GLRTLCFAYV
DLEEGVYQEW LKEYTRISTI IKDRAQKLED CYELLEKDLL LLGATAIEDR LQAGVPETIA
TLMKADIKIW VLTGDKQETA INIGYSCRLV SHGMSLIIVN EDSLDATRAT LTAHCTSLGD
SLGKENELAL IIDGQTLKYA LSFELRQAFL DLALSCKAVI CCRVSPLQKS EIVDMVKKHV
KAITLAIGDG ANDVGMIQTA HVGVGISGNE GMQATNSSDY SIAQFSYLEK LLLVHGAWSY
NRVTKCILYC FYKNVVLYII ELWFAFVNGF SGQILFERWC IGLYNVIFTA LPPFTLGIFD
RPCSQQNMLR FPQLYRITQN AEGFNTKVFW GHCINALIHS IILFWFPLKV LEHGNPFNNG
HGTDYLFVGN MVYTYVVVTV CLKAGMETTA WTKFSHLAVW GSMILWMLFF TVYSAFWPSI
PIAPDMQGQA SLLLKSSLFD RIYHQKKHKV QELEARAVDP GAAVLNERAH LLTRVFRKTP
SNVGRKNSVQ QNGYAFSQEE HGVVSQSQVC RSYDTTRQRP SI
//
