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Database: UniProt
Entry: A0A6J3R0B9_TURTR
LinkDB: A0A6J3R0B9_TURTR
Original site: A0A6J3R0B9_TURTR 
ID   A0A6J3R0B9_TURTR        Unreviewed;      1101 AA.
AC   A0A6J3R0B9;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=ATP8B4 {ECO:0000313|RefSeq:XP_033707558.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033707558.1};
RN   [1] {ECO:0000313|RefSeq:XP_033707558.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_033707558.1};
RG   RefSeq;
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   RefSeq; XP_033707558.1; XM_033851667.1.
DR   AlphaFoldDB; A0A6J3R0B9; -.
DR   Proteomes; UP000245320; Chromosome 2.
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; 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:SF80; PHOSPHOLIPID-TRANSPORTING ATPASE IM-RELATED; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 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|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:UP000245320};
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        167..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        209..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        767..789
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        795..816
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        846..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        885..903
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        915..938
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        958..979
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1000..1019
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          732..986
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1101 AA;  124711 MW;  3AE8F8E8434662C4 CRC64;
     MTVNIMRSTS TQLQNEKWMN VKVGDIIKLE NNQFVAADLL LLSSSEPHGL CYIETAELDG
     ETNLKVRHAL SVTSELGADI SRLAKFDGIV VCEAPNNKLD KFTGVLSWKG SKHSLNNEKI
     ILRGCVLRNT SWCFGMVIFA GPDTKLMQNS GKTKFKRTSI DRLMNTLVLW IFGFLICLGI
     ILAIGNSIWE NQVGDQFRTF LFWNEGEKNS VFSGFLTFWS YIIILNTVVP ISLYVSVEVI
     RLGHSYFINW DRKMYYSGKA TPAQARTTTL NEELGQIEYV FSDKTGTLTE NIMTFKRCSI
     NGRIYGEVHD VLGQKTDMTK KKEAVGFSVN PQADRTFQFF DHHLMESIKM GDPKVHEFLR
     LLALCHTVMS EENSAGELIY QVQSPDEGAL VTAAKNLGFI FKSRTPETIT IEELGTLVTY
     QLLAFLDFNN FRKRMSVIVR NPEGQIKLYS KGADTILFER LHPSNEDLLT LTSDHLSEFA
     GEGLRTLAIA YRDLDDKYFK EWHKMLEDAN AAVDERDERI AGLYEEIERD LMLLGATAVE
     DKLQEGVIET VTSLSLANIK IWVLTGDKQE TAINIGYACN MLTDDMHDVF IIAGNTAVEV
     REELRKAKEN LFGQNRSFSN GHVVFEKKQP LELDSVVEET VTGDYALIIN GHSLAHALEN
     DVKNDLLELA CMCKTVVCCR VTPLQKAQVV ELVKKHRNAV TLAIGDGAND VSMIKSAHIG
     VGISGQEGLQ AVLASDYAFA QFRYLQRLLL VHGRWSYFRM CKFLRYFFYK NFAFTLVHFW
     FGFFCGFSAQ TVYDQWFITL FNIVYTSLPV LAMGIFDQDV NDQNSMDCPQ LYKPGQLNLL
     FNKHKFFICV AHGIYTSLVL FFIPYGAFYN VAGEDGQHIA DYQSFAVTMA TSLVIVVSVQ
     IALDTSYWTI INHVFVWGSI ATYFSILFTM HSNGLFGIFP RQFPFVGNAR HSLTQKCIWL
     VILLTTVASV MPVVAFRFLK VDLFPTLSDQ KRLSLHKVAH CVESISSGCF ISLWVSFVSR
     SASGRRLKRR QDPCVGESLR LGDQAREDLD MLLLTKRAME SLSHLEKICE LKIHPRHQGW
     KRHCIIALAG LKIYVRKPQT Q
//
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