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
//