ID A0A674ME76_TAKRU Unreviewed; 1161 AA.
AC A0A674ME76;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC101064206 {ECO:0000313|Ensembl:ENSTRUP00000059278.1};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000059278.1, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000059278.1, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000059278.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A674ME76; -.
DR Ensembl; ENSTRUT00000072054.1; ENSTRUP00000059278.1; ENSTRUG00000015919.3.
DR GeneTree; ENSGT00940000161917; -.
DR Proteomes; UP000005226; Chromosome 21.
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:SF52; PHOSPHOLIPID-TRANSPORTING ATPASE FETA; 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|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:UP000005226};
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 77..95
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 312..337
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 854..876
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 882..903
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 932..952
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 972..990
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1002..1025
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1045..1066
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 32..83
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 819..1072
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1079..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1161 AA; 132060 MW; 1337FA5247194050 CRC64;
MTRVEPTVCQ IASVALFCSL YKPHIYHKAD TTNAIKTSKY NFFTFLPLNL FEQFQRIANA
YFLFLLVLQV IPQISSLSWF TTVVPLVLVL TVTAAKDATD DIVSSYIVHL RFIIKHSYEK
WMDVQVGDII KLENNQFVTA DLLLLCSSEP LNLVYIETAE LDGETNLKVK QSLTVTGDLG
DDVEKLADFN GEVCCEPPNN RLDRFTGTLT YSGQKYALDN EKILLRGCTL RNTDWCFGLV
LFAGQETKLM QNCGKSTFKR TSIDRLMNVL VLCIFGFLVL MCSILAIGNY FWETNTGSNF
TAFLPRQDGN DASLSAFLTF WSYVIILNTV VPISLYVSVE VIRLGNSFYI DWDSNMYYAQ
KDTPAEARTT TLNEELGQIK YIFSDKTGTL TQNIMTFNKC SINGRSYVTE VSLILMNSAV
DFSFNALADP RFTFHDHALV EAVKLENPEV HAFFRLLALC HTVMAEEKKE GEIFYQAQSP
DEGALVTAAR NFGFVFRSRT PDSITIVEMG NQRSYELLAI LDFNNVRKRM SVIVRSPEGK
LSLYCKGADT IIYERLHQSC SKLMDVTTEH LNEFAGDGLR TLALAYKDLD EEYFNQWKQR
HHEASTELED RERKLDQLYE EIEMDLLLLG ATAIEDKLQD KVPETIELLS KADIKIWVLT
GDKQETAENI GYACNLLCEE MNDVFIISSN SPEEVRQDLR SDGHFQKFIM KYFQSYLWSV
KTIADEVANG EYGLVINGHS LAYALDQSME LEFLKTACMC KAVICCRVTP LQKAQVVELV
KKYKKAVTLA IGDGANDVSM IKAAHIGVGI SGQEGMQAVL SSDYSFAQFC FLQRLLLVHG
RWSYLRMCKF LRYFFYKNFT FTFVHFWFAF FCGFSAQTVY DQWFITLYNL MYTALPVLGM
GLFDQDVNDA WSFQHPELYI PGQINLYFSK KAFFKCALHG GYSSLVLFFI PYAALYDTMR
DDGKDVADYQ SFALLTQTCL LFAVSIQLGL EMSYWTAVNT LFLLGSLAMY FVVTFTMYSN
GLFLTLPRAF AFIGSARNSL SQPSIWLSIL LTSILCVLPV VTYRFLSIRL CPSVMRKVRQ
AKATPPPPTR RRQIRRTSSR RSGYAFSHVQ GYGDLVTSGR FLRRNAVSRD ILEQQFTAWK
SCKKSPTTDL VIYLTTAGII I
//
