ID A0A674N2T7_TAKRU Unreviewed; 1146 AA.
AC A0A674N2T7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-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=ATP11C {ECO:0000313|Ensembl:ENSTRUP00000067490.1};
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:ENSTRUP00000067490.1, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000067490.1, 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:ENSTRUP00000067490.1}
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; A0A674N2T7; -.
DR Ensembl; ENSTRUT00000085987.1; ENSTRUP00000067490.1; ENSTRUG00000008062.3.
DR GeneTree; ENSGT00940000158878; -.
DR Proteomes; UP000005226; Chromosome 14.
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; 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 NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF38; PHOSPHOLIPID-TRANSPORTING ATPASE IG; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 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.
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 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 286..309
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 340..359
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 948..965
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 985..1004
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1016..1037
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1057..1079
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 39..92
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 834..1081
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1146 AA; 131146 MW; D04A21128B7F6B61 CRC64;
QDCEMLVVHC LGGDERRVDS RTIYVGPHSC SATEAFIPPK FCDNRIVSSK YTVWNFLPKN
LFEQFRRIAN FYFLIIFLVQ VIVDTPTSPV TSGLPLFFVI TVTAIKQGYE DWLRHKADNE
VNKYPVTLLE GGRRIRKDSE KIKVGDIVEV IEDETFPCDL ILLHSTREDN TCFVTTASLD
GESNHKTHYT VPDTEKDLES LNATIECEQP QPDLYKFVGR MHIDKNDQEP VVRSLGPENL
LLKGATLKNT QKICGVAIYT GMETKMALNY QGKSQKRSAV EKSINAFLLV YLCILVSKAL
VCTTLKYVWQ STPGQDEPWY NEKTEREKNS NWYLKVFTDF LSFMVLFNFI IPVSMYVTVE
MQKFFGSFFI AWDRDFFDPE IKEGALVNTS DLNEELGQVS PLYVSYGTYN SNCWYRSSAT
YGHYIAQCSG RPSEREELFL RALCLCHTVQ VKESTEQDQS QENVVDQVDG IISDGNVGQP
QQEQRGFIAS SPDEVALVKG AMRYGFTFLG LESKTMKILN NNNDIEKYEL LHVLNFDPVR
RRMSVIVRSK SGDTLLFCKG ADSSIFPRVR PEEVEKICMH VERNATEGYR TLCVAYKILS
ADEYAQADAQ LREARLALQD REEKLTAVYN QVETGMSLIG ATAVEDRLQE QAAETMEALQ
GAGIKVWVLT GDKMETAKST CYACRLFQRN TELLELTVRT LENGERRREE RLHELLLEYH
KKAVEIFFQR SWSSTGQDYG FIIDGATLSM VLNSSSESNA SRYKNLFLQI CQNCTTVLCC
RMAPLQKAQI VRMVKNSKGS PITLSVGDGA NDVSMILEAH VGIGIKGKEG RQAVRNSDYA
IPKLKHLKKL LLAHGHLYYV RIAHLVQYFF YKNLCFILPQ FLYQFFCGYS QQPLYDAAYL
TMYNICFTSM PILAYSLLEQ HISINYLLDN STLYRQIGKN AMLRWRPFLY WTLLGVFHGL
LFFFGVRCLF SNPALQDNGQ VFGNWSYGTI IFTVLVFTVT LKLALDTRHW TWINHFVIWG
SLAFYVFFSF FWGGIIWPFL RQQRLYFVFA NMLSSVSAWL VIILLILLSL LPEILIVVFR
RPRGPHARQV ETKNKPEHTS IRSRSLCLGD AIHERVFPEV GMLSLKDISV AKICGQGTPE
RLLRQC
//
