ID A0A669DZ44_ORENI Unreviewed; 1335 AA.
AC A0A669DZ44;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=atp10d {ECO:0000313|Ensembl:ENSONIP00000065753.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000065753.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000065753.1}
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 Ensembl; ENSONIT00000053860.1; ENSONIP00000065753.1; ENSONIG00000011353.2.
DR GeneTree; ENSGT00940000156728; -.
DR Proteomes; UP000005207; Linkage group LG19.
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; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF84; PHOSPHOLIPID-TRANSPORTING ATPASE VD; 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:UP000005207};
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 102..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 326..347
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1036..1053
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1065..1085
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1113..1136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1142..1161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1173..1193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1213..1231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 72..126
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1001..1238
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 607..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1335 AA; 150428 MW; 6E12976EA9F0BFF3 CRC64;
IRKINTEIRA VRSHGKLRLM IGDKLTNIIC WKSGLMNSTE QPSCPHATKE HHQKKRTVVP
SFTENEELKE LLQLYKSNKI RTTKYSFLSF LPKNIFEQLH RIANVYFIFL AALNFVPVVE
AFQPEIALVP IVLVLSLTAL KDICEDYRRF KTDHLINGLL CRVYSSTQKS YIDQCWKNVR
VGDFVHLSCN EIIPADMLLL YSSDPRGVCY IETANLDGET NLKQRQVVSD FPLQGEEFTP
ESFHSRIECE NPNNDLSRFR GYMEHSNGVR VGLHSGNLLL RSCTIRNTET VVGIVVYAGH
ETKAMMNNSG PRYKRSKLEK HLNTDILWCV VLLFIMCLTA AIGHGFWMNS FEESIFQVDT
ETSPALAGFY IFWTMVIVLQ VLIPISLYVS IEIVKLGQIY FIHNDLSMYN EQLDSRIQCR
ALNITEDLGQ IQYLFSDKTG TLTENKMVFR CCSIFGVEYP HEENGRNYRV AGATPPPPAH
PGEHQGVPRP QYWVYGESHS PNAPPTSLKP CTITLRTWST LLTPSSMELT YITDFFLALA
ICNSVVVSSP NQPRHVIPEE RTPLKSLEEI KLMFQRFSFS PFSALSPSQI KGSPHSFKSR
LFIRGKREEE EQDVEDQETE DDLRDTQTNP DETRQSMQDL TRQVECVEEI TDELVYEAES
PDEAALVHAA RAYRCTLRGR SAESLLVDLP GIGSLAIQLL HILPFDSNRK RMSVVVRHPL
TGQVVVFTKG ADSVIMDLAE SPTDQTEVYN HIKEKTQKHL DAYAREGLRT LCIAKKVLKE
DEYDLWLKAH MLAESSIENR EELLLESAQR LETNLTLLGS TGIVDRLQEE VPETVAALQR
ARIKVWVLTG DKQETAINIA YACKLLCASD KLLTANCGSK DACAALFEDL ILEVQGGESL
TDLTGNGESM SSSFILVIDG RTLGWALEDE LRSNFLELSQ RCKAVICCRS TPLQKSQVVQ
LIRDHLGVMT LAVGDGANDV SMIQVADVGV GISGQEGMQA VMSSDFAISR FKHLSKLLLV
HGHWCYSRLA NMIQYFIYKN VMYVNLLFWY QFFCGFSGSV MTNSWVLILF NLIFTSAPPL
IYGILDQDLP AVTLMELPEL YQDAQTSKTC VPYMFWITVL DAFYQSLVCF FVPYFAYAGS
DVGVLSFGSP INASALFIIL LHQVIESNTL TWIHVVVLVL SCASYFGFVL LLSGFCVTCS
PPVNPLGIEL LQMSHSLFYI ICVLTTVTAL LPRYTHTHTH THTHTHTHTH THRHTHTKTT
AKTHAHVVYF LWGLDRPVEG PSAELISALL CNEEQEQHCQ QATGVNVSDQ TIRNRLHEGG
GSVMVFVSST QTSTG
//
