ID A0A0C7N3R5_9SACH Unreviewed; 1315 AA.
AC A0A0C7N3R5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=LALA0_S14e00166g {ECO:0000313|EMBL:CEP64826.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP64826.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP64826.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP64826.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
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 EMBL; LN736373; CEP64826.1; -; Genomic_DNA.
DR STRING; 1245769.A0A0C7N3R5; -.
DR HOGENOM; CLU_000846_3_0_1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000054304; Unassembled WGS sequence.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR GO; GO:0045332; P:phospholipid translocation; IEA:UniProt.
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; 2.
DR PANTHER; PTHR24092:SF214; PHOSPHOLIPID-TRANSPORTING ATPASE; 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|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|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000054304};
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 447..469
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 497..518
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1017..1036
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1048..1069
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1089..1117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1137..1154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1161..1180
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1200..1219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 186..252
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 981..1233
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1315 AA; 148461 MW; 37CF7C09680382E6 CRC64;
MNKTGRRSNE DTLFDIDFLN DEFTPTFDGH GGTNGNNTNP FESQIVDSDF DLLNNLRHGA
VPQETVNLNR ESTELRHGDN IENDVVENPF VDETYSQSLR NQRSVKLSAK NSSRFGRAFR
RLKSGLSFGK NGSNEYQGFE MHNYDDLGQE DRYARSRNRF NIKILFNRYI LRRPEEGAEA
GAPRIIYLNN REANIAHGFN DNHISTTKYN LATFLPKFLF QEFSKYANLF FLFTSAIQQV
PNVTPTNRYT TIGTLLIVLI VSAVKESVED LKRAASDREL NDSGALVYSE QLHDFTTSKW
VNISVGDIIK IKSEEAIPAD IILISSSEPE GLCYIETANL DGETNLKIKQ ARVETSKNIE
AAQLATITGK VVSEQPNSSL YTYEGTLNLK GKDIPLTPEQ LILRGATLRN TAWVYGLVVF
TGHETKLMRN ATATPIKRTA VERVINMQIL ALFGVLIVLA LISSIGNVIK VTSDAKHLTY
LYLEGTNKVG LFFKDILTYW ILFSNLVPIS LFVTVEMIKY YQAYMISSDL DLYDEKTDTP
TVVRTSSLVE ELGQIEYIFS DKTGTLTRNV MEFKSCSIAG KCYIETIPEE SGARLEDGIE
VGFRKFEDMT TTLGEVDDPE SHVINSFLTL LATCHTVIPE FQDDGSIKYQ AASPDEGALV
EGAAMLGYKF IIRKPNSVTI VIESTGTEQV YELLDICEFN STRKRMSGIF RMPDGQIKLF
CKGADTVILE RLRANDNPYV EATVRHLEDY AAQGLRTLCL AMRTVSESEY ANWKTLYNEA
STTLDDRAAK MDETAELIEK DLFLIGATAI EDKLQDGVPE TIHTLQDAGI KIWVLTGDRQ
ETAINIGMSC RLLSEDMNLL IVNEDTKEAT RRNLLEKLKA IGDHQISQQE INSLALVIDG
KSLGFALESD LEEYLLAVGK ICKAVICCRV SPLQKALVVK MVKRRTNSLL LAIGDGANDV
SMIQAAHIGV GISGMEGMQA ARSADFAIGQ FKFVKKLLLV HGSWSYQRIS QAILYSFYKN
IALYMTQFWY VFANAYSGQS IMESWTMTFY NVFFTVLPPF VMGVFDQFVS SRLLDRYPQL
YKLGQKGQFF SVTIFWGWVA NGFYHSAVTF LGSYLIYGPG NVLNSHGETA DHWTWGVAIY
TCSIIIVIGK AALVTNQWTK FTAFAIPGSL AFWLVFFPIY ASIFPHANVS REYYGIVPHV
YGSGTFWLMC IVLPFFALLR DFVWKYYKRT YTPESYHVVQ EMQKYNIGDY RPRIEHFQKA
IRRVRQVQRM KKQRGFAFSQ SEFGGQDKVI RMYDTTLKRG IHGELQDASA NPFHD
//
