ID A0A1U8BAA6_NELNU Unreviewed; 1104 AA.
AC A0A1U8BAA6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC104611332 {ECO:0000313|RefSeq:XP_010276647.1,
GN ECO:0000313|RefSeq:XP_010276648.1};
GN ORFNames=HUJ06_000987 {ECO:0000313|EMBL:DAD42757.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010276648.1};
RN [1] {ECO:0000313|EMBL:DAD42757.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:DAD42757.1};
RX PubMed=32343808;
RA Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT "Distinct Expression and Methylation Patterns for Genes with Different
RT Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL Mol. Biol. Evol. 37:2394-2413(2020).
RN [2] {ECO:0000313|RefSeq:XP_010276647.1, ECO:0000313|RefSeq:XP_010276648.1}
RP IDENTIFICATION.
RG RefSeq;
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 -!- 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; DUZY01000006; DAD42757.1; -; Genomic_DNA.
DR RefSeq; XP_010276647.1; XM_010278345.2.
DR RefSeq; XP_010276648.1; XM_010278346.2.
DR STRING; 4432.A0A1U8BAA6; -.
DR GeneID; 104611332; -.
DR KEGG; nnu:104611332; -.
DR eggNOG; KOG0206; Eukaryota.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR Proteomes; UP000607653; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR CDD; cd07536; P-type_ATPase_APLT; 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:SF19; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF08282; Hydrolase_3; 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|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:UP000189703};
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 44..61
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 271..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 814..833
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 839..861
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 891..911
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 923..941
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 948..968
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 988..1007
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 5..70
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 778..1015
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1104 AA; 124693 MW; 7DC9CFB53CF46121 CRC64;
MKRCVYINDN DLSEDLYCDN RISNRKYTVL NFLPKNLWEQ FSRFMNQYFL LIACLQLWPL
ITPVNPASTW GPLIFIFAVS ASKEAWDDYN RYLSDKKANE REVWVVKQGI KRHIKAQDIH
VGNIVWLREN DEVPCDLVLL GTSEQQGVCY VETAALDGET DLKTRTIPAA CMGIASELLH
KIKGVIECPN PDKDIRRFDA NLRLFPPFID NDFCPLTINN TLLQSCYLRN TEWACGVAVY
TGNETKLGMS RGIPEPKLTA VDAMIDKLTG AIFLFQIVVV FVLGIAGNVW KNTEARKQWY
VQYPDEGPWY ELLVIPLRFE LLCSIMIPIS IKVSLDLVKS LYAKFIDWDV EMYDQETSTP
SHAANTAISE DLGQVEYILT DKTGTLTENR MILRRCCING IFYGNESGDA LKDVELLNAV
SNNSPDVIRF LTVMAICNTV VPTKSKSGAI SYKAQSQDED ALVRAASHLH MTFFNKNANI
LEINLNGSII HYELLDTLEF TSDRKRMSVV VKDCQNGKIF LLSKGADEAI LPYACSGQQI
RTFIEAVEHY AQLGLRTLCL AWRELKEDEY REWSLLFKEA NSTLVDREWR LAEVCQRLEH
DLEILGVTAI EDRLQDGVPE TIETLRKAGI NFWMLTGDKQ STAIQIALSC NFISPEPKGQ
LLLITGKTED EVSRSLERVL LTMRITTSEP KDVAFVVDGW ALEIAIKHHR KAFTDLAILS
RTAICCRVTP SQKAQLVEIL KSCDYRTLAI GDGGNDVRMI QQADIGVGIS GREGLQAARA
ADYSIGKFKF LKRLILVHGR YSYNRTAFLS QYSFYKSLVI CFIQILFSFI SGISGTSLFN
SVSLMAYNVF YTSIPVLVSV LDKDLNERTV MQHPQILFYC QAGRLLNPST FAGWFGRSLF
HAIVVFIVSI HAYAYEKSEM EEVAMVALSG CIWLQAFVVA LETNSFTILQ HLAIWGNLAA
FYIINFMVST LPSSGMYTIM FRLCRQPSYW ITMFLIVVAG MGPVFALKYF RYTYRSSAIN
KLQQAERLGG PILSLGNVES QSRTIEKDVA PLSITQSKSR SPVYEPLLSD SASTRRSLGA
TPFDFFQSSQ SRLSSSSYTR NKNN
//
