ID A0A1U8AU92_NELNU Unreviewed; 1227 AA.
AC A0A1U8AU92;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC104604173 {ECO:0000313|RefSeq:XP_010266737.1};
GN ORFNames=HUJ06_030629 {ECO:0000313|EMBL:DAD29161.1};
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_010266737.1};
RN [1] {ECO:0000313|EMBL:DAD29161.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:DAD29161.1};
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_010266737.1}
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; DUZY01000002; DAD29161.1; -; Genomic_DNA.
DR RefSeq; XP_010266737.1; XM_010268435.2.
DR STRING; 4432.A0A1U8AU92; -.
DR GeneID; 104604173; -.
DR KEGG; nnu:104604173; -.
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; 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:SF91; 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 PRINTS; PR00121; NAKATPASE.
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: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 187..205
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 382..404
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 439..460
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 987..1006
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1018..1035
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1064..1086
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1098..1115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1122..1142
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1162..1181
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 122..188
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 951..1191
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 29..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 137835 MW; 5B0B4942286440BA CRC64;
MASERPLLIP SPQTLNTQNR HIAMSTFADL IKSTPRNPDP STSSRMDRSD LVENSSHEGV
SALKSSSVRS ISSIQSKESV TFTVDSFRGS GSKPVRYGSG RTESEGFGSS QKEISDEDAR
LVYINDPLRT NERFEFAGNS IRTGKYSVLT FLPRNLFEQF HRVAYIYFLV IAILNQLPQL
AVFGRGASIL PLAFVLLVTA VKDAYEDWRR HRSDRIENNR LASVLVNGQF QTKRWADIRV
GETLMVSANE TLPCDMVLLS TSDQTGVAYV QTLNLDGESN LKTRYAKQET LSKMPEKEGI
NGLIKCERPN RNIYGFHANM EIDGKRLSLG PSNIILRGCE LKNTAWAVGV AVYAGRETKV
MLNSSGAPSK RSRLETRMNR EIILLSFFLI TLCSIVSIFA GIWLRHHRDE LDTSPYYRRK
DYSEGNIENY NYYGWGWEIF FTFLMSVIVF QIMIPISLYI SMELVRLGQA YFMIRDTTLY
DETTNSRFQC RALNINEDLG QIKYIFSDKT GTLTENKMEF RCASIWGVDY SGARNLMPGE
QDGYSVKVDG KIWRPKMTVK ADPELQWLLR NGQKTEEGKR AYDFFLALAA CNTIVPLVTE
TSDPAVRLVD YQGESPDEQA LVYAAATYGF MLLERTSGHI IIDVNGERQR FNVLGLHEFD
SDRKRMSVIV GCPDNMVKVF VKGADTSMFG VIDRSLGLEV IRSTESHLHA YSSLGLRTLV
VGMRELNVSE FEQWQSAYEK ASTSLMGRAS LLRAVAGKVE NNLCILGASG IEDKLQQGVP
EAIESLKQAG IKVWVLTGDK QETAISIGYS CKLLTSRMTQ IIINSTSKES CRKSLEDAKA
MSKHLLGIST QNGGSGVLPT KVPLALIIDG TSLVYVLDSE LEDELFQLAT KCSVVLCCRV
APLQKAGIVA LIKNRTDDMT LAIGDGANDV SMIQMADVGI GISGQEGRQA VMASDFAMGQ
FRFLVPLLLV HGHWNYQRMG YMILYNFYRN AVFVLILFWY VLYTAFSLTT AITEWSSVLY
SIIYTSLPTI IVGILDKDLS RRTLLKYPQL YAAGQRRECY NLKLFWLTMT DTVFQSVVVF
FVPFLAYRQS TVDGSSIGDL WTLAVVILVN IHLAMDVIHW TWVTHVVIWG SILATFICVI
IIDVIPTLPG YWAIFDIAKT GLFWLCLLAI LVAAVVPRFV VKVSSQYFSP SDVQIAREAE
KFGIPQEFER TEVEMNPILD HPREMTR
//
