ID A0A540L5J8_MALBA Unreviewed; 1184 AA.
AC A0A540L5J8;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-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 ORFNames=C1H46_032659 {ECO:0000313|EMBL:TQD81725.1};
OS Malus baccata (Siberian crab apple) (Pyrus baccata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=106549 {ECO:0000313|EMBL:TQD81725.1, ECO:0000313|Proteomes:UP000315295};
RN [1] {ECO:0000313|EMBL:TQD81725.1, ECO:0000313|Proteomes:UP000315295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shandingzi {ECO:0000313|Proteomes:UP000315295};
RC TISSUE=Leaves {ECO:0000313|EMBL:TQD81725.1};
RA Chen X.;
RT "Sequencing of a Wild Apple (Malus baccata) Genome Unravels the Differences
RT Between Cultivated and Wild Apple Species Regarding Disease Resistance and
RT Cold Tolerance.";
RL G3 (Bethesda) 9:1785-1793(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TQD81725.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VIEB01000753; TQD81725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A540L5J8; -.
DR STRING; 106549.A0A540L5J8; -.
DR Proteomes; UP000315295; 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: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; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF165; PHOSPHOLIPID-TRANSPORTING ATPASE 8-RELATED; 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 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:UP000315295};
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 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 107..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 303..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 958..975
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1005..1023
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1043..1066
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1073..1092
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1112..1132
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 41..106
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 891..1141
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1184 AA; 134946 MW; 19DDACC0821C97B3 CRC64;
MTEGRRRRGI HFSKLYSFSC IRSPFVDSHP QIGERGYSRV VHCNEPDCPE ALQLRYGGNY
VSTTKYTAAN FIPKSLFEQF RRVANIYFLV VACVSFSPLA PFKAVSVLAP LLVVIGATMA
KEAVEDWRRR KQDIEANNRK VRVYGRNYTF YETRWKKLRV GDIVKVHKDE YFPADLLLLS
SSYEDGICYV ETMNLDGETN LKLKHALEVT SHLQDEKSLE NFKAVIKCED PNENLYSFVG
TLFYDGKPYP LSLQQMLLRD SKLKNTEYVY GVVVFTGHDT KVMQNATDPP SKRSKIERKM
DKIIYILFST LVVISFTGSV FFGINTRRDI SGGKMRRWYL RPDHTTVFYD PKRPELAAFF
HFLTALMLYG YLIPISLYVS IEIVKVLQSI FINQDREMYY EEMDRPAHAR TSNLNEELGQ
VDMILSDKTG TLTCNSMEFI KCSIAGTAYG HGITEVERAL ANRRDRVDGL HETGNVSSDV
LDSASYNVDS GKSIKGFNFR DERIMNGQWV NEPHSDIIQK FFRVLAICHT AIPVVDKASG
EITYEAESPD EAAFVIAARE LGFEFFERTQ TNISLHELDF ESGRKVDREY ELLHVLEFSS
SRKRMSVIVR SPENKLLLLC KGADSAILER LAKDGRQFED QTKEHIHRYA EAGLRTLVIA
YRELGVEEFE IWAKEFVKAK ASVTEGRDVL VDGVADKIER DLFLLGVTAV EDKLQKGVPE
CISKLAEAGI KIWVLTGDKM ETAVNIGYAC SLLRQDMKRI VISLDSPDIN ALEKQGDKEA
VGQASLESIR KQIGEGISQI NEAKGSSNQP KSFGLVIDGK SLEFCLKKDV KNSFFELAIT
CASVICCRST PKQKARVTRL VKLGTGKITL SVGDGANDVG MLQEADIGVA VMASDFAIAQ
FRFLERLLLV HGHWCYRRIS MMICYFFYKN ITFGFTLFWF EAYASFSGQP AYNDWYMSFY
NVFFTSLPVI ALGVFDQDVS ARFCLKYPSL YLEGVENILF SWSRILGWMV NGVLSSVIIF
FFTTNSMIGQ ALRKDGKVVD YEVLGVTMYS CVVWVVNCQM ALSINYFTWI QHFFIWGSIA
FWYIFLVIYG SVSPSVSTTA HRVLVEACAP SPLFWMVTLL VTICTLLPYF SYRAFQTRFK
PMRHDVIQQE RLNGSDNETS GELPLRFSSK LQHLKQRLRE RRRS
//
