ID A0A4U5P4R4_POPAL Unreviewed; 1390 AA.
AC A0A4U5P4R4;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-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=D5086_0000231520 {ECO:0000313|EMBL:TKR90661.1};
OS Populus alba (White poplar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=43335 {ECO:0000313|EMBL:TKR90661.1, ECO:0000313|Proteomes:UP000309997};
RN [1] {ECO:0000313|Proteomes:UP000309997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PAL-ZL1 {ECO:0000313|Proteomes:UP000309997};
RX PubMed=30661181; DOI=10.1007/s11427-018-9455-2;
RA Liu Y.-J., Wang X.-R., Zeng Q.-Y.;
RT "De novo assembly of white poplar genome and genetic diversity of white
RT poplar population in Irtysh River basin in China.";
RL Sci. China Life Sci. 62:609-618(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:TKR90661.1}.
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DR EMBL; RCHU01000853; TKR90661.1; -; Genomic_DNA.
DR STRING; 43335.A0A4U5P4R4; -.
DR Proteomes; UP000309997; 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:SF157; 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:UP000309997};
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 308..331
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 360..382
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 942..962
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 974..994
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1024..1045
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1065..1086
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1093..1113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1133..1154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 46..112
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 910..1160
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1230..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1390 AA; 157970 MW; C3911729B10911D5 CRC64;
MHGSSRRTKG KIRWSKLYSF SCFRPHTSDP DSAQELIGQP GFSRVVFCNE PQVHKRKPYK
YTNNSVSTKK YTAVTFLPKA LFEQFRRVAN LYFLLTAALS ITSLAPVKPV SLIAPLVFVV
GISMLKEAVE DWYRFLQDLN VNTRTVKAHA GNGLFVDKLW REISVGDVVK VNKDEYFSSD
LLLLSSSYED GVCYVETMNL DGETNLKIKR CLEVTLDLNE DAKFSEFKAT TRCEDPNPSL
YTFVGNLEFE NKVYPLSPSQ ILLRDSKLRN TDYVYGAVIF SGHDTKVVRN STMSPSKRSR
LEKKMDKVIY LLFSMLLLIS LITSIGSAVV IKSDMSQWWY LSLEDSDPLF DPSNPLKSGF
LQFIRALILY GYLIPISLYV SIEIVKVLQA KFIDKDKKMY DEATCKSVQA RTSNLNEELG
QVEIILSDKT GTLTCNQMEF RKCSIAGISY GGNINEVDIA ASKRMNTGID AYRSSIDQSD
TTSQSLEMSE FSVADIITQQ AILRGQENAD NLNVIKGFNF RDDRLMNNQW IYRSDLFDMT
MFFRVMALCH TGIPVEDGQT DKLKYEAESP EEVAFLIASQ EFGFQFFQRT QSLMTLKEHD
PSSGKQVKRE YKLLNLLEFS SSRKRMSVIV RDEDGKIYLL CKGADSIIFD RLADNGGAYQ
EATTSHLSNY AEDGFRTLAF AYRVLELAEY EQWNSIFMQA KTTVGPEREE LLEHATEMIE
KELILLGVAA VEDKLQKGVI ECIDKLAQAG MKIWLLTGDK KETAINIGFS CSLLRQDMKQ
FHVCLSKETE SKNQLKAMKE EILHQIESSY QVMCQESKKY SPFSLVVDGR ALEIALKSDV
RDQFLQLAVN CASVICCRVS PKEKALITRL VKEYTGKTTL AIGDGANDVG MIQEADIGVG
ISGMEGMQAV MASDFSLPQF RFLERLLIIH GHWCYKRISK MVLYFVYKNI AFGLTLFYYE
IFTNFSGDSL YDDWYMVMFN VLLTSLPVIS LGVFEQDVSS DVCLQFPSLY RQGQRNIIFS
WSRIVGWILN GTVAASVVFL ANIYIFSPDA FRQEGNVADI THFGVIMYTC IIWTVNCQIA
LIITHFTWIQ HLFIWGSILL WYIFAIAFGA LPPDYSQRGF NIITESIGSA PKYWIATFLV
IVVALLPYFT HIAFQRLLYP MDDHIIQEMK HCKKDVTENQ MWLREQRNSQ RSTQVGFTAR
VDARIRSFKE GLSLKRISIY NLLGFSRNLK TQPPPSSPPP AAAYGAKDSQ ALSHMDNRQD
ILGNNSPEVI RWLCNLSASE LDMLIRLKSL ILHRAKVLGH DELAKNFDLP TLRAIGLFLM
EYLKGKFKDL SQVQGLTKLV VFPECCNLLK GNPGEDSSME ELKACIGIDE RKRPTERPGE
EATKQKKQRL
//
