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Database: UniProt
Entry: B9GK47_POPTR
LinkDB: B9GK47_POPTR
Original site: B9GK47_POPTR 
ID   B9GK47_POPTR            Unreviewed;      1255 AA.
AC   B9GK47;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=POPTR_001G081200 {ECO:0000313|EMBL:PNT53361.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT53361.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNT53361.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
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; CM009290; PNT53361.1; -; Genomic_DNA.
DR   RefSeq; XP_002297933.1; XM_002297897.1.
DR   AlphaFoldDB; B9GK47; -.
DR   STRING; 3694.B9GK47; -.
DR   EnsemblPlants; Potri.001G081200.1.v4.1; Potri.001G081200.1.v4.1; Potri.001G081200.v4.1.
DR   GeneID; 7477805; -.
DR   Gramene; Potri.001G081200.1.v4.1; Potri.001G081200.1.v4.1; Potri.001G081200.v4.1.
DR   KEGG; pop:7477805; -.
DR   eggNOG; KOG0206; Eukaryota.
DR   HOGENOM; CLU_000846_5_2_1; -.
DR   InParanoid; B9GK47; -.
DR   OMA; FYPMDDH; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000006729; Chromosome 1.
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: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; 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:UP000006729};
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        363..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        958..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        990..1010
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1040..1061
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1081..1101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1108..1127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1149..1170
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          926..1176
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1255 AA;  143033 MW;  7980DC4325D3EE7D CRC64;
     MHGSSRRTKG KVRWSKLYSF SCFRPHTSDP DSAQELIGQP GFSRVVFCNE PQVHKRKPYK
     YTNNSVSTKK YTAVTFLPKA LFEQFRRVAN LYFLLTAALS ITSLAPVKPV SLIAPLVFVV
     GISMLKEAVE DWYRFLQDLN VNTRTVKAHA GNGLFVDKLW REISVGDVVK VNKDEYFSSD
     LLLLSSSYED GVCYVETMNL DGETNLKIKR CLEVTLDLNE DAKFSEFKAT TRCEDPNPSL
     YTFVGNLEFE NKIYPLSPSQ ILLRDSKLRN TDYVYGAVIF SGHDTKVVRN STMSPSKRSR
     LEKKMDKVIY LLFSMLLLIS LVTSIGSAVV IKSDMSQWWY LSLEDSDPLF DPSNPLKSGF
     LQFIRALILY GYLIPISLYV SIEIVKVLQA KFINKDKKMY DEATCKSVQA RTSNLNEELG
     QVEIILSDKT GTLTCNQMEF RKCSIAGISY GGNINEVDIA ASKRMNTDIE AYRSSIDQSD
     TTSQSLEMSE FSVADIITQE AILRGQENAD NLNARNSRLS DVRKESVIRV IKGFNFRDDR
     LMNNQWIYRS DLFDMTMFFR VMALCHTGIP VEDGQTDKLK YEAESPEEVA FLIASQEFGF
     QFFQRTQSLM TLKELDPSSG KQVKREYKLL NLLEFSSFRK RMSVIVRDED GKIYLLCKGA
     DSIIFDRLAD NGGAYQEATT SHLSNYAEDG FRTLAFAYRV LELAEYEQWN SIFMQAKTTV
     GPEREELLEH ATEMIEKELI LLGVAAVEDK LQKGVVECID KLAQAGMKIW LLTGDKKETA
     INIGFSCSLL RQDMKQFHVC LSKETESKNQ LKAMKEEILH QIESSYQVMC QDSNKYSPFA
     LVLDGRALEI ALKSDVRDQF LQLAVNCASV ICCRVSPKQK ALITRLVKEY TGKTTLAIGD
     GANDVGMIQE ADIGVGISGM EGMQAVMASD FSLPQFRFLE RLLIVHGHWC YKRISKMVLY
     FVYKNIAFGL TLFYYEIFTN FSGDSLYDDW YMVMFNVLLT SLPVISLGVF EQDVSSDVCL
     QFPSLYRQGQ RNIIFSWSRI VGWILNGTVA ASVVFLANIY IFSPAAFRQE GNVADITHFG
     AIMYTCIIWT VNCQIALIIT HFTWIQHLFI WGSILLWYIF AVAYGALPPD YSQRGFNIIT
     ESIGSTPKYW IATFLVIVVA LLPYFTHIAF QRLLYPMDDH IIQEMKHCKK DVTENQMWLR
     EQRNSQRSTQ VGFSARVDAR IRSFKEGLSL KRISIYKSVT NTPFYKSWTS SPIFS
//
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