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Database: UniProt
Entry: A0A078GLL5_BRANA
LinkDB: A0A078GLL5_BRANA
Original site: A0A078GLL5_BRANA 
ID   A0A078GLL5_BRANA        Unreviewed;      1228 AA.
AC   A0A078GLL5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=BnaC06g10670D {ECO:0000313|EMBL:CDY26129.1};
GN   ORFNames=GSBRNA2T00034772001 {ECO:0000313|EMBL:CDY26129.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY26129.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY26129.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
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; LK032185; CDY26129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078GLL5; -.
DR   STRING; 3708.A0A078GLL5; -.
DR   PaxDb; 3708-A0A078GLL5; -.
DR   EnsemblPlants; CDY26129; CDY26129; GSBRNA2T00034772001.
DR   Gramene; CDY26129; CDY26129; GSBRNA2T00034772001.
DR   OMA; LICCRIS; -.
DR   Proteomes; UP000028999; 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; 2.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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:SF149; PHOSPHOLIPID-TRANSPORTING ATPASE 6; 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:UP000028999};
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        87..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        109..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        306..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        355..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        938..956
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        968..987
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1017..1041
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1053..1073
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1085..1104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1124..1143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          44..112
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          903..1153
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1228 AA;  138741 MW;  4E98A24F13C4BA8B CRC64;
     MARRHRIRSR IRKSHFYTFR CLRPKTLDDQ GPHVINGPGY TRIVHCNQPH LHLATKLLRY
     RSNYVSTTRY NMLTFLPKCL YEQFHRVANF YFLVAAILSV FPLSPFNKWS MIAPLVFVVG
     LSMGKEALED WRRFMQDVGV NSRKASVHKG NGEFGRRTWK KLRVGDVVRV EKDEFFPADL
     FLLSSSYEDG ICYVETMNLD GETNLKVKRC LDATLSLEKD ESFQSFSGTI KCEDPNPNLY
     TFVGNLECDG QVYPLDPNQI LLRDSKLRNT SYIYGVVVFT GHDTKVMQNS TKSPSKRSSI
     EKTMDYIIYT LFGLLLFVSV ISSLGFAVMT KLLMADWWYL RPDKPESLTN PTNPLYAWVV
     HLITALLLYG YLIPISLYVS IELVKVLQAT FINHDLQMYD SESGTPAEAR TSNLNEELGQ
     VDTILSDKTG TLTCNQMDFL KCSIAGTSYG VRASEVELAA AKQMEMDLEE QGDDITNLPM
     TKTSSGFELE TVITASDEKD QKKSSGIKGF SFEDKRLMDD NWVNEPNSDD VLMFFRILAV
     CHTAIPEVDE DNGKCTYEAE SPDEVAFLVA SREFGFEFTK RTQSSVFIAE RFSPSGHPVD
     REYKVLNLLD FTSKRKRMSA IIRDEEGQIL LLCKGADSII FDRLSKKRKD YLGATSKHLN
     EYGEAGLRTL ALGYRKLDEA EYAAWNSEFH KAKTSVGADR DELLEKVSDM MEKELILVGA
     TAVEDKLQKG VPQCIDNLAQ AGLKIWVLTG DKMETAINIG YACSLLRQGM KQIAISFTNV
     EESSQNSEAA VKQNILMQIT NASQMIKIEK DPHAAFALII DGKTLTYALK DDVKYQFLAL
     AVACASVICC RVSPKQKALV TRLAKEGTGK TTLAIGDGAN DVGMIQEAHI GVGISGVEGM
     QAVMASDFSI AQFRFLERLL VVHGHWCYKR IAQMICYFFY KNIAFGLTLF YFEAFTGFSG
     QSIFNDSYLL LFNVVLTSLP VISLGVFEQD VPSDVCLQFP ALYQQGPKNL FFDWYRILGW
     MGNGVYASIV IFALNLGIFH VQSFRSDGQT ADMNAMGTAM FTCIIWAVNV QIALTMSHFT
     WIQHVMIWGS IGAWYIFLAL YGMLPPKLSG NIFHMLIEVL APAPIFWLTN LLVIAATTLP
     YLFHISYQRS VNPLDHHIIQ EIKHFRIDLE DERMWKREKS KAREKTKIGF TARVDAKIRQ
     LRVKLHRKHS VLSVISGTSS NDTASNMI
//
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