ID A0A443PT20_9MAGN Unreviewed; 1203 AA.
AC A0A443PT20;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=CKAN_02321800 {ECO:0000313|EMBL:RWR93940.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR93940.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR93940.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR93940.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(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:RWR93940.1}.
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DR EMBL; QPKB01000010; RWR93940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443PT20; -.
DR STRING; 337451.A0A443PT20; -.
DR Proteomes; UP000283530; 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; 1.
DR PANTHER; PTHR24092:SF175; PHOSPHOLIPID-TRANSPORTING ATPASE 9-RELATED; 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:UP000283530};
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 82..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 106..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 302..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 357..378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 925..942
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 954..974
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1004..1026
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1072..1091
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 42..106
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 890..1140
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 462..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1203 AA; 136006 MW; EF5791444C150AC9 CRC64;
MSGVRRRRVH FSKIYNFTCG KSSFREEHSN IGGPGFSRVA FCNDPNCFEA GIHNYDTNYV
STTKYTLATF IPKSLFEQFR RVANFYFLVV GCLSFTPLAP YSAVSALLPL IVVIGATMAK
EAVEDYRRKK QDIEVNNRKV KVHRGDGTFE NTEWKNLRVG DIVKVEKDEF FPADLLLLSS
SYEDAICYVE TMNLDGETNL KLKQALEVTS GLQDDSSFRE FKALVKCEDP NANLYSFVGS
MDFEEQQYPL SPQQLLLRDS KLRNTDYIYG AVIFTGHDTK VLQNSTEPPS KRSRIERKMD
RIVYFLFGLL FLLSMVGSIF FGIWTREDLR DGKMKRWYLR PDDTTIYFNP KKSAAAAVLH
FLTALMLYSY FIPISLYVSI EIVKVLQSIF INQDVRMYYE EADKPAHART SNLNEELGQV
DTILSDKTGT LTCNSMEFIK CSVAGTAYGR GVTEVERAMA RRKGSPLVEE EENGDHVDDQ
ADAKPSVKGF NFKDERIMNG KWIDEPHADV IQKFFRVLAI CHTAIPEVDE EMGKVAYEAE
SPDEAAFVIA ARELGFEFYK RTQTSISLHE LDLVSGKKVE RSYDLLNILE FSSARRRMSV
IVRNEEGQLL LLCKGADSVM FERLAKNGKD FENQTKEHLN GYADAGLRTL VLAYRELHEQ
EYMEFNNAFN EAKNSVSADR DARIDEITET IEKDLILLGA TAVEDKLQNG VPECIDKLAQ
AGIKIWVLTG DKMETAINIG FACSLLRQGM KQIIINLETP QILALEKEGD KNAIAKASKA
SVVEQIHNGK SLLSSRSGSS DAFALIIDGK SLTYALEDDV KNMFLDLAIG CASVICCRSS
PKQKALVTRL VKAGTGKTTL AIGDGANDVG MLQEADIGIG ISGVEGMQAV MSSDIAIAQF
RFLERLLLVH GHWCYRRISS MVCYFFYKNI TFGFTLFLFE AYASFSGQPA YNDWYLSLYN
VFFTSLPVIA LGVFDQDVSA RFCLKFPLLY QEGVQNVLFS WLRIVSWMFN GVLSSIIIFF
FCTNAFEHQA FRKGGEVVGI EILGTTMYTC VVWVVNCQMA LSVSYFTLVQ HIFIWGGIAL
WYLFLLAYGA ITPSISTTAY KVFIEACAPA ASYWLVTLCV VISTLIPYFA YSAIQMRFFP
MYHGMIQWIR YEGQAEDPEY CHMVRQRSLR PTTVGFTARA EARRSRTKER VHRTTELVEE
LGR
//
