ID A0A2I4FN33_JUGRE Unreviewed; 1108 AA.
AC A0A2I4FN33;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC109000577 {ECO:0000313|RefSeq:XP_018833042.1};
GN ORFNames=F2P56_022498 {ECO:0000313|EMBL:KAF5458471.1};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018833042.1};
RN [1] {ECO:0000313|EMBL:KAF5458471.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5458471.1};
RA Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA Stevens K., Paul R., Butterfield T., Britton M., Reagan R., Chakraborty S.,
RA Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R., Pratt K.,
RA Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M., Salzberg S.L.,
RA Wegrzyn J.L., Langley C.H., Neale D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF5458471.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5458471.1};
RA Marrano A., Britton M., Zimin A.V., Zaini P.A., Workman R., Puiu D.,
RA Bianco L., Allen B.J., Troggio M., Leslie C.A., Timp W., Dendekar A.,
RA Salzberg S.L., Neale D.B.;
RT "Walnut 2.0.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_018833042.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018833042.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; LIHL02000010; KAF5458471.1; -; Genomic_DNA.
DR RefSeq; XP_018833042.1; XM_018977497.2.
DR EnsemblPlants; Jr10_15340_p1; cds.Jr10_15340_p1; Jr10_15340.
DR GeneID; 109000577; -.
DR Gramene; Jr10_15340_p1; cds.Jr10_15340_p1; Jr10_15340.
DR KEGG; jre:109000577; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000235220; Chromosome 10.
DR Proteomes; UP000619265; 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; cd07536; P-type_ATPase_APLT; 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:SF19; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 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:UP000235220};
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 272..294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 848..865
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 903..920
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 926..944
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 956..973
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 993..1014
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 9..74
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 782..1021
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1108 AA; 125443 MW; B89D0BF1E89F42B7 CRC64;
MLITMKRYVY INDDETSHDL YCDNRISNRK YTLLNFLPKN LWEQFSRFMN QYFLLIACLQ
LWPLITPVNP ASTWGPLIFI FAVSATKEAW DDYNRYLSDM KANEKEVWVV RQGIRKHVQA
QDIHVGNIVW IRENDEVPCD LVLLGTSDPQ GVCYIETAAL DGETDLKTRV IPSACMGIEY
ELLHKIKGVI ECHSPDKDIR RFDANLRLFP PFLDNDLCPL TITNTILQSC YLRNTEWACG
VAVYTGNETK LGMSRGIPEP KLTAVDAMID KLTGAIFIFQ IVVVIVLGIA GNVWKDTEAR
KQWYVHYPME GPWFELLVIP LRFELLCSIM IPISIKVSLD LVKSLYAKFI DWDNKMIDQE
TGTPSHATNT AISEDLGQVE YILTDKTGTL TENKMIFRRC CINGVFYGNE SGDALKDAEL
IDAVSNDSAD VVRFLTVMAI CNTVIPVKSK SGDILYKAQS QDEDALVRAA VQLHMVFVNR
NANILEIKFN ASTIQYEVLE TLEFTSDRKR MSVVVKNCQN GRILLLSKGA DEAIIPYACA
GQQTRAFLEA VEQYTQLGLR TLCLAWRELK EDEYREWSLL LKEASSTLVD REWRIAEVCQ
RLEHDLEILG VTAIEDRLQD GVPETIETLR KAGINFWMLT GDKQNTAIQI ALSCNFISPE
PKGQLLSIDG RTEDEVHRSL ERVLLTMRIT MSEPKDMAFV VDGWALEIAL KYYRKAFTEL
AILSRTAICC RVTPSQKAQL VELLKSCDYR TLAIGDGGND VRMIQQADIG VGISGREGLQ
AARAADYSIG KFRFLKRLIL VHGRYSYNRT AFLSQYSFYK SLLICFIQIF FSFISGVSGT
SLFNSVSLMA YNVFYTSIPV LVSVLDKDLG EETVMQHPQI LFYCQAGRLL NPSTFAGSFG
RSLFHALVVF VISINAYAYE KSEMEEVSMV ALSGCIWLQV FVVILETNSF TTLQHIAIWG
NLVAFYLINW IFSAVPSSGM YTIMFRLCRQ PSYWTTVFLI IAAGMGPILA LKYFRYTYRP
SKINTLQQAE RMGGPILSIG SIEPQPRSLE KDVSPLSITL PKNRNPVFEP LLSDSPNTRR
SFGSGTPFDF FQSPSRLSSS YARNCKDN
//
