ID A0A2I4FAG2_JUGRE Unreviewed; 1191 AA.
AC A0A2I4FAG2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=LOC108997017 {ECO:0000313|RefSeq:XP_018828636.1};
GN ORFNames=F2P56_021367 {ECO:0000313|EMBL:KAF5457252.1};
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_018828636.1};
RN [1] {ECO:0000313|EMBL:KAF5457252.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5457252.1};
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:KAF5457252.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5457252.1};
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_018828636.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018828636.1};
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; KAF5457252.1; -; Genomic_DNA.
DR RefSeq; XP_018828636.1; XM_018973091.2.
DR STRING; 51240.A0A2I4FAG2; -.
DR EnsemblPlants; Jr10_03250_p1; cds.Jr10_03250_p1; Jr10_03250.
DR GeneID; 108997017; -.
DR Gramene; Jr10_03250_p1; cds.Jr10_03250_p1; Jr10_03250.
DR KEGG; jre:108997017; -.
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; 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:SF165; PHOSPHOLIPID-TRANSPORTING ATPASE 8-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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: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 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 301..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 353..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 927..948
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1013..1031
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1051..1074
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1081..1100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1120..1140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 40..102
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 899..1149
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1191 AA; 136286 MW; DCA3F9F99EA1B814 CRC64;
MPEGRRRGIL FSKLYSFACF LSKFEDKHAQ IGRRGYSRVV YCNDPGNPGA VQLKYRGNFV
STTKYTAVNF IPKSLFEQFR RVANIYFLVV ACVSFTPLAP YSAPSVLVPL LVVIGATMAK
EGVEDWRRKK QDIEANNRKV RVYRDYTFHE IKWKKLRVGD LVKVCKDEYF PADIILLSSS
YEDGICYVET MNLDGETNLK LKHALEVTSH LQDEKSFRQF RAVIKCEDPN ENLFSFVGAL
TYDGKEYPLS IKQLLLRDSK LKNTEYIYGV VVFTGHDTKV MQNATDPPSK RSKIEKKMDK
IIYILFSTLI VIASVGSVFF GIETKKDISG GKYRRWYLRP DDSTVFYDPK RSLLAAFLHF
FTALMLYGYL IPISLYVSIE IVKVLQSIFI NQDQDMYDEE TNRPAHARTS NLNEELGQVY
TILSDKTGTL TCNSMEFMKC SIAGTDYGRG TTEVERALMR RRGALSEPGD ASNDVQSHDG
DAMDFRRLIR GFNFRDERIM NGQWVNQPHP DIIQKFFRVL AICHTAIPVV DKESGEIFYE
AESPDEAAFI IAAREVGFEF YGRTQTSISL HELDYETGKK VDRVYELLQV LEFSSARKRM
SVVVRNAENQ LLLLCKGADS VMFERLSQDG RLFESQTRDH IKKYAEDGLR TMVIAYRELG
EEEYKSWDEE FRMAKTSVTV YHDVLVDEAA DKIERNLILL GATAVEDKLQ KGVPECIKKL
SRAGIKIWVL TGDKMETAVN IGYACSLLRQ DMKQIIITLD SPDIDALEKQ GDKEAIAKAS
LESITKQIRE GISQINSAKQ SSNSAKESTI LFGLIIDGKS LDFSLEKNVV KSFFELAINC
SSVICCRSSP KQKARVTRLV KEGTSKTTLS IGDGANDVGM LQEADIGVGI SGVEGMQAVM
ASDYSIAQFR FLERLLLVHG HWCYRRIAMM ICYFFYKNIT FGFTLFWFEA LASFSGQPAY
NDWYMSFYNV FFTSLPVIAL GVFDQDVSAR FCLEYPILYS EGVENILFSW PRILGWMFNG
FISSIIIFFS TTKFMTNQAF RRDGQVLDYE ILGVTMYTCV VWAVNCQMAL SINYFTWIQH
LFIWGSIAFW YIFLIIYGSL PSTISTTAYQ VFVEACAPSV LYWLVTPFVV ICTLLPYFCY
RAFQTRFKPM LHDIIQIKRL EDSETLNTPT LHGQLKDRLL HLRERLMHRE L
//
