ID A0A061E5H9_THECC Unreviewed; 1226 AA.
AC A0A061E5H9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=TCM_010087 {ECO:0000313|EMBL:EOY00260.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY00260.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY00260.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001880; EOY00260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061E5H9; -.
DR STRING; 3641.A0A061E5H9; -.
DR EnsemblPlants; EOY00260; EOY00260; TCM_010087.
DR Gramene; EOY00260; EOY00260; TCM_010087.
DR eggNOG; KOG0206; Eukaryota.
DR InParanoid; A0A061E5H9; -.
DR OMA; MHSFWSW; -.
DR Proteomes; UP000026915; Chromosome 2.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; 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:0048194; P:Golgi vesicle budding; IBA:GO_Central.
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:SF180; PHOSPHOLIPID-TRANSPORTING ATPASE 3; 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:UP000026915};
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 305..328
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 351..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 913..931
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 951..970
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 991..1014
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1029..1048
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1060..1082
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1094..1118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 45..110
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 882..1132
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 139650 MW; 64083165BEF7A082 CRC64;
MSGWDRVRSS TRSQQDRSQN STQRAPSRTV TLGRVQPQAP SFRTIYCNDR EANYAHRFKG
NSISTTKYNF FTFLPKGLYE QQFRRVANLY FLMVSILSAT PYSPVHPVTN VVPLSLVLLV
SLVKEAFEDW KRFQNDMAIN NTLVDVLQDQ RWESIPWKRL QVGDIVRVKQ DGFFPADVLL
LASSNPDGVC YIETANLDGE TNLKIRKALE RTWDYLTPEK ACEFKGEMQC EQPNNSLYTF
TGNLVMDNQT LPLSPNQILL RGCSLKNTEF IVGAVIFSGH ETKVMMNSMN VPSKRSTLER
KLDKLILTLF GTLFTMCLIG AIGSGVFIDR KYYFLGLSKS VEDQFNPNNR FLVALLTMLT
LLTLYSTIIP ISLYVSIEMI KFIQSTQFIN KDLNMYHAET DTPALARTSN LNEELGQVEY
IFSDKTGTLT RNLMEFFKCS IGGEIYGTGM TEIERGVAER KGIKIQEVQT STNSIHEKGF
NFDDVRLMRG AWRNEHNPDA CKEFFRCLAI CHTVLPEGDE SPEKIKYQAA SPDEAALVLA
AKNFGFFFYR RTPTMIYVRE SHVERMGKIQ DVSYEILNVL EFNSTRKRQS VVCRYPDGRL
VLYCKGADTV IYERLVGGGD DLKKVTREHL EQFGSAGLRT LCLAYKDLAP DMYESWNEKF
IQAKSSLRDR EKKLDEVAEL IEKDLVLIGA TAIEDKLQEG VPNCIETLSR AGIKIWVLTG
DKMETAINIA YACNLLNNEM KQFIISSDTD AIRAVEERGD QVEIARFIKE EVKKQLKKCL
DEAQQYFNTV SGPKLALIID GKCLMYALDP SLRIMLLTLS LNCSSVVCCR VSPLQKAQVT
SLVKKGARKI TLSIGDGAND VSMIQAAHIG VGISGLEGMQ AVMASDFAIA QFRFLTDLLL
VHGRWSYLRL CKVVTYFFYK NLTFTLTQFW FTFNTGFSGQ RFYDDWFQSL YNVIFTALPV
IIVGLFDKDV SSSLSKKYPE LYKEGIRNMF FKWRVVAIWA FFAVYQSLVF YHFVTVSSST
SQGSSGKMFG LWDVSTMAFT CVVVTVNLRL LMICNSITRW HYISVGGSIL AWFLFIFLYS
GIMTPYDRQE NVFWVIYVLM STFYFYITLL LVPVAALLGD FLYQGVQRWF FPYDYQIVQE
IHKDEADDTG RTDLLEIGSQ LTPDEARSFA ISQLPREISK HTGFAFDSPG YESFFASQLG
IYAPQKAWDV ARRASMKSKP KTNKKN
//
