ID A0A2G9G3U3_9LAMI Unreviewed; 1124 AA.
AC A0A2G9G3U3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=CDL12_27514 {ECO:0000313|EMBL:PIM99982.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIM99982.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
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:PIM99982.1}.
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DR EMBL; NKXS01007239; PIM99982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9G3U3; -.
DR STRING; 429701.A0A2G9G3U3; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000231279; 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:SF180; PHOSPHOLIPID-TRANSPORTING ATPASE 3; 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 Hydrolase {ECO:0000313|EMBL:PIM99982.1};
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:UP000231279};
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 300..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 345..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 986..1007
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1027..1044
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1056..1075
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1095..1118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 41..105
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 875..1124
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1124 AA; 127752 MW; C215D5C37C033389 CRC64;
MAAWRGSRSG GDGLQSVEHI SSSRTVRLGK VQPQAPGHRT VFCNDRDANA LAKFKGNSVS
TTKYDVFTFL PKGLFEQFRR VANLYFLMIS ILSCTPVSPV SPITNVLPLT LVLLVSLIKE
AWEDWKRFQN DMAINNSTIE VLQDQKWVLT PWKKLQVGDI VKVKQDGFFP ADLLFLASTN
PDGICYIETA NLDGETNLKI RKALEKTWDY VTPEKVCEFK GEVQCEQPNN SLYTFTGNLI
INKQTLPLSP NQLLLRGCSL RNTDYIVGAV IFTGHETKVM MNSMKIPSKR STLEKKLDKL
ILTLFCVLFC MCLLGAIGSG VFINRKYYYL RFDKSEKQFD PDNRFVVAIL TFFTLITLYS
PIIPISLYVS VEMIKFIQST QFINNDLSMY HAESNTPALA RTSNLNEELG QVEYIFSDKT
GTLTRNLMEF FKCSIGGEVY GTGVSEIEMG TAQRTGAKIE TQKQSNTARE KGFNFDDARL
MRGAWRNEPN PEACKEFFKC LAICHTVLPE GDESPEKIRY QAASPDESAL VTAAKNFGFF
FYKRSPTTIY VRESHVEKMG KVQDVPYEIL NVLEFNSTRK RQSVVCRYPD GRLVLYCKGA
DTVIYERLVD GDNELKRITR EHLEQFGASG LRTLCLAYRN LSSDVYESWN EKYIQAKSSL
RDREKKLDEV AELIEKELIL IGCTAIEDKL QEGVPACIET LSRAGIKIWV LTGDKMETAI
NIAYACKLIN NSMKQFIISS ETDAVREIED RGDQVELARF MKELVKNELK RCNEEAQQYL
LSVPRSKLAL VIDGKCLMYA LDPSLRVMLL NLSMNCSAVV CCRVSPLQKA QVTSLVRKGA
NRITLSIGDG ANDVSMIQAA HVGVGISGQE GMQAVMASDF AIAQFRFLTD LLLVHGRWSY
HRICKVVTYF FYKNLTFTLT QFWFTFQTGF SGQRLYDDWF QSLYNVIFTA LPVIIIGLFD
KDVSATLSKQ YPELYKEGIR NAFFKWRVVA TWAFFAIYQS LVLYYFVVAS SNRAINSSGK
MFGLWDVSTM AFTCVVVTVN LRLLMMCNTI TRWHHISVGG SILAWFVFVF IYSGVILPKE
QENIYLVIYV LMSTFYFYFA LILVPVAALF CDFVYLGVQR WFFP
//
