ID A0A2G5D9Q1_AQUCA Unreviewed; 1085 AA.
AC A0A2G5D9Q1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=AQUCO_02500157v1 {ECO:0000313|EMBL:PIA40259.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA40259.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA40259.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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; KZ305042; PIA40259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5D9Q1; -.
DR Proteomes; UP000230069; 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; 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:UP000230069};
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 297..320
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 343..367
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 945..966
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 987..1006
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1026..1043
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1055..1074
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 38..102
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 874..1078
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 122959 MW; 7304508FECFC6316 CRC64;
MSGGGWQKVK SSKKDRQPSS RTVRLGRVQP QAPTSRTIFC NDRDANLPVK FKGNSVSTTK
YSILTFLPKG LFEQFRRVAN LYFLMISILS TTPISPVSPI TNVLPLSLVL LVSLIKEAFE
DWKRFQNDRV INGSLIDVLQ DQNWVKMPWR RLQVGDIVRI NQDGFFPADL LFLASSNADG
VCYTETANLD GETNLKIRKA LERTWDYLTP DKASEFKGEV QCEQPNNSLY TFTGNLIIQK
QTLPLSSNQI LLRGCSLRNT EYIVAAVIFT GHETKVMMNS MNVPSKRSTL ERKLDKLILT
LFATLFLMCF IGAIGSGVFI NRKYYYLGLD ESVEKQFNPN NRIVVAILTM FTLITLYSTI
IPISLYVSIE MIKFIQSTQF INKDLNMYHV ETNTPASART SNLNEELGQV EYIFSDKTGT
LTRNLMEFFK CSIGGDVYGT GITEIEIGGA QRNGMKVEEI PKLAAAIHEK GFNFDDARLM
RGAWKNEPNP EICKEFFRCL AICHTVLPEG DESPEKIAYQ AASPDEAALV TAAKNFGFFF
YRRTPTSIMV RESHVEKMGK IQDVTYEILN VLEFNSTRKR QSVICRYPDG RLVLYCKGAD
TVIYERLADG NNDLRNLSRE HLEQFGSAGL RTLCLAYRDL NMDLYESWNE KFIQAKSSLR
DREKKLDEVS ELIEKDLCLI GCTAIEDKLQ EGVPSCIETL SRAGIKIWVL TGDKMETAIN
IAYACSLINN SMKQFIISSE TDAIRDVESR GDQVEIARFM RDTVKQELKK CLEEAQHSLL
TLSGPKLALI IDGKCLMYAL DQALRKSLLE LSLNCNSVVC CRVSPLQKAQ VTSLVKKGAR
KITLSIGDGA NDVSMIQAAH VGVGISGLEG MQAVMASDFA IAQFRFLSDL LLVHGRWSYL
RICKVVTYFF YKNLTFTLTQ FWFTFQTGFS GQRFYDDWFQ SLYNVIFTAL PVIIVGLFDK
DVSAALSKKY PQLYMEGIRN NFFKWRVVAV WAVFSVYQSL VFFYFVTASG QRGHNPSGRM
FGLWDVSTMG FTCVVITVNI RLLMACNSIT RWHHISIWGS ILAWFVFIFI YSGITTPWDR
QVSTF
//
