ID A0A4Y7KRI6_PAPSO Unreviewed; 1211 AA.
AC A0A4Y7KRI6;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=C5167_050244 {ECO:0000313|EMBL:RZC74768.1};
OS Papaver somniferum (Opium poppy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Papaver.
OX NCBI_TaxID=3469 {ECO:0000313|EMBL:RZC74768.1, ECO:0000313|Proteomes:UP000316621};
RN [1] {ECO:0000313|EMBL:RZC74768.1, ECO:0000313|Proteomes:UP000316621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HN1 {ECO:0000313|Proteomes:UP000316621};
RC TISSUE=Leaves {ECO:0000313|EMBL:RZC74768.1};
RX PubMed=30166436; DOI=.1126/science.aat4096;
RA Guo L., Winzer T., Yang X., Li Y., Ning Z., He Z., Teodor R., Lu Y.,
RA Bowser T.A., Graham I.A., Ye K.;
RT "The opium poppy genome and morphinan production.";
RL Science 362:343-347(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}.
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DR EMBL; CM010722; RZC74768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y7KRI6; -.
DR STRING; 3469.A0A4Y7KRI6; -.
DR EnsemblPlants; RZC74768; RZC74768; C5167_050244.
DR Gramene; RZC74768; RZC74768; C5167_050244.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000316621; Chromosome 8.
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:SF175; PHOSPHOLIPID-TRANSPORTING ATPASE 9-RELATED; 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 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:UP000316621};
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..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 104..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 302..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 355..378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 927..944
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 956..976
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1006..1028
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1040..1062
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1074..1093
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1113..1133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 41..106
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 892..1142
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1211 AA; 137183 MW; 1AD9C881723DC95C CRC64;
MSGVGRKKLQ LSKIYAFHCG KASFVEDHSQ IGGPGFSRVV FCNEPYSFDA SLRNYGSNYI
RTTKYTLATF FPKSLFEQFR RVANIYFLIA ACLSFTSLSP YTPISAVLPL VVVIGATMIK
EAVEDWRRKS QDNEVNNRTV KVHQSDGVFD YTTWKNLRVG DVVKVENDEY FPADLLLLSS
SYEDAICYVE TMNLDGETNL KVKQALEVSS NLVEDSNFKD FKAVVKCEDP NANLYTFVGS
MDVEEQQYPL VPQQLLLRDS KLRNTDYIYG VVIFTGSDTK VMQNSTDPPS KRSRVEKKMD
KVIYFLFAIL VLMSFIGSIW FGIITSKDLV NGRMKRWYLR PDKTTDFYNP KDAPFAAILH
FLTALMLYGY LIPISLYVSI EVVKVLQSTF INQDLHMYHE ETDRPAHART SNLNEELGQV
NTILSDKTGT LTCNSMEFIK CSIAGTAYGR GITEVERSMA RRKGSPLAYE VEDDEEHNMV
DPTDKKQSIK GYNFKDERIV NGQWVYERRS DVIQQFFRLL AICHTALPEV DEETGRISYE
AESPDEAAFV IAARELGFEF CKRTQTSISL HEIDPLSGKK VERSYNLLNF LEFNSTRKRM
SVIVRDEEGK LLLLSKGADS VMLERLSKDG REFEEQTTEH MNEYADAGLR TLVLAYRGIT
KEEYEKFNEE FTEAKNSVSA DRDAMVDEVA AKLEKDLILL GATAVEDKLQ NGVPECIDKL
AQAGIKIWVL TGDKMETAIN IGFSCSLLRQ GMKQTIITLE TPEIKAIVKE GDKSAIRKVS
KESIIHQITE GKKQVTASSG SSDAFALIID GKSLAYALED DVKNLFLEFA VGCASVICCR
SSPKQKALVT RLVKNGTGKT TLAIGDGAND VGMLQEADIG IGISGVEGMQ AVMSSDISIA
QFRYLERLLL VHGHWCYRRI SSMICYFFYK NIAFGFTLFL YEAHASFSGQ AAYNDWYMSL
YNVFFTSLPV IALGVFDQDA SARFCLKFPL LYQEGVQNVL FSWLRILSWM LNGVCSAIMI
FFLCINALEL QAFRKGGEVV GFEILGATMY TCVIWVVNCQ MALSVSYFTM IQHLFIWGGI
ALWYLFLLAY GAMSPLLSTT AYQVFIEALA PAPTYWLVTL FVVIATLMPY FAYSAIQMRF
FPMYHQMIQW LRLEGQTDDP EYCHMVRQRS IRPITVGYTA RREARSNRLR EKRYHKTRIA
ARDSLDITVA E
//
