ID A0A6Q2YKE1_ESOLU Unreviewed; 1152 AA.
AC A0A6Q2YKE1;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000066449.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000066449.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000066449.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 AlphaFoldDB; A0A6Q2YKE1; -.
DR Ensembl; ENSELUT00000054137.1; ENSELUP00000066449.1; ENSELUG00000000790.2.
DR GeneTree; ENSGT00940000165675; -.
DR Proteomes; UP000265140; LG14.
DR Bgee; ENSELUG00000000790; Expressed in liver and 5 other cell types or tissues.
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; 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; 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:SF177; PHOSPHOLIPID-TRANSPORTING ATPASE; 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; 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|ARBA:ARBA00022840, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
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 84..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 278..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 321..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 837..858
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 919..941
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 961..981
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 988..1013
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1033..1053
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 24..90
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 806..1060
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1152 AA; 131631 MW; BAE5F896F3484E42 CRC64;
MGSLLSRLGL ECGAKEVKEE ERNIRANDRE YNLSYKYANN AIKTSKYNIF TFLPLNLFEQ
FQRLANAYFL FLLCLQLIPD ISSLSWFTTV VPLVLVLAMT MAKDGSDDIV SACSAQDQKQ
LTMFTLYRLR SEKWMNVQVG DIIKLQNNQF DSIEKLASFD GETGNKMDTL SPLRSLHLLE
SKYFWSVCYP FPEPLCPCLG QVRCEPPNNR LDKFTGCLSL DGAMYSLDNE KILLRGCTLR
NTQWCFGLVL FGGPDTKLMQ NCGKTTFKRT SIDRLMNVLV LSIFGFLAIM CLILAIGNGI
WEYQEGATFA AFLPKPEGVN PPFSAFLTFW SYVIILNTVV PISLYVSVEI IRLGNSFYID
WDRKMYYPKN DTPAQARTTT LNEELGQIKY IFSDKTGTLT QNIMTFNKCS INGKSYERVD
FSWNKLADPK FWFHDHSLVE VVRGGNPKAH DFFRLLALCH TVMPEEKKEG ELYYQAQSPD
EGALVTAARN FGFVFRSRTP ESITVVEMGK LVTYELLAVL DFNNVRKRMS VIVRSPDGRL
TLYCKGADTI IFERLHPSSK NEYAGDGLRT LALAYKDIDL NYMEDWKKRH HEASTGMEQR
EEKLDALYEE IEKGLLLLGA TAVEDKLQDG VPQTIEQLAK ADIKIWVLTG DKQETAENIG
YSCNMLREEM TEVFIVAGNT AEEVRVELQS RNGLFCLLKK ETMEDEPVNG EYAMVINGHS
LVRTKNPVTG HLIKDMQKEL LRTACMCQTV ICCRVTPLQK AQVVELVKKY KQAITLAIGD
GANDVSMIKA AHIGVGISGQ EGMQAVLSSD YSFAQFRYLQ RLLLVHGRWS YLRMCKFLRY
FFYKNFTFTL VHFWYGFFCG FSAQTVYDEW FITLYNLVYT ALPVLGLSLF DQDVNDRWSF
QYPQLYAPGQ LNQYFSKKAF IYTVLHSGYS SLVLFFIPWA AMYDTVRDDG KDIVDYQSFA
LLAQTCLLIA VNIQLGLDTY YWTAVNQFFL WGSLSVYFAV TFTMYSNGMF LIFTSSFPFI
GAARNSLNQP NMWLTILITS ILCVVPVVAY RFLRILLWPT INDKVRHKMR QEKAVLPAAP
RRIQPRRIST RRSGYAFSHA QGYGDLVTSG RFLRRTPRSR GIVFSHTDSP LAQAKPQLYR
TIVEGEEPPQ IP
//
