ID A0A6Q2ZKP5_ESOLU Unreviewed; 1174 AA.
AC A0A6Q2ZKP5;
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:ENSELUP00000078493.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000078493.1, 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:ENSELUP00000078493.1}
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; A0A6Q2ZKP5; -.
DR Ensembl; ENSELUT00000045897.1; ENSELUP00000078493.1; ENSELUG00000022044.2.
DR GeneTree; ENSGT00940000161917; -.
DR Proteomes; UP000265140; LG13.
DR Bgee; ENSELUG00000022044; Expressed in spleen and 14 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:SF52; PHOSPHOLIPID-TRANSPORTING ATPASE FETA; 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 40..70
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 252..275
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 295..320
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 835..856
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 917..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 957..975
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 987..1010
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1030..1052
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 11..63
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 804..1058
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1137..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 132900 MW; 1068D91DEE387B06 CRC64;
MKQRTVPLFH HTNAIKTSKY NVFTFLPLNL FEQFQRIANA YFLILLLLQL IPAISSLSWF
TTVVPLVLVL SVTAAKDATD DIVSINMLQS ERWMNVQVGD IIKLENNQFV TGFLLLMFSR
LLSSPHPLLS FSSPPSFLYS STPPLRETNL KVKQALTVTG DMGDNIQKLA AFNGEVRCEP
PNNRLDRFTG TLNNAGQKYS LDNNRILLRG CTLRNTDWCF GLVLFGGPET KLMKNCGKTT
FKRTSVDRLM NVLVLCIFGF LAVMCTILAI GNRIWEQRWG SDFTAFLPRE DGVNASFSAF
LTFWSYIIIL NTVVPISLYV SMEVIRLGNS FYIDWDRNMY HAHSDTPAEA RTTTLNEELG
QIKYIFSDKT GTLTQNIMTF NKCSINGKSY GDVIDYNGQR LEINENTETV DWSFNPLADQ
RFSFHDHSLV EAVKLESPEV HTFFRLLSLC HTVMAEEKRE GELLYQAQSP DEGALVTAAR
NFGFVFRSRT PESVTVVEMG KQRCYDLLAI LDFNNVRKRM SVIVRSPEGK LCLYCKGADT
IIYERLHQSC SKLMDITTEH LNEYAGEGLR TLALACKDLD EKYFKEWQQR HHVASTALED
REQKLDLLYE EIEKDLMLLG ATAIEDKLQD GVPQTIEQLS QADIKIWVLT GDKQETAENI
GYSCNMLREE MNDIFIVSAN NTDDVRQELR SDDVFTPVTS LGSKVKVIKD EEVDGEFGLV
INGHSLAYAL DGSMELLFLR VACLCKTVIC CRVTPLQKAQ VVELVKKYKQ AVTLAIGDGA
NDVSMIKAAH IGVGISGQEG MQAVLSSDYS FAQFRYLERL LLVHGRWSYL RMCKFLSYFF
YKNFTFTFVH LWYAFFCGFS AQTVYDEWFI TLYNLVYTAL PVLGMSLFDQ DVNDMWSFQH
PKLYVPGQLN QYFSKTAFFK CALHSVYSSV VLFFIPYAAM YDTVRSDGKD IADYQSFALL
TQTCLVFTVC IQLGLDMSYW TAVNQLFVWG SLTMYFAVTF AMYSNGMYLA APASFPFIGT
ARNSLNQPNV WLTILLTSIL CVLPVVAYRF LLIQLRPTIN NKVGPLDTKM VRQAKAAPLP
PKRRAKIRRS STRRSGYAFS HAQGYGDLVT STRFLRRPAI VPSSGFTLLG RTTGFSPMGR
SAGYSPTGHA QNNRPRDVEA TSLQMYSTAQ TLGL
//
