ID A0A6Q2Z8D3_ESOLU Unreviewed; 912 AA.
AC A0A6Q2Z8D3;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Phospholipid-transporting ATPase IA {ECO:0000313|Ensembl:ENSELUP00000074128.1};
GN Name=ATP8A1 {ECO:0000313|Ensembl:ENSELUP00000074128.1};
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:ENSELUP00000074128.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000074128.1, 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:ENSELUP00000074128.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A6Q2Z8D3; -.
DR Ensembl; ENSELUT00000069349.1; ENSELUP00000074128.1; ENSELUG00000017038.2.
DR GeneTree; ENSGT00940000157110; -.
DR Proteomes; UP000265140; LG15.
DR Bgee; ENSELUG00000017038; Expressed in spleen and 15 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF225; PHOSPHOLIPID-TRANSPORTING ATPASE IA; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
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 PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 250..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 676..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 718..740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 752..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 777..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..97
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 609..837
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 912 AA; 103037 MW; C1DBDDB8FDA0D988 CRC64;
MLSCSLDSYP VGYDKTEEAT SSVPAANLED SRLIFINQPQ LTKFCTNHVS TAKYNMLTFL
PRFLYSQFRR AANSFFLFIA LLQQIPDVSP TGRWTTLVPL VLILLVAALK EIIEDLVRPL
FNIPCVFHSE PMAMCYIETS NLDGETNLKI RQGLQVTADD RDVDSLSRLS GRLECESPNR
HLYDFVGVIR LEGHSPVPLG PEQILLRGAR LRNTRWVHGM VVYTGHDTKL MQNSTRPPLK
LSSVERVTNT LILALFGCLL AISLGCSAGQ TVWKTRHGDQ AWYMDLNYGG AANFGLNFLT
FIILFNNLIP ISLLVTLEVI KFVQAYFINW DMDMHYEATD SSAMARTSNL NEELGQVQYV
FSDKTGTLTC NVMQFKKCTV AGVAYGHDRE TPLEGAFDDP SLLENLQNDH STATVIRDFL
TMMAVCHTAV PEKTGDSIVY QASSPDEGAL VRAAGYLGFV FSGRTPHSVI IQAVSGEIVL
HLHSYTAQFF HLKHYCKFTQ FLPAICHHCG ILGEALRREN DIALVIDGET LKYALSFEVC
QYFLDLALSC KAVICCRVSP LQKSEVVDLV KRQVKVITLA IGDGANDVGM IQTAHVGIGI
SGNEGLQAAN SSDYSIAQFK YLRNLLLVHG SWNYNRVSKC ILYCFYKNIV LYIIEIWFAI
VNGFSGQILF ERWCIGLYNV IFTAMPPLAL GIFERCCKKE NMLKYPELYK SSQNALGFNT
KVFWAYCLNG LLHSVVLFWL PLLAFHDWLS DLWFLCLQFV VITVCLKAGL ETSSWTLFSH
IAIWGSICLW VLFFWLYSSL WPVIPIAPDM SGQVKYNLHL MHNIVLLTLY RVKRTFWKNL
VDEVQELEAK SQDLGAVVHG KRCFSYKTLC KLRFRLRIQY GYAFSQDENG AVSQSDVIRS
YDTTRQRPAQ TQ
//
