ID A0A4W4HCL1_ELEEL Unreviewed; 1116 AA.
AC A0A4W4HCL1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP8A1 {ECO:0000313|Ensembl:ENSEEEP00000047735.1};
OS Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC Gymnotoidei; Gymnotidae; Electrophorus.
OX NCBI_TaxID=8005 {ECO:0000313|Ensembl:ENSEEEP00000047735.1, ECO:0000313|Proteomes:UP000314983};
RN [1] {ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24970089;
RA Gallant J.R., Traeger L.L., Volkening J.D., Moffett H., Chen P.H.,
RA Novina C.D., Phillips G.N.Jr., Anand R., Wells G.B., Pinch M., Guth R.,
RA Unguez G.A., Albert J.S., Zakon H.H., Samanta M.P., Sussman M.R.;
RT "Nonhuman genetics. Genomic basis for the convergent evolution of electric
RT organs.";
RL Science 344:1522-1525(2014).
RN [2] {ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28695212;
RA Traeger L.L., Sabat G., Barrett-Wilt G.A., Wells G.B., Sussman M.R.;
RT "A tail of two voltages: Proteomic comparison of the three electric organs
RT of the electric eel.";
RL Sci. Adv. 3:e1700523-e1700523(2017).
RN [3] {ECO:0000313|Ensembl:ENSEEEP00000047735.1}
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; A0A4W4HCL1; -.
DR Ensembl; ENSEEET00000048261.1; ENSEEEP00000047735.1; ENSEEEG00000021982.1.
DR GeneTree; ENSGT00940000157110; -.
DR Proteomes; UP000314983; 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; 2.
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; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_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|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:UP000314983};
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 289..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 332..358
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 819..839
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 845..863
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 892..910
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 930..949
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 961..981
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1001..1021
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 35..95
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 779..1030
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 125833 MW; 17D262E1110B8219 CRC64;
MSDLRSRAEG YEKTEDQSEK TSLADQEDAR LIFINRPQFT KFCSNRVSTA KYNVLTFLPR
FLYSQFRRAA NSFFLFIALL QQIPDVSPTG RWTTLVPLLF ILVVAAVKEV IEDLKRHKAD
SVVNKKETQV LRNGAWEIVH WEKVAVGEVV RASNGDHLPA DLIILSSSEP QGMCYIETSN
LDGETNLKIR QGLQITAEIK DIESLMRLSG RMECESPNRH LYEFVGNIRL DGHSTVPLGP
DQILLRGAQL RNTQWVHGIV VYTGHDTKLM QNSTRPPLKL SNVERITNFQ ILVLFGCLLA
ISLVCSIGQT IWKYQCGDDA WYMDLNCKNG GAANFGLNFL TFIILFNNLI PISLLVTLEV
IKFIQAFFIN WDTDMLYEAT NTPAMARTSN LNEELGQVKY IFSDKTGTLT CNVMQFKKCT
IAGVAYGHSS QSTEEAGFND PSLLENLQSN HPTAPVIMEF MTMMAICHTA VPERNGDTII
YQAASPGDHT WADTQHNPTH ISTARKRMSV IMRTPSGKIR LYCKGADTVV YDRLADNSRY
KDITLKHLEQ FATEGLRTLC FAVTDITESV YQQWQEVHHR ACTSLQNRAL KLEESYELIE
KNLQLLGATA IEDKLQDRVP ETIETLIKAD IKIWILTGDK QETAINIGHS CKLLTKNMGL
LVINEESLDG TRETLSHHCN MLGDALHKEN DFALVIDGKT LKYALTFGVR QYFLDLALSC
KAVICCRVSP LQKSEVVEMV KKHVKVITLA IGDGANDVGM IQTAHVGVGI SGNEGLQAAN
SSDYSIAQFK YLKNLLLVHG AWNYNRVAKC ILYCFYKNIV LYIIEIWFAF VNGFSGQILF
ERWCIGLYNV IFTALPPLTL GIFERSCRKE NMLKYPELYK TSQNAMGFNT KVFWAHCLNG
LFHSVILFWF PLKAFQHDTV FGNGKTPDYL LLGNMVYTFV VITVCLKAGL ETSSWTMFSH
IAIWGSIALW VVFFGIYSSL WPLIPFAPDM SGEADMMFSS GVFWTGLLFI PITSLVFDLA
YKVIKKACFK TLVDEVQVLE ALSKDPGAVV HGKSLTERAQ LLKNVFKKST VSLYRSDSMQ
QSLLHGYAFS QDENGVVSQS EVIRAYDTTK QRTNEW
//
