ID A0A4W4EHF1_ELEEL Unreviewed; 1074 AA.
AC A0A4W4EHF1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
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:ENSEEEP00000011473.1, 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:ENSEEEP00000011473.1}
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 Ensembl; ENSEEET00000011608.1; ENSEEEP00000011473.1; ENSEEEG00000005691.1.
DR GeneTree; ENSGT00940000157071; -.
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; cd07541; P-type_ATPase_APLT_Neo1-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; 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; 2.
DR PANTHER; PTHR24092:SF50; PHOSPHOLIPID-TRANSPORTING ATPASE IIB-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 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.
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 128..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 352..371
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 865..885
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 891..913
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 943..965
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 971..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1004..1023
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1035..1057
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 74..131
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 831..1066
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 443..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 120461 MW; F541D700A5E72B0D CRC64;
MPLMMSEEAF ENEESDYHTL PRARVGHRRR GLGWFLCGGW KVLCGSCCDC LLRTCRRRKE
LKARTVWLGC PEKCEEKYPK NGIKNQKYNI LTFVPGVLYQ QFKFFLNLYF LVVACSQFVP
SLKIGYLYTY WAPLGFVLAV TMVREAVDEV RRHRRDKEMN SQLYSKLTVR GLILMSSVPC
GFVAQNQRVP ADMIFLRTSE KTGACFIRTD QLDGETDWKL KVAVACTQRL PAVGDLFSIT
AYVYAQQPEL DIHSFEGNFT REDCDPPVHE SLSIENTLWA STVVASGTVI GVVIYTGKET
RSVLNTSQSK NKVGLLDLEL NRLTKALFLA QVVLSVVMVA LQGFVGPWFR NLFRFVVLFS
YIIPISLRVN LDMGKSAYGW IIMKDENIPG TVVRTSTIPE ELGRLVYLLT DKTGTAAMHR
PCLREGLPEY HIVQSHAQPC SVASSGTGAS ATPSHTATPS APKVRKSVVS RVHEAVKAIA
LCHNVTPVYE TRTGMAEAEG TEADQDFGDH NRTYQASSPD EVALVRWTES VGLTLVNRDL
TSLQLKTPVG QILTFTILQI FPFTSESKRM GIIVKEEATG EITFYMKGAD VAMASIVQYN
DWLEEECGNM AREGLRTLVV AKKSLSEEQY QDFESRYNQA RLSLYDRALK VAAVVESLER
EMELLCLTGV EDQLQTDVRP TLELLRNAGI KIWMLTGDKL ETATCIAKSS RLVARSQDIH
VFRPVSNRVE AHLELNAFRR KHDCALVISG DSLEVCLRYY EHELVELACQ CPAVVCCRCS
PTQKAQIVRL LQQHTANRTC AIGDGGNDVS MIQAADCGIG IEGKEGRQAS LAADFSITQF
KHIGRLLMVH GRNSYKRSAA LGQFVMHRGM IISAMQAVFS SIFYFASVPL YQGFLMVGYA
TIYTMFPVFS LVLDQDVKPE MALLYPELYK DLTKGRSLSF KTFFIWALIS VYQGGILMYG
ALVLFDQEFV HVVAISFTAL VLTELLMVAL TVRTWHWLMV MAEFLSLGCY LASLAFLNEY
FGIGRVSLGA CLPLYIIKXL WKGCVITLVS CLPLYIIKYL KRKFSPPSYS KLSS
//
