ID W5M7R2_LEPOC Unreviewed; 601 AA.
AC W5M7R2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP8B1 {ECO:0000313|Ensembl:ENSLOCP00000004420.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000004420.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000004420.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|RuleBase:RU362033};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362033}; Multi-
CC pass membrane protein {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|RuleBase:RU362033}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362033}.
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DR EMBL; AHAT01012545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01012546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M7R2; -.
DR STRING; 7918.ENSLOCP00000004420; -.
DR Ensembl; ENSLOCT00000004428.1; ENSLOCP00000004420.1; ENSLOCG00000003720.1.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000158002; -.
DR HOGENOM; CLU_000846_8_3_1; -.
DR InParanoid; W5M7R2; -.
DR OMA; RANERQY; -.
DR Proteomes; UP000018468; Linkage group LG2.
DR Bgee; ENSLOCG00000003720; Expressed in zone of skin and 8 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: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 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 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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR PANTHER; PTHR24092:SF48; PHOSPHOLIPID-TRANSPORTING ATPASE IC; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 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|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|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
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 137..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 337..361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 381..406
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 79..143
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 69387 MW; E686DCEDBADFF520 CRC64;
MKTLPDTMNR SNRVNSEDSL GPNDEYVPYS DDETDDELDE RTDIEDSQVQ QETVPETIVG
AWKVKANDKD FYNLPEFQKK TFLCLKQSKY SGNAIKTYKY NALTFLPLNL FEQFNRAANL
YFLGLLILQI IPEISTLPWY TTLVPLVLVL GITAIKDLVD DLARHRMDKE INNRKSEVLF
NGRFRESKWK KIQVGDVVRL KKNDFIPADI LLLSSSEPNS LCYVETAELD GETNLKFKMG
LKVTHERLQT EHQLANFDAM IECEEPNNRL DKFIGMMKWR QERYALDLDN ILLRGCTVRN
TEFCHGLVIY AGSDTKIMRN GGKTRFKRTK IDELMNYMVY TIFILLILVA AGLAIGHTFW
YEEMGSIAWY LYDGKNQSSS YRGFLSFWGY IIVLNTMVPI SLYVSVEAIR LGQSRFINWD
LQMYYSEKDT PAKARTTTLN EQLGQIEYIF SDKTGTLTQN IMAFKKCTIS GKTYGDPYST
DGVAMENMVP VDFSWNSYVD KKFKFYDHRL PSCIRAGKEP EVLEFFKLLS LCHTVMVEQK
DDELVYQAAS PDEGALVTAA RNFGYVFLSR TQDTITISEM GEERTYTMLA LLDFNSDRKR
M
//
