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Database: UniProt
Entry: A0A3S2PF48_ORYJA
LinkDB: A0A3S2PF48_ORYJA
Original site: A0A3S2PF48_ORYJA 
ID   A0A3S2PF48_ORYJA        Unreviewed;       908 AA.
AC   A0A3S2PF48;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-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};
GN   ORFNames=OJAV_G00037470 {ECO:0000313|EMBL:RVE74070.1};
OS   Oryzias javanicus (Javanese ricefish) (Aplocheilus javanicus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=123683 {ECO:0000313|EMBL:RVE74070.1, ECO:0000313|Proteomes:UP000283210};
RN   [1] {ECO:0000313|EMBL:RVE74070.1, ECO:0000313|Proteomes:UP000283210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS831 {ECO:0000313|EMBL:RVE74070.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:RVE74070.1};
RA   Lopez-Roques C., Donnadieu C., Bouchez O., Klopp C., Cabau C., Zahm M.;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RVE74070.1, ECO:0000313|Proteomes:UP000283210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS831 {ECO:0000313|EMBL:RVE74070.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:RVE74070.1};
RA   Herpin A., Takehana Y., Naruse K., Ansai S., Kawaguchi M.;
RT   "A chromosome length genome reference of the Java medaka (oryzias
RT   javanicus).";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362033}.
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DR   EMBL; CM012440; RVE74070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S2PF48; -.
DR   Proteomes; UP000283210; Chromosome 4.
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   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; 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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR24092:SF81; PHOSPHOLIPID-TRANSPORTING ATPASE VA; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 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:UP000283210};
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        613..637
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        644..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        671..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        716..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          501..746
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          67..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          779..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..875
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   908 AA;  101119 MW;  39D9C57414004CBE CRC64;
     MRLHSQPVSQ LPSDLSDIFD FFIALTVCNT VVVSSPNQPR QKVRMRFELK SPVKTIEDFI
     KRFTPSRLTS GSNNSSSSSL NRSSNKGGSS MLSSPSAEST LTKLNEEQSS GGLEHAFSPA
     PPSYEEKAFC TPEEGELRYE AESPDEAALV YAARAYKCSL VGRLPDQVTV ELPHLGKLNF
     ELLHTLGFDS TRKRMSVVVR HPLTDQITVY TKGADSVIME LIRPPNTGNS KGRRQKKILC
     RTQNYLNLYA ADGLRTLCIA KKVLSKEEYA RWLQHHLEAE TAIQRREELL FESALRLETN
     LQLLGATGIE DRLQDGVPET IASLRKAGLQ IWVLTGDKQE TAVNIAYACK LLDPEEELLT
     LNADSKEACK LLLEESLHYI QAKFLCSSGD VSSFEIYPPA PPSSHAASFS VHQLGLVIDG
     RTLAYALDSS LEDKFLAVAR SCRSVLCCRS TPLQKSMVVK LVRNKLKVMT LAIGDGANDV
     SMIQVADVGV GISGQEGMQA VMASDFALPR FRYLQKLLLV HGHWCYSRLA NMILYFFYKN
     AMFVALIFWY QFYCGFSGSA MIDQWYLIFF NLMFSSFPQL ISGTLDKDVS AETLQQLPQL
     YTSGQNSEEY KPYMFWMNMI DAFYQSLVCF FIPYFTYTDS DVDLFTWGTP ITAIALLTIL
     LHLSIETKTW TWMNCLSITF SIALFFTVAL CYNASCPTCY PPSNPYWTIQ RLLQDPVFYL
     LCTITPVAAL LPRYFYRACH STLFPNPVQV GRQLDKLPAD TRRNILSLSR VKMGSWLSPR
     PPSLPVGKPQ SCVQKDQRSK LAPAQRGDAE SVQQGAGPES CTKNDPLLSE ELQPASTKDP
     SDSGPCSGMT STPVVAQMDR VQLNLPPSRT SPCVAYVRSS EAPLSREQTP PCSHGTGQGA
     EPALYTVL
//
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