ID A0A553QRP6_9TELE Unreviewed; 1141 AA.
AC A0A553QRP6;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=DNTS_007692 {ECO:0000313|EMBL:TRY92635.1};
OS Danionella translucida.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danionella.
OX NCBI_TaxID=623744 {ECO:0000313|EMBL:TRY92635.1, ECO:0000313|Proteomes:UP000316079};
RN [1] {ECO:0000313|Proteomes:UP000316079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bolton {ECO:0000313|Proteomes:UP000316079};
RA Kadobianskyi M., Schulze L., Schuelke M., Judkewitz B.;
RT "Hybrid genome assembly and annotation of Danionella translucida.";
RL bioRxiv 0:0-0(2019).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TRY92635.1}.
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DR EMBL; SRMA01025600; TRY92635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553QRP6; -.
DR Proteomes; UP000316079; 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 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; 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:SF33; PHOSPHOLIPID-TRANSPORTING ATPASE IH; 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 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:UP000316079};
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 255..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 309..328
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 910..932
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 952..974
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 986..1010
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1016..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 796..1056
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1141 AA; 129961 MW; 54EDD698C6418C2E CRC64;
MALCTGEESW VDSRTVYIGH KEPPPGTEAY IPQRFPDNRV VSSKLIIDTP TSPMTSGLPL
FFVITVTAIK QGYEDWIRHK ADNAVNQCPV HIIQHGKVVR KQSRKLRVGD VVQVKENEVF
PCDLILLSTS KEDGTCFVTT ASLDGESSHK TYYAVQDTKA FSTAEEVDTL HATIECEQPQ
PDLYKFVGRI NIYLDRDEPI ARPLGSENLL LRGATLKNTE YIHAVAIYTG METKMALNYQ
SKSQKRSAVE KSMNAYLIVY LCILISKALI NTVLKYVWQA DANRDEPWYN QKTEIERQRH
VIIRAFTDFL AFMVLFNYII PVSMYVTVEM QKFLGSYFIL WDDDMFDEEI GERPLVNTSD
LNEELGQVEY VFTDKTGTLT ENNMELRECC VNGHVYVPDA ICNGQVLPGA AGMDMIDSSP
GVEGKEREEL FFRALCLCHT VQVKEEETVD SIKRGIHQGK STSFYISSSP DEDSHMEILN
REDEMERFEL LEVLNFDSVR RRMSVVVRSS SGEFFLFCKG ADSSIFPRVV SGKVEQVRAR
VEHNAVEGLR TLCVAYKKLS QEEYEEMCHL LNSAKLALQD RDKKLAEAYD VIEKDFILLG
ATAVEDRLQD KAADTIESLH KAGIKVWVLT GDKMETAAAT CYASKLFHRN TQILELTTKR
TEEQSLHDVL FDLSRTVLRQ QGSMTRDTFS GLSGDFQDYG LIIDGATLSA VLKPTQEGSS
SGGNYKEIFL EICRNCSAVL CCRMAPLQKA QIVKMIKASK EHPITLAIGD GANDVSMILE
AHVGIGIMGK EGRQAARNSD YAITKFKHLK KMLLVHGHYY YIRISELVQY FFYKNVCFIF
PQFLYQFFCG FSQQPLYDTA YLTLYNISFT SLPILLYSLM EQHINMDILK RDPSLYRDIA
KNSLLTWPTF IYWTFLGVFD AVVFFFGAFF LFDNTTFTSN GQLMATNTQM MFGNWTFGTL
VFTVLVFTVT LKLALDTHYW TWINHFVIWG SLLFYVIFSL LWGGIIWPFL NYQRMYYVFM
QMLSSGPAWL SIILLVIVSL LPDVVKKVLC RALWPTTTEK IQNADKLYKG HLSEFTPLSS
LHAPPLRKHD RPGNDSQIHT HRRPFLGMFE KSPKFVHSSE LVGVRKVCEN GSKAPLYCSL
S
//
