UniProt: A0A4W5P6B9

Database: UniProt
Entry: A0A4W5P6B9_9TELE

LinkDB:  A0A4W5P6B9_9TELE 
Original site:  A0A4W5P6B9_9TELE

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (15)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
All databases (25)   

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ID   A0A4W5P6B9_9TELE        Unreviewed;      1190 AA.
AC   A0A4W5P6B9;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS   Hucho hucho (huchen).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Hucho.
OX   NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000058927.1, ECO:0000313|Proteomes:UP000314982};
RN   [1] {ECO:0000313|Proteomes:UP000314982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Macqueen D.J., Gundappa M.K.;
RT   "Genome assembly of Danube salmon.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSHHUP00000058927.1}
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; A0A4W5P6B9; -.
DR   Ensembl; ENSHHUT00000060940.1; ENSHHUP00000058927.1; ENSHHUG00000034972.1.
DR   GeneTree; ENSGT00940000165675; -.
DR   Proteomes; UP000314982; 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; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR24092:SF177; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000314982};
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        305..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        348..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        877..898
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        910..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        959..979
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        999..1017
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1029..1053
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1073..1093
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          22..76
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          846..1100
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1190 AA;  135685 MW;  648D3ADBD243226F CRC64;
     RANDREFNLS YEYAVSTVID YLFQDNAIKT SKYNIFTFLP LNLFEQFQRL ANAYFLFLLC
     LQLIPEISSL SWFTTVVPLV LVLSMTMAKD GSDDINRHRC DRQVNNRKVE VLIDGELRSE
     KWMDVQVGDI IKLENNQFVT ADLLLLSSSE PLNLVYIETA ELDGCVSVAF KHAFVFTFAF
     LNCMSSSSVF LILPSSSFRE TNLKVKQALT VTGELEDGIE KLANFNGEVR CEPPNNRLDK
     FTGTLTLKGE MYSLDNERVL LRGCTLRNTQ WCFGLVVFGG PDTKLMQNCG KTTLKRTSID
     RLMNVLVLSI FGFLAIMCLI LAVGNGIWEY QEGSKFAAFL PKQEGVNAPF SAFLTFWSYV
     IILNTVVPIS LYVSVEIIRL GNSFYIDWDR KMYYPKSDTP AEARTTTLNE ELGQIKYIFS
     DKTGTLTQNI MTFNKCSING KSYGEPYQCA GMDGNRGRYV DFSWNNLADP KFCFHDHSLV
     EVVREGNPEV QAFFRLLALC HTVMPEEKKE GELYYQAQSP DEGALVTAAR NFGFVFRSRT
     PESITVVEMG ELVTYELLAV LDFNNVRKRM SVIVRSPEGK LTLYCKGADT IIFERLNPSC
     SKLKEVTTEH LNEYAGDGLR TLALAYKDID PEYMEEWKLR HHEASTAMDE REEKLDALYE
     EIEKGLLVGS TAVEDKLQDG VPQTIEQLSK ADIKIWVLTG DKQGGLSSLE YTINRLQLFS
     LAHLDSLFSL SEQKRQRTLC SSCRQTQQRK SERSSSESTD GLLTITFVAF ALEKDMEMEL
     LRTACMCQTV ICCRVTPLQK AQVVELVKKY KQAITLAIGD GANDVSMIKA AHIGVGISGQ
     EGMQAVLSSD FSFAQFRYLQ RLLLVHGRWS YLRMCKFLRY FFYKNFTFTF VHFWYGFFCG
     FSAQTVYDEW FITLYNLVYT ALPVLALSLF DQDVNDRWSF QYPKLYAPGQ LNQYFSKRAF
     VYTVLHSGYS SLVLFFIPWA AMYDTVRDDG KDIVDYQSFA LLAQTCLLIA VSIQLGLDTH
     YWTSVNQFFL WGSLCVYFAV IFTMYSNGMF LIFTSSFPFI GTARNSLNQP NVWLTMLLTS
     ILCVLPVVAY RFLRILLWPT INDKVRCRGQ DKVLPPVPRR VQARRVSTRR SGYAFSHAQG
     YGDLVTSGRF LRWTPKSRLA LFSQTDSPLA QTQPQFYRTI NEGGEPPLSP
//

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