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Database: UniProt
Entry: A0A4W5PU00_9TELE
LinkDB: A0A4W5PU00_9TELE
Original site: A0A4W5PU00_9TELE 
ID   A0A4W5PU00_9TELE        Unreviewed;      1166 AA.
AC   A0A4W5PU00;
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   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:ENSHHUP00000063984.1, 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:ENSHHUP00000063984.1}
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; A0A4W5PU00; -.
DR   Ensembl; ENSHHUT00000066150.1; ENSHHUP00000063984.1; ENSHHUG00000037573.1.
DR   GeneTree; ENSGT00940000156728; -.
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; 2.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 2.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR24092:SF84; PHOSPHOLIPID-TRANSPORTING ATPASE VD; 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        48..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        266..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        312..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        978..1002
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1043..1063
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1075..1093
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1100..1125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1145..1163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          18..74
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          929..1165
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          433..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1166 AA;  130802 MW;  FE896C1A21A3F5CA CRC64;
     MRTVVSSLTE DEELTEILKS YSSNKVTTTK YSFLSFIPKN LFEQLHRVAN IYFIFLAALN
     FVPVVNAFQP EISIIPILLV LTVTAVKDLW EDYRRHKSDK FINGLLSCGL FYHRKQQTYV
     DQRWQDVHVG DFVRLSCNEI IPADMLLLYS SDPHGVCYIE TANLDGETNL KQRQVVRDLP
     QQVCENFHSR IECESPNNDL SRFRGYMEYP SKARVGLHND NLLLRSCTIR NTETVIGIVV
     YAGHETKAMK NNSGPRYKRS KLERRLNVDV LWSVVLLVIM CLTAAIGHGL WLRNLKEASF
     LIPDTTSPAL SGFYLFWTMI IVLQVLIPIS LYVSIEIVKL CQIFFIQNDV DFYNEYMDSR
     IQCRALNITE DLGQIQYVFS DKTGTLTENK MVFRRCTIAG VEYPHEENGE KSKVHFSTQH
     NIFHQGSVSL HTLTGHSEGE EPPSPTLPQQ SAFSSPLEKD IVPDPFLVQK LNSLSSPLFL
     LKDASMELTY IVDFFMALAI CNTVVVSSPN QPRHVVSNIT SPVCTGQSFS RKLRTGDSEM
     SRLSTGEHGS WKGEENKMLH LTLGACSGLG NSNGAQGPPG EPGADELIYE AESPDEAALV
     HAARAYRCTL QGRSLESLLV ELPGMGSLAV RLLHILPFDS TRKRMSVVVR HPLTNQVVVY
     TKGADSVIMD LAESPKGAEQ SDGRQGHIRE QTQKHLDNYA REGLRTLCVA KKVLEEEEYE
     IWLKRHAFAE TSIENREELL LESAQRLETN LTLLGATGIV DRLQEEVPET IEALQRAGVK
     VWVLTGDKQE TAINIACACK LLRSTDQLLT ANCGSKEACK ALLLELRAEV ERGEAAEGTS
     GFTLVVDGRT LDFALQEDLK GDFLELSRRC RAVVCCRSTP LQKSHVVKLV RDQLRVMTLA
     IGDGANDVSM IQVADVGIGI SGQEGMQAVM SSDFAISRFK HLRKLLLVHG HWCYTRLANM
     ILYFFYKNVM YVNLLFWYQF FCGFSGSVMT NSWVLIFFNL LFTSAPPLLY GILDKDVSAD
     TLIKLPELYK SGQNSKAYLP STFWLTMLDA LYQSLVCFFI PYFANAGSDA DMLTFGSPIN
     ASALLTILLH QVIESCTLTW LHVLVLVGSA LFYFSFTLVF SVVCVTCSPP TNPLGVDKLQ
     MSQPLFYGVC ALTTVLALLP RYIHQQ
//
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