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
//