ID A0A484CWV9_PERFV Unreviewed; 1164 AA.
AC A0A484CWV9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-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=EPR50_G00105740 {ECO:0000313|EMBL:TDH07409.1};
OS Perca flavescens (American yellow perch) (Morone flavescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8167 {ECO:0000313|EMBL:TDH07409.1, ECO:0000313|Proteomes:UP000295070};
RN [1] {ECO:0000313|EMBL:TDH07409.1, ECO:0000313|Proteomes:UP000295070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YP-PL-M2 {ECO:0000313|EMBL:TDH07409.1};
RC TISSUE=Blood {ECO:0000313|EMBL:TDH07409.1};
RA Feron R., Morvezen R., Bestin A., Haffray P., Klopp C., Zahm M., Cabau C.,
RA Roques C., Donnadieu C., Bouchez O., Christie M., Larson W., Guiguen Y.;
RT "A chromosome-scale genome assembly of the yellow perch, Perca
RT flavescens.";
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: 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:TDH07409.1}.
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DR EMBL; SCKG01000010; TDH07409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A484CWV9; -.
DR STRING; 8167.A0A484CWV9; -.
DR Proteomes; UP000295070; Chromosome 10.
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; 3.
DR PANTHER; PTHR24092:SF225; PHOSPHOLIPID-TRANSPORTING ATPASE IA; 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 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:UP000295070};
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 296..319
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 339..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 867..887
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 893..911
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 940..958
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 978..997
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1009..1029
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1049..1069
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 39..102
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 827..1078
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1164 AA; 131403 MW; D941D8B0BB4A6988 CRC64;
MPPVQRTMSD LRTRAEGYEK TEDTTEKTSL ADQEDARLIY LNQPQFTKFC NNRVSTAKYN
VLTFLPRFLY SQFRRAANAF FLFIALLQQI PDVSPTGRWT TLVPLLFILM VAAVKEFIED
LKRHNADSVV NKKECQVLRN GAWEIVHWEK VSVGEVVRAA NGDHLPADLV ILSSSEPQGM
CYIETSNLDG ETNLKIRQGL QITADIKDID SLMRLSGRME CESPNRHLYE FVGNIRLDGH
STMPLGPDQI LLRGAQLRNT QWVHGVVVYT GHDTKLMQNS TRPPLKLSNV ERITNFQILV
LFGCLLAISL VCSIGQTIWK YQYGNDAWYM DLNYGGAANF GLNFLTFIIL FNNLIPISLL
VTLEVIKFIQ AFFINWDTDM LYEPTNTPAM ARTSNLNEEL GQVKYIFSDK TGTLTCNVMQ
FKKCTIAGVA YGHVPEAEEG SFAEDDCHST HSSEEEGFND LSLLENLQSN HPTAAVILDF
MTMMAICHTA VPERTDGKIT YQAASPDEGA LVRAAQNLGF VFSGRTPDSV IVEMPGTEER
YELLHVLEFT STRKRMSVIM RTPSGKIRLY CKGADTVIYD RLADSSRYKE ITLKHLEQFA
TEGLRTLCFA ATDVSESSYQ QWLEIYRRAC TSLQNRSLKL EESYELIEKN LQLLGATAIE
DKLQDKVPET IETLMKADIK IWILTGDKQE TAINIGHSCK LLTKNMGMLV INEDTLDRTR
EALSHHCGML GDALYKENDF ALIIDGKTLK YALAFGVRQY FLDLALSCKA VICCRVSPLQ
KSEVVEMVKK QVKVITLAIG DGANDVGMIQ TAHVGVGISG NEGLQAANSS DYSIAQFKYL
KNLLLVHGAW NYNRVAKCIL YCFYKNIVLY IIEIWFAFVN GFSGQILFER WCIGLYNVIF
TALPPLTLGI FERSCRKENM LKYPELYKTS QNAMGFNTKV FWAHCLNGLF HSVILFWIPL
KAFQHDTVFG NGRTPDYLLL GNMVYTFVVI TVCLKAGLET SSWTMFSHIA IWGSIGLWVV
FFIIYSSLWP LIPLAPDMSG EAEMMFCSGV FWTGLVFIPI TSLVFDVAYK VVKKVCFKTL
VDEVQELEAL SKDPGAVVHG KSLTERAQLL KNVFKKSTVS LYRSDSMQQN LLHGYAFSQD
ENGVVSQSDV IRAYDTTKQR TNEW
//
