ID A0A4U5TY34_COLLU Unreviewed; 1180 AA.
AC A0A4U5TY34;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=D9C73_027867 {ECO:0000313|EMBL:TKS65355.1};
OS Collichthys lucidus (Big head croaker) (Sciaena lucida).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Collichthys.
OX NCBI_TaxID=240159 {ECO:0000313|EMBL:TKS65355.1, ECO:0000313|Proteomes:UP000298787};
RN [1] {ECO:0000313|EMBL:TKS65355.1, ECO:0000313|Proteomes:UP000298787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JT15FE1705JMU {ECO:0000313|EMBL:TKS65355.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TKS65355.1};
RA Cai M., Xiao S.;
RT "Genome Assembly of Collichthys lucidus.";
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ML240683; TKS65355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U5TY34; -.
DR STRING; 240159.A0A4U5TY34; -.
DR Proteomes; UP000298787; 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; 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:SF198; 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:UP000298787};
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 335..366
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 386..408
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 875..896
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 908..928
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 956..981
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1029..1055
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 73..141
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 844..996
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1180 AA; 132709 MW; A26B3F4323D84F85 CRC64;
MSCERVRCTG NSGYCDTGAF TWEREEGGAE NRFRLQKERD GGWMKQVLYN AQGLANNPGF
TWEVRANSRH YHKPKQKNSF MCFRWGRYAD NLVRSYKYSP LTFLPLTLFE QFQRVANLYF
LLMVVLQCVP VISSIPWYIS IIPLITVLSI RALKDLANDM ARRRSDSWIN SRPCDVLIPQ
SFNTAQWKDL FVGDVLRIRK DQVIPADLLL LCSSEPHSLC YVETADIDGE TNLKYRQAPS
ATHNELTSHP SEEALAAFDG VVLCEEPNNR LHTFRGQLHW RGECLLLDNE HILLRGTVLR
NTEFAYGLTI YTGADTKILR NCGKVRMKIT RMEKVFNKVV IGIVVSVLMT ALLLAIGSGV
FSAWLMNDLG VMSVLVVDGN PVYTGFLVYW SYIILLSPAM PIILYITFEM IHTVHSQFIG
SDLEMYWQPA DKPAQARNTS LSEELGQVGY LLSDKTGTLT QNHLLFRQCC IAGEIYAPSL
VEKLRGQQCP LSRQFLSAMS LCHTVMAEWK NEAPVYQAAS PDEEALVCAA RELGWVFLSR
TRDFIVVSEL GVTRQYQLLA LLDFTSQRRR MSVLVREPEG GLKLYCKGAD IVILERLQKD
FPYLERSETA LEACLRTLCV AVRSVPEASW EQWSKILAQS AAMATCERDA LLEKLYDQME
RELQLLGVTA IEDRLQEGVP ETIALLQQAG LKVWVLTGDK KVNIGYSCKL LDSDTRLLEW
QELRQILQSP DPVVSFFKGR QTELWAVDKG RTKGKTAIVL TGPELAEFDQ RPDWGATFMS
LAAGCQSVLC CRVTPGQKAE IVTLVRKHTN SVTMSIGDGA NDVNMIKTAH VGVGIAGVEG
GQAVQNADFA LSQFRFLQRL LLVHGRWSYR RISIFLRYFL FKTCGFALVH IWFGFLNGFS
AQTLYENWFI ALYTVFYTST PIMLLAFFEQ DVSSESSLRW PELYKVGQRQ ELSSPLLLSL
SLLHAVYASL IFFFIPCGVF YNTAFDYQTM AVTVSMAARS LPSLRYPTAT TFLREHPRSV
SEKAFADPVV WLTALLTACT AVLPSMTAHA LNVILTVHGK HKGAGHGRLI TSTTSMRSIA
MSLDQKHLVA LPSLSSALSP IAPLDTGLCY RQQGALLLCQ HRQGPGRESC NVVGWMPERV
VVAWFSVIDQ RKSSLQNKEH VQTSHPPLLL VRETQTLGSG
//
