ID A0A6G0I3G2_LARCR Unreviewed; 1146 AA.
AC A0A6G0I3G2;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=D5F01_LYC15413 {ECO:0000313|EMBL:KAE8285746.1};
OS Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Larimichthys.
OX NCBI_TaxID=215358 {ECO:0000313|EMBL:KAE8285746.1, ECO:0000313|Proteomes:UP000424527};
RN [1] {ECO:0000313|EMBL:KAE8285746.1, ECO:0000313|Proteomes:UP000424527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMULYC20181020 {ECO:0000313|EMBL:KAE8285746.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAE8285746.1};
RA Xiao S.;
RT "Chromosome genome assembly for large yellow croaker.";
RL Submitted (JUL-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:KAE8285746.1}.
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DR EMBL; REGW02000015; KAE8285746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G0I3G2; -.
DR Proteomes; UP000424527; 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; 2.
DR PANTHER; PTHR24092:SF38; PHOSPHOLIPID-TRANSPORTING ATPASE IG; 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; SFLDS00003; Haloacid_Dehalogenase; 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:UP000424527};
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 56..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 277..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 888..910
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 979..1001
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1016..1035
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1047..1068
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1088..1110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 30..83
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 854..1112
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1146 AA; 130932 MW; BF96431F7D9D8F79 CRC64;
MLGGDERRVD SRTIYVGHRS CSTTEAFIPP KFCDNRIVSS KYTVWNFLPK NLFEQFRRIA
NFYFLIIFLV QVIVDTPTSP VTSGLPLFFV ITVTAIKQGY EDWLRHKADN EVNKYQVKVL
EDGRRIQKES EKIKVGDVVE VEEDETFPCD LILLQSSRDD DTCFVTTASL DGESNHKTHY
TVPDIEKDLE SLNATIECEQ PQPDLYKFVG RMHIDKNDQE PAVRSLGPEN LLLKGATLKN
TQKIYGVAVY TGMETKMALN YQGKSQKRSA VEKSINAFLL VYLCILVSKA LVCTTLKYVW
QSKDGQDEPW YNEKTQREKD TNLYLKMFTD FLSFMVLFNF IIPVSMYVTV EMQKFLGSFF
ITWDKDFFDP EIQEGALVNT SDLNEELGQV EYVFTDKTGT LTQNNMEFIE CCIDGFQYKY
RDASSELDGF CVTDGPVSKL QQKAGREKEE LFLRALCLCH TVQVKESTDQ GQSQQDGLID
QVDGLEVDAG LFHPPQEQRG FIASSPDEVA LVKGAMRYGF TFLGLESKTM KILNRNNDVE
MYELLHVLNF DPVRRRMSVI VRSKSGDTLL FCKGADSSIF PRVRQEEVER IRMHVERNAT
EGYRTLCVAY KILSAEEYAQ ADAGLRDARL ALQDREEKLM TVYNQVETGM SLIGATAVED
RLQEEAAETM EALQGAGIKV WVLTGDKMET AKSTCYACRL FQRNTELLEL TVRTLEDGER
SREVRLHELL LEYHKKAVQD APPVKAGVNR SWSSAGQDYG FIIDGATLSM VLNNSPESNS
SRYKNLFLQI CQNCTSVLCC RMAPLQKAQI VKMVKNSKGS PITLSIGDGA NDVSMILEAH
VGIGIKGKEG RQAVRNSDYA VPKLKHLKKL LLAHGHLYYV RIAHLVQYFF TSVIWFSFSV
CLQNLCFILP QFLYQFFCGY SQQPLYDAAY LTMYNICFTS MPILAYSLLE QHICIEVLLD
NATLYREIAK NAVLRWGTFL YWTVLGVFHG LLFFFGVRFL FSNPALQDNG QVFGNWSYGT
IVFTVLVFTV TLKLALDTRH WTWINHFVIW GSLAFYVFFS FFWGGIIWPF LRQQRLYFVF
ANMLSSVSAW LVIILLILLS LLPEILLVVF RKPRGPHARQ KKMMSPILSF KQLSEDGLLQ
SSRLQL
//
