ID A0A3B4AST8_9GOBI Unreviewed; 1173 AA.
AC A0A3B4AST8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000020247.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000020247.1}
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; A0A3B4AST8; -.
DR STRING; 409849.ENSPMGP00000020247; -.
DR Ensembl; ENSPMGT00000021573.1; ENSPMGP00000020247.1; ENSPMGG00000016396.1.
DR Proteomes; UP000261520; Unplaced.
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; 1.
DR PANTHER; PTHR24092:SF52; PHOSPHOLIPID-TRANSPORTING ATPASE FETA; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00121; NAKATPASE.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 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 63..93
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 276..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 322..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 839..860
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 921..941
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 961..979
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 991..1013
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1033..1055
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 21..86
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 808..1061
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1121..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 605..639
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1173 AA; 134164 MW; D58927F944B78529 CRC64;
MTFFGLDCLA KKERELERKL RANDREYNLS FKYATNAIKT SKYNFFTFLP LNLFEQFQRI
ANAYFLFLLV LQVIPAISSL SWFTTVVPLV LVLTVTAAKD ATDDINRHRS DNQVNNRKVQ
VLINRLQNEK WMNVQVGDII KLENNQFVTA DLLLLSSSEP LNLVYIETAE LDETNLKVKQ
ALPVTGDLGD NIEKLADFNE VRCEPPNNRL DRFTGTLTFA GQKYSLDNEK ILLRGCTLRN
TDWCFGLVLF APETKLMQNC GKSTFKRTSI DRLMNILVLC QIFGFLAFMC TVLAIGNCIW
ELNDGSQFTV FLPRQEGTSA TFSAFLTFWS YVIILNTVVP ISLYVVEIIR LGNSFYIEWD
RKMYYARNDT PAEARTTTLN EELGQIKYVF SDKTGTLTQN IMTFNKCSIN GKTYDVFDYM
GQRLEITEHT DTVDFSFNPL ADTRFQFHDH SLVEVVKLEN PEVHAFFRLL ALCHTVMAEE
KTEELVYQAQ SPDEGALVTA ARNFGFVFRS RTPESVSIVE MGQPRTYDLL AILDFNNVRK
RMSVIRSPEG KLSLYCKGAD TIIYERLHQS CSKLMDVTTE HLNEFAGEGL RTLALAYKDL
DEEYLSEWQQ RHHEASTALE NREEKLDELY EEIEKDLMLL GATAIEDKLQ DGVPHTIEQL
AKADIKVWVL TGDKQETAEN IGYSCNLLRE EMNDVFIVSG NSPEDVRQEL KVMTDEVVNG
EYGLVINGHS LAYALEHSME QEFLRTACMC KAVICCRVTP LQKAQVVELV KKYKQAVTLA
IGDGANDVSM IKAHIGVGIS GQEGMQAVLS SDYSFAQFRF LQRLLLVHGR WSYLRMCKFL
RYFFYKNFTF TFVHFWYAFF CGFSAQTVYD EWFITLYNLV YTALPVLGMS LFEQDVNDAW
SFQHPQLYVP GQLNLYFSKK AFFKCALHSC YSSLVLFFIP YLSIFDTVRD DGKDVADYQS
FAVLTQTCLM FAVTIQLGFE MTYWTAVNTL FVMGSLVMYF AITFTMYCNG LFLMLPAAFP
FITARNSFNQ PNIWLTIVLT SLLCILPVVT HRFLMVQLYP TINDKVMFKV RQAKTKLPPP
TRRARIRRTS SRRSGYAFSH AQGYGDLVTS NRFLRRPAVS RSSGFTHAGR TTGFSPMGRS
AGYSPTGRPQ NAKVNNVEVT SLQMYRTIGE PSL
//
