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Database: UniProt
Entry: A0A3Q4BZ97_MOLML
LinkDB: A0A3Q4BZ97_MOLML
Original site: A0A3Q4BZ97_MOLML 
ID   A0A3Q4BZ97_MOLML        Unreviewed;      1088 AA.
AC   A0A3Q4BZ97;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000027942.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000027942.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A3Q4BZ97; -.
DR   STRING; 94237.ENSMMOP00000027942; -.
DR   Ensembl; ENSMMOT00000028418.1; ENSMMOP00000027942.1; ENSMMOG00000021126.1.
DR   OMA; APAYWIT; -.
DR   Proteomes; UP000261620; 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:SF177; PHOSPHOLIPID-TRANSPORTING ATPASE; 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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000261620};
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        67..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        90..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        264..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        305..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        790..811
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        823..843
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        872..892
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        912..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        937..962
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        982..1006
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          45..95
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          759..1009
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   COILED          588..615
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1088 AA;  123231 MW;  FBC3CD7E7936DE74 CRC64;
     ARAGGNSAKA GPPFLSVLHK PTLTLSFTAP RSSSRSAVHL FLPQNNAIKT AKYNIFTFFP
     LNLFEQLQRL ANIYFLFLMV LQTIPQVSSL PWFTTAVPVI FIMSITAVKD ASDDIKRHKS
     DAQVNNRRAD VLLDGRLRNE MWMNVQVGDV IKLENNQFVP ADLLLLSSSK PLGLVYLETA
     ELDGLSLSGE VRCEPPNNRL DKFRGNLVLD GQTYALDNDK VLLRGCTLRN TEWCFGLVVF
     GGPDTKLMQN SGKSTFKRTS IDHLMNILVL CVILCTFLTI CNAFWEKGEG SMFTAFLPRE
     PDTDVPLAAL FTFWSYVIVL NTFVPLSLHT SMEVIRLGSS FFIDWDRKMY YPKTDTPAQA
     RTTTLNEELG QIKYIFSDKT GTLTQNIMTF NKCSISGKIE KVDGMIVDFS WNSLADPKFA
     FYDHSLVETV KEGIPEAQAF FRLLALCHTV MPEEKKEGEL FYQARSPDEG ALVTAARNFG
     FVFRSRTPET ITVVEMGSQV IYQLLAVLDF SNVRKRMSVI VRSPEGRLTL YCKGADTIIF
     ERLHPSCNRL KEVTTGHLNE YASDGLRTLA LAYKDLDEAY MVMWKQRHHE ASTAMEGQEE
     KLDELYEEIE KDLLLLAATA VEDKLQDGVP QTIEQLAEAD IKMWVLTGDK QETAENIGYS
     CNMLREEMKD IFIVAAKTAE GAFALEKNLQ LELLRTACMC QTVICCRVTP LQKAQVVQLV
     KKYKQAVTLA IGDGANDVSM IKAAHIGVGI SGQEGMQAVL SSDYSFAQFR YLQRLLLVHG
     RWSYLRMCKF LRYFFYKNFT LSFVHFWYSF FCGFSAQIVY DNWFITLYNT VYTLLPVLGL
     GLFDQDVNDL WSLMFPRLYT PGQLNAYLNK KVFLGCLLHS CFSSLVLFLV PWAAMRNAIR
     DDGKDIADHQ SFAFLAQTCV LVVVCLETHY WTAMNQFFVL ASVLAYFSFS LTLYSNEMFL
     VFTSNFPFIG TARNALKQPS VWLTIFLTSL LCVLPVVALR FALVLLRPTV SDKVRKHLSD
     RFMVRSFRPG FLKSMREVRQ KGSGLDAAVG PGSCQRVKTM GRSYRAKTGR EGERRCFHTS
     LMLDSKQF
//
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