ID A0A3Q4BS14_MOLML Unreviewed; 1303 AA.
AC A0A3Q4BS14;
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:ENSMMOP00000024052.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000024052.1}
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 STRING; 94237.ENSMMOP00000024052; -.
DR Ensembl; ENSMMOT00000024454.1; ENSMMOP00000024052.1; ENSMMOG00000018305.1.
DR OMA; FKVAREC; -.
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; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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:SF84; PHOSPHOLIPID-TRANSPORTING ATPASE VD; 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: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 306..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 347..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1046..1066
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1078..1098
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1127..1148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1160..1178
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1185..1210
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1230..1247
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 66..120
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1014..1247
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 30..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1303 AA; 146363 MW; 6DB004CB3AAE23EC CRC64;
MERLHWVQHR CRQLLNGDSG RGWYSAPDGL PNKRSMDAHS SPQRHLGKKR TVVPSSADKE
ELSELLKSYK DNRIKTTKYS FLSFLPKNLF EQLHRFANVY FISLAVLNFV PVVEAFQPEI
AVIPITLVLS VTAVKDIWED YRKFKSDLKC CFDLCWKDVH VGDFVRLSCN EIIPADMLLL
HSSDPRGVCY IETANLDGET NLKQRQVVID LPFQAAEVTL ESFQCRIECE NPNNDLSRFR
GYIEHPNGVR VGLHNSNLLL RSCTIRNTET VVGIVVYAGH ETKAMMNNSG PRYKRSYLEK
RLNTDVLWCV LLLIVMCLTA AIGHGLWLNN LKDPLFETDG DTSPALAGFH VFWTMIIVLQ
VLIPISLYVS IEIVKLGQIY FIHNDLALYN EQLDSRIQCR ALNITEDLGQ IQYLFSDKTG
TLTENKMVFL RCSVFGVEYP HEENARRLEV YEVEKSEAAA RSVTLRSGCS RKSLSCRSLS
CNHSSVSLNT FCAESEDDEQ LPNHIFLWPS VQAKEVVPDP ELVKKLNWLC SPVPPPSDGS
NGSPSSLELA YVTDFFLALA ICNTVVVSSS TQPRHVVPES PAPLKLMIQR LSFSPFSGFS
PPKIKGSPHS FSRLFSLGRT GSFTFSTPSN TPAGGPEPDQ ESKQQIPYPT CQLDLPFDLS
KDSDSDPDDE LLYEAESPDE AALVHAAHAY RCTLRGRSAD RLLVNLPGIG SLDVELLHIL
PFDSNRKRMS VVVRHPLSGQ VVVYTKGADS VIMDLSEPPK GKCPDRSGDN NKKTQKHLDN
YARDGLRTLC IAKKILQEEE YEQWLKRQLL AESSIENREE LLLDSAQRLE TNLTLLGSTG
VLDRLQEEVP ETIESLQRAG IKVWVLTGDK KETAINIAFA CKLLHPNDQL LTVSCGSKDA
CAALLNELKE QTEVRAAGNL REASSDFVLV IDGSTLEWAL QEELKGDFLE LSCGCKAVIC
CRSTPLQKSQ VVQLIRDQLG VMTLAVGDGA NDVGMIQVAD VGIGISGQEG MQAVMSSDFA
ISRFKHLSKL LLVHGHWCYR RLANMILYFF YKNVMYVNLL FWYQFFCGFS GAVMSNSWVL
ILFNLIFTSV PPLIYGVLDQ DLAAETLMNL PELYQMAPYS KVYVPRIFWI TVLDAFYQSL
VCFFMPYFAL AGSDVGELSF GSPINTSALF IILLHQVLEC NTLTWIHVLV LLFSIGSYFG
FVVLFSLFCV TCSPPTNPLG VETLQLSQPL FYFICALTTV TALLPRYKQQ HRHWILSAQI
GEADSEKYRR RMQRWNQKQA EIKRLRVCAD NPGLEHSTAS VVS
//
