UniProt: A0A3Q3W7G7

Database: UniProt
Entry: A0A3Q3W7G7_MOLML

LinkDB:  A0A3Q3W7G7_MOLML 
Original site:  A0A3Q3W7G7_MOLML

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (15)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
All databases (25)   

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ID   A0A3Q3W7G7_MOLML        Unreviewed;      1193 AA.
AC   A0A3Q3W7G7;
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:ENSMMOP00000004539.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000004539.1}
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; A0A3Q3W7G7; -.
DR   STRING; 94237.ENSMMOP00000004539; -.
DR   Ensembl; ENSMMOT00000004622.1; ENSMMOP00000004539.1; ENSMMOG00000003611.1.
DR   OMA; PECIHKL; -.
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:SF46; PHOSPHOLIPID-TRANSPORTING ATPASE ID; 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        60..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        276..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        318..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        841..862
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        874..894
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        924..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        960..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        993..1014
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1034..1057
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          16..82
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          810..1063
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1193 AA;  135133 MW;  37AF1C11B6200C90 CRC64;
     ICVCARKRAV KEERRVRAND RQYNEKFQYA SNCIMTSKYN IITFLPVNLF EQFQEVANTY
     FLFLLILQLI PQISSLSWFT TIVPLALVLS ITAVKDATDD YFRHKSDNQV NNRQSQVLIR
     GSLQSQKWMN VRVGDIIKLE NNQFVAADLL LLSTSEPHGL CYIETAELDG ETNMKVRQSV
     SVTSELGDQN NLASFDGEVV CEPPNNKLDR FCGTLHWRHK RYTLTNQNVL LRGCVLRNTE
     TCYGLVIFAG PDTKLMQNSG RTKFKRTSID RLMNTLVLWI FGFLVCMGVI LAVGNAVWES
     EVGSLFQSYL PWDPPVNNFL FSAFLSFWSY VIILNTVVPI SLYVSVEVIR LGHSYFINWD
     QQMFWSQCNT PAEARTTTLN EELGQVEYIF SDKTGTLTQN IMSFNKCSIN GQTYGETTDP
     LGPQPKRLDF TRFNPLADPD FCFYDGTLLE SVTVGNSHTH EFFRLLSLCH TVMSEEKSEG
     ELVYKAQSPD EGALVTAARN FGFVFRSRTP STITTTEMGR PVTYTLLAIL DFNNIRKRMS
     VIVRNPEGRI RLYCKGADTV LLERLHPCNQ ELMNITSDHL NEYGADGLRT LALAYRDLSE
     DEWEAWSESH HCADRATSCR EDRLAATYEE IEQDMMLLGA TAIEDKLQEG VPETIAVLSL
     ANIKIWVLTG DKQETAVNIG YSCKMLTDDM TEVFIISGHT VQSVRQELRS VFRYLMDNIS
     EEFALIINGH SLAHALEADM EMEFVSTACA CKAVICCRVT PLQKAQVVEL IKKHKRAVTL
     AIGDGANDVS MIKSAHIGVG ISGQEGIQAV LASDYSFSQF RFLQRLLLVH GRWSYLRMCR
     FLCYFFYKNF AFTMVHFWFG FFCGFSAQTV YDQYFITLFN IVYTSLPVLA MGTFDQDVPD
     QRSLEYPKLY EPGQLNLLFN KREFFICIAQ GIYTSVVLFF IPYAILSDAT QSTGVPLADY
     QTFAVTTATA LVIVVSVQIA LDTGFWTVFN HVFVWGSLGF YFTIMFALHS QTLFRIFPNQ
     FRFVGHAQST LLQPVVWLTI ALATVICIVP VLVFRFLKVD LKPQLSDMVR HTQLVRQKKK
     KLVGSTGGAW RGVGRIAEGR LGARGGSRRS GYAFAHQEGF GELITSGKNM RLSSLALATF
     ASKHSSSWID TLRRKKHTRA HTPPIASGES EYPLRQLKKQ QWTVKHGLSC PQS
//

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