UniProt: A0A3Q3G623

Database: UniProt
Entry: A0A3Q3G623_9LABR

LinkDB:  A0A3Q3G623_9LABR 
Original site:  A0A3Q3G623_9LABR

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (26)   

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ID   A0A3Q3G623_9LABR        Unreviewed;      1158 AA.
AC   A0A3Q3G623;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=ATP11A {ECO:0000313|Ensembl:ENSLBEP00000026383.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000026383.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000026383.1}
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; A0A3Q3G623; -.
DR   STRING; 56723.ENSLBEP00000026383; -.
DR   Ensembl; ENSLBET00000027680.1; ENSLBEP00000026383.1; ENSLBEG00000020048.1.
DR   GeneTree; ENSGT00940000157849; -.
DR   InParanoid; A0A3Q3G623; -.
DR   Proteomes; UP000261660; 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; 2.
DR   PANTHER; PTHR24092:SF33; PHOSPHOLIPID-TRANSPORTING ATPASE IH; 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:UP000261660};
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        68..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        293..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        347..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        914..934
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        964..986
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        998..1020
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1032..1056
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1062..1087
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          37..95
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          850..1102
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1158 AA;  132994 MW;  9D2F3DE845453BF1 CRC64;
     FVCSLIQTET KPCVGEENWV DSRTIYIGHK EPPSGTEAFI QQRYPDNRIV SSKYTFWNFI
     PKNMFEQFRR IANFYFLIIF LIQLIIDTPT SPITSGLPLF FVITVTAIKQ GYEDWLRHKA
     DNSVNQCPVH VVQHGKVVRK QSRKLRVGDV VSVKEDETFP CDLILLSTSR EDGTCFVTTA
     SLDGESSHKT YYAVQDTRAY NTEKEVDSIH ATIECEQPQP DLYKFVGRIN IYMDNEPVAR
     PLGSENLLLR GATLKNTEYI YAVAIYTGME TKMALNYQSK SQKRSAVEKS MNAYLVVYLC
     ILIGKSIINT IMKYAWQADT NRDEPWYNHR TVSERERHIL IRAFTDFLAF MVLFNYIIPV
     SMYVTVEMQK FLGSYFIMWD DEMFDEELGE RAVVNTSDLN EELGQVEYVF TDKTGTLTEN
     NMEFIECCVD GHVYVPNIIC NGQVMTGAGM DMIDTSPGPG AREHEELFFR ALCLCHTVQV
     KEEETVDGIK QGIHQGKSTS FYISSSPDEV ALVEGMKRLG FTFLRLKDSH MEILNREDEI
     ERFELLEVLT FDSVRRRMSV IVRSSTGELY LFCKGADSSI FPRVISGKVE QIKARVEHNA
     VEGLRTLCVA YRPLSPEQYQ EVCDLLNGAK LALQDRDRQL AEAYDLIEKD LILLGATAVE
     DRLQDKAADT IESLHKAGMK VWVLTGDKME TAAATCYASK LFRRNTQILE LTTKRTEEQS
     LHDVLFDLSR TVLRQHGGMT RDTFSSLSGD CTDYGLIIDG ATLSAVMRPA QEDSNSGNYK
     EIFLEICRNC SAVLCCRMAP LQKAQIVKLI KASKEHPITL AIGDGANDVS MILEAHVGIG
     IMGKEGRQAV RNSDYAIPKF KHLKKMLLVH GHYYYIRIAE LVQYFFYKNV CFIFPQFLYQ
     FFCGFSQQPL YDTAYLTLYN ISFTSLPILL YSLIEQHINM DILKKDPSLY RDIAKNSLLR
     WRNFIYWTVL GVYDAVVMFF GAYFLFDNTT FTSNGQMFGN WTFGTLVFTV LVFTVTFKLA
     LDTHYWTWIN HFIIWGSLIF FVIFSLLWGG IIWPFLNYQR MYYVFMQMLS SGPAWLSIIL
     LITASLVPDV VKKVIWRALW PTTTERIQVG SHTHVLCRSC GCIKEEEEAF KMIYQQIYLR
     AQVLQKRKEQ LLLLGKFI
//

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