UniProt: A0A3Q1AHU8

Database: UniProt
Entry: A0A3Q1AHU8_AMPOC

LinkDB:  A0A3Q1AHU8_AMPOC 
Original site:  A0A3Q1AHU8_AMPOC

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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   A0A3Q1AHU8_AMPOC        Unreviewed;      1113 AA.
AC   A0A3Q1AHU8;
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};
GN   Name=ATP11A {ECO:0000313|Ensembl:ENSAOCP00000000592.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000000592.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000000592.1}
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; A0A3Q1AHU8; -.
DR   STRING; 80972.ENSAOCP00000000592; -.
DR   Ensembl; ENSAOCT00000014676.1; ENSAOCP00000000592.1; ENSAOCG00000003461.1.
DR   GeneTree; ENSGT00940000157849; -.
DR   OMA; DAQITEY; -.
DR   Proteomes; UP000257160; 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; 3.
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:UP000257160};
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        72..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        293..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        346..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        884..902
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          45..99
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   1113 AA;  127497 MW;  BF27D18BE36ECCDF CRC64;
     MDERESEGGT EERIRCCVGE ENWVDSRTIY IGHKEPPPGT EAFIQQRFPD NRIVSSKYTF
     WNFIPKNMFE QFRRVANFYF LIIFLVQLII DTPTSPITSG LPLFFVITVT AIKQGYEDWL
     RHKADNAVNK CPVHVVQHGK VLRKQSRKLR VGDVVLVKED ESFPCDLILL SSSRDDGTCY
     VTTASLDGES SHKTYYAVQD TKAYNTEKEV DSIHATIECE QPQPDLYKSV QHTDLNKAFL
     PLGSENLLLR GATLKNTEYI FAVAIYTGME TKMALNYQSK SQKRSAVEKS MNAYLVVYLC
     ILISKAVINT VLKYAWQADP NRDEPWYNER TEVERQRHLI RAFTDFLAFM VLFNYIIPVS
     MYVTVEMQKF LGSYFIMWDD EMFDEELGER AVVNTSDLNE ELGQVEYVFT DKTGTLTENN
     MEFIECCVDG HVYVPHVICN GQVMPGAAGM DMIDTSPGPK AREHEELFFR ALCLCHTVQV
     KEEETVDGIK HGIHQGKSTS FYISSSPDEV ALVEGMKRLG FTYLRLKDGQ MEILNREDEI
     ERFELLEVLT FDSVRRRMSV IVRANTGELY LFCKGADSSI FPRVISGKVD QVRARVEHNA
     VEGLRTLCVA YRPLSPEQYQ EVCHLLSSAK LALQDRDKRL AEAYDLIEKD LILLGATAVE
     DRLQEKAADT IESLHKAGMK VWVLTGDKME TAAATCYASK LFRRNTQILE LTTKRTEEQS
     LHDVLFDLSR TVLRQHGGMT RDTFSGLSGD CTDYGLIIDG ATLSAVMRPG QEDSNSGNYK
     EIFLEICRNC SAVLCCRMAP LQKAQIVKLI KASKEHPITL AIGDGANDVS MILEAHVGIG
     IMGKEGRQAV RNSDYAIPKF KHLKKMLLVH GHYYYIRISE LVQYFFYKNV CFIFPQFLYQ
     FFCGFSQQPL YDTAYLTLYN ISFTSLPILL YSLIEQHINM DILKKDPSLY RDIAKNSLLR
     WPSFIYWTVL GVYDAIVMFF GAYFLFDNTT FTSNGQMFGN WTFGTLVFTV LVFTVTFKLA
     LDTHYWTWIN HFVIWGSLIF FVVFSLLWGG IIWPFLNYQR MYYVFMQMLS SGPAWLSIIL
     LITASLLPDV VKKVIWRALW PTTTERIQVG SHT
//

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