UniProt: A0A3Q3KZS3

Database: UniProt
Entry: A0A3Q3KZS3_9LABR

LinkDB:  A0A3Q3KZS3_9LABR 
Original site:  A0A3Q3KZS3_9LABR

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (17)   
   InterPro (11)   
   Pfam (5)   
   PROSITE (1)   
All databases (27)   

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ID   A0A3Q3KZS3_9LABR        Unreviewed;      1163 AA.
AC   A0A3Q3KZS3;
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=ATP11B {ECO:0000313|Ensembl:ENSLBEP00000002119.1};
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:ENSLBEP00000002119.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000002119.1}
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; A0A3Q3KZS3; -.
DR   STRING; 56723.ENSLBEP00000002119; -.
DR   Ensembl; ENSLBET00000002248.1; ENSLBEP00000002119.1; ENSLBEG00000001582.1.
DR   GeneTree; ENSGT00940000156162; -.
DR   InParanoid; A0A3Q3KZS3; -.
DR   OrthoDB; 275833at2759; -.
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; 3.
DR   PANTHER; PTHR24092:SF57; PHOSPHOLIPID-TRANSPORTING ATPASE IF; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00122; E1-E2_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   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        66..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        288..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        342..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        839..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        937..959
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        971..994
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1006..1030
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1036..1061
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          36..90
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          823..1076
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1163 AA;  132360 MW;  22BB0D6600ADA4AF CRC64;
     MLRWIRQQLG FDPPHQSDTR TVYVANRFPE HGHYVPQRFA DNRIISSKYT VWNFVPKNLF
     EQFRRIANFY FLIIFLVQLM IDTPTSPVTS GLPLFFVITV TAIKQGYEDW LRHKADNEVN
     GAPVFVVRSG SLVQTRSKNI RVGDIVRVAK DETFPADLAL LSSDRAEGTC HITTASLDGE
     TNLKTHFSVA ETSVCQSVSQ LEALQAVVEC QQPEADLYRF VGRITVTQLG EEIVRPLGPE
     NLLLRGARLK NTKEIFGVAI YTGMESKMAL NYKCKSQKRS AVEKSMNTFL IIYLCILLFE
     AVLSTILKYA WQAEEKWDEP FYNQKTEQEK NSSPILKFIS DFLAFLVLYN FIIPISLYVT
     VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ VEYVFTDKTG TLTENEMQFR
     ECSINGTKYR EVNGKLVPEG MTEESPDGST PQLMGEELLF LKAVSLCHTV QISYDQPDCL
     VGGGDPFSQV NGFSSSHMEY YASSPDEKAL VEATKRIGVA FTCSNGETVE IKTFGKSEKY
     KLLHVLEFDA NRRRMSVILQ TPSGGQVLFT KGAESAILPF TTSGEIEKTR LHVDEFALKG
     LRTLVVACRH FRPEEYIDVD RRLNAARTAL QQREERLQEA FSYIEKDLHL LGATGVEDKL
     QDKVQETIEA LRLAGIKVWV LTGDKSETAV SVSLSCGHFH RTMNILELLQ QRSDNECAEQ
     LRRLARRIKE DNVIQHGLVV DGASLSLALR EHEKLFMEVC KNCSAVLCCR MAPLQKAKVV
     RLLKTSPEKP ITLAIGDGAN DVSMIQEAHV GIGIMGKEGR QAVRNSDYAI ARFKFLAKLL
     LVHGHFYYIR IATLVQYFFY KNVCFITPQF LYQFFCLFSQ QTLYDSVYLT LYNICFTSLP
     ILVYSLFEQL VHPHILQSKP ALYRDISKNS LLSFRTFLYW TLLGFCHAFV FFFGSYILMG
     EDTTLMGNGQ MFGNWTFGTL VFTVMVITVT LKLALETHFW TWMNHFVTWG SIAFYFIFSL
     FYGGIIWPFL HTQDMYFVFV QLLSSGSAWF AIIIIIITCL FPDVVKKVFY RHLQPTSTQK
     SQSLSIPQEQ ALSCMESLCC YQHGQSGCSR LARLMEQMTG QCRAGANQCT ASSRSNRSWS
     DTENFYSNDR SILTLSPIES THC
//

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