UniProt: I3JHK7

Database: UniProt
Entry: I3JHK7_ORENI

LinkDB:  I3JHK7_ORENI 
Original site:  I3JHK7_ORENI

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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   I3JHK7_ORENI            Unreviewed;      1121 AA.
AC   I3JHK7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 80.
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:ENSONIP00000008351.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000008351.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Ensembl:ENSONIP00000008351.2}
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; I3JHK7; -.
DR   STRING; 8128.ENSONIP00000029834; -.
DR   Ensembl; ENSONIT00000008356.2; ENSONIP00000008351.2; ENSONIG00000006612.2.
DR   eggNOG; KOG0206; Eukaryota.
DR   GeneTree; ENSGT00940000157849; -.
DR   HOGENOM; CLU_000846_3_1_1; -.
DR   TreeFam; TF326897; -.
DR   Proteomes; UP000005207; 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:UP000005207};
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..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        286..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        340..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        902..922
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        952..974
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        986..1008
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1020..1044
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1050..1075
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          33..87
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          838..1090
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1121 AA;  128330 MW;  9F0F364737EF4C5F CRC64;
     PDCSCVGEEI WVDSRTVYIG HKEPPPGAEA YIPQRYPDNR IVSSKYTFWN FIPKNLFEQF
     RRIANFYFLV IFLVQLIIDT PTSPVTSGLP LFFVITVTAI KQGYEDWLRH KADCSINECP
     VDVVQQGKVV RTQSHKLRVG DIVVVKEDET FPCDLILLSS SRPDGTCFVT TTSLDGESSH
     KTYYAIPDTM AFRTEQEVDS LHATIECEQP QPDLYKFVGR INIYKDKEEP VARPLGAENL
     LLRGATLKNT QHIHAVAVYT GMETKMALNY QSKSQKRSAV EKSMNAFLIV YLCILISKAV
     INTVLKYAWQ WSPDRDEPWY NHRTEHERQR HVVIRAFTDF LAFMVLFNYI IPVSMYVTVE
     MQKFLGSYFI SWDEEMFDEE LGEGAQVNTS DLNEELGQVE YVFTDKTGTL TENNMEFIEC
     CVDGNVYIPH AICNGQILSA ASSIDMIDAS PGGYRREYED LFFRALCLCH TVQVKEEETV
     DGIKRGIHQG RPTSFYISSS PDEVALVEGM KRLGYTYLRL KDNYMEILNK DDEIERFELL
     HVLNFDSVRR RMSVIVKSSS GDYLLFCKGA DSSIFPRVVS GKVEQVKARV EQNAVEGLRT
     LCVAYRRLSE SEYQEACHHL MEAKLALQDR EQRLAQAYDI IERDFVLLGA TAVEDRLQEK
     AADTIESLHK AGMKVWVLTG DKMETAAATC YASKLFRRTT QILELTKKRT EEQSLHDVLF
     ELNRTVLRQR SISGLSVDCL DFGLIIDGAT LSAVLKPNQE GAGHGNYREI FLEICRNCSA
     VLCCRMAPLQ KAQIVKLIKA SKEHPITLAI GDGANDVSMI LEAHVGIGIM GKEGRQAARN
     SDYAIPKFKH LKKMLLVHGH YYYIRIAELV QYFFYKNVCF IFPQFLYQFF CGFSQQPLYD
     TAYLTLYNIS FTSLPILLYS LVEQHVSMDT LKREPSLYRD IAKNSLLRWP VFLYWTCLGV
     FDAVVFFFGA YFLFDNTTFT SNGQMFGNWT FGTLIFTVLV FTVTLKLALD THHWTWINHF
     VIWGSLLFYV IFSLLWGGII WPFLNYQRMY YVFMQMLSSG PAWLSIILLI TVSLLPDVIK
     KVLCRAMCPT ATERAQSTRP CLTVEPSTIF MLSQSSSRMS F
//

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