PI4KB_DANRE
ID PI4KB_DANRE Reviewed; 835 AA.
AC Q49GP3; B5TXD8; Q08BS7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phosphatidylinositol 4-kinase beta;
DE Short=PI4K-beta;
DE Short=PI4Kbeta;
DE Short=PtdIns 4-kinase beta;
DE EC=2.7.1.67 {ECO:0000250|UniProtKB:Q9UBF8};
GN Name=pi4kb; Synonyms=pik4cb;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ma H., Balla T.;
RT "Phosphatidylinositol 4-kinases of Danio rerio.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Petko J., Kabbani N., Woll M., Decotiis D., Frey C., Hickey K., Craig M.,
RA Canfield V., Levenson R.;
RT "Proteomic analysis of NCS-1 interacting proteins reveals novel signaling
RT pathways required for inner ear development in zebrafish.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first
CC committed step in the production of the second messenger inositol-
CC 1,4,5,-trisphosphate (PIP). {ECO:0000250|UniProtKB:Q9UBF8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000250|UniProtKB:Q9UBF8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000250|UniProtKB:Q9UBF8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UBF8};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UBF8};
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Mitochondrion
CC outer membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACH92118.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY929293; AAY16568.1; -; mRNA.
DR EMBL; FJ032032; ACH92118.1; ALT_SEQ; mRNA.
DR EMBL; BC124584; AAI24585.1; -; mRNA.
DR RefSeq; NP_001030149.2; NM_001034977.2.
DR AlphaFoldDB; Q49GP3; -.
DR SMR; Q49GP3; -.
DR STRING; 7955.ENSDARP00000099330; -.
DR PaxDb; Q49GP3; -.
DR Ensembl; ENSDART00000058666; ENSDARP00000058665; ENSDARG00000040111.
DR Ensembl; ENSDART00000160332; ENSDARP00000130423; ENSDARG00000040111.
DR Ensembl; ENSDART00000182202; ENSDARP00000149614; ENSDARG00000111175.
DR GeneID; 563201; -.
DR KEGG; dre:563201; -.
DR CTD; 5298; -.
DR ZFIN; ZDB-GENE-061013-96; pi4kb.
DR eggNOG; KOG0903; Eukaryota.
DR GeneTree; ENSGT00550000074892; -.
DR HOGENOM; CLU_002446_6_0_1; -.
DR InParanoid; Q49GP3; -.
DR OMA; GNKMFSF; -.
DR OrthoDB; 1147978at2759; -.
DR PhylomeDB; Q49GP3; -.
DR TreeFam; TF102042; -.
DR Reactome; R-DRE-1660514; Synthesis of PIPs at the Golgi membrane.
DR PRO; PR:Q49GP3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000040111; Expressed in gastrula and 25 other tissues.
DR ExpressionAtlas; Q49GP3; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0060872; P:semicircular canal development; IMP:ZFIN.
DR Gene3D; 1.10.1070.11; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 2.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Endoplasmic reticulum; Kinase; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..835
FT /note="Phosphatidylinositol 4-kinase beta"
FT /id="PRO_0000365169"
FT DOMAIN 59..262
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 554..820
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..566
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 687..695
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 706..730
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 14..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 100
FT /note="S -> L (in Ref. 1; AAY16568)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="R -> G (in Ref. 3; AAI24585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 835 AA; 94059 MW; DE044DB4C925B795 CRC64;
MGDTELELSP THLEELQKSP STSTTSSLSL PSSPSSGPHP LTSSSPSTSE GLPTSSPPLD
VISEGLGELS LVIDTEVAKK ACQEVLQKVK FLKGDGEVSS ASSEPILANG TAHPEANDGG
QPPKISEEEV EPIKSVRRRQ KNNSSKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI
GNRLFSFRNE DVDFYLPQLL NMYIHMDEDV GDAIKPYVVY RCRQSINFSL QCAWLLGAYS
SDMHISTQRH SRGTKLRKLI LSDELKPSSQ RIRREVPQPP PPYPPPLHHG PGMSEHSLSP
SKRTHQRSKS DATVSISLSS NLKRTASNPK VETSQDEPVR LTPQREFIKS LMGIGKRLAT
LPTKEQKTQR LISELSLLNH KLPARVWLPT AAFDHHVVRV PHTQAVVLNS KDKAPYLIYV
EVLECENFET SSVPVRIPET QIRSTRSVEN LPDCGITPDQ RASSFSTVPN YDNDDEAWSV
DDIGELQVEL PEIHTNSCDN ISQFSVDSIT SQESKEPIFI AAGDIRRRLS EQLAHTPTTF
RKDPEDPSAV ALKEPWQEKV RRIREGSPYG HLPNWRLLSV IVKCGDDLRQ ELLAYQVLKQ
LQIIWEQERV PLWIKPYKIL VISSDSGMIE PVVNAVSIHQ VKKQSQLLLL DYFRQEHGNF
NTEEFLTAQR NFVQSCAGYC LICYLLQVKD RHNGNILLDS EGHIIHIDFG FILSSSPRNL
GFETSAFKLT SEFVDVMGGL DGDMFNYYKM LMLQGLIAAR KHMEKVIQIV EIMQQGSQLP
CFHGSSTIRN LKERFHMNLT EEQLQVLVEQ MVDGSMRSIT TKLYDGFQYL TNGIM
