PI4KB_XENTR
ID PI4KB_XENTR Reviewed; 806 AA.
AC A4IID4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) 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}.
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DR EMBL; BC135973; AAI35974.1; -; mRNA.
DR RefSeq; NP_001096204.1; NM_001102734.1.
DR AlphaFoldDB; A4IID4; -.
DR SMR; A4IID4; -.
DR DNASU; 100124755; -.
DR GeneID; 100124755; -.
DR KEGG; xtr:100124755; -.
DR CTD; 5298; -.
DR Xenbase; XB-GENE-997612; pi4kb.
DR InParanoid; A4IID4; -.
DR OrthoDB; 1147978at2759; -.
DR Reactome; R-XTR-1660514; Synthesis of PIPs at the Golgi membrane.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
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 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; 1.
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..806
FT /note="Phosphatidylinositol 4-kinase beta"
FT /id="PRO_0000365171"
FT DOMAIN 55..247
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 525..791
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 69..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..537
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 658..666
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 677..701
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 282..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 90709 MW; E1323728B674D708 CRC64;
MGDTMVEPVP AKLSDPTLVL RGNGGSPLCV ITEGVGEAQM VIDPDVAEKA CQDVLDKVKL
IRGSSAESLD KIDGSDTGDG GSLANGDAGP RHSESCGPPV SASRITEEEE SLIDINSVKS
ARRRQKNNSA KQSWLLRLFE CKLFDVSMAI SYLYNSKEPG VQAYIGNRLF CFRYEDVDFY
LPQLLNMYIH MDEDVGDAIK PYVVHRCRQS INFSLQCAWL LGAYSSDMHI STQRHSRGTK
LRKLILSDEL KPAHKKREIP PLSLAPDTGL SPSKRTHQRS KSDATVSISL SSNLKRTSSN
PKVENDDEPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ RLISELSLLN HKLPARVWLP
TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY VEVLECENFE TSLVPVRIPE NRIRSTRSVE
NLPECGITHE QRASSFTTVP NYDNDDEAWS VDDIGELQVE LPELHTNSCD NISQFSVDSI
TSQESKDPVF IAAGDIRRRL SEQLAHTPTT FRRDPEDPSA VALKEPWQEK VRRIREGSPY
GHFPNWRLLS VIVKCGDDLR QELLAYQVLK QLQSIWESER VPLWIRPYKI LVISADSGMI
EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS CTTEAFLTAQ RNFVQSCAGY CLVCYLLQVK
DRHNGNILLD AEGHIIHIDF GFILSSSPRN LGFETSAFKL TSEFVDVMGG LNGDMFNYYK
MLMLQGLIAA RKHMDRVVQI VEIMQQGSQL PCFHGSSTIR NLKERFHMNM TEEQLQVLVE
QMVDGSMRSI TTKLYDGFQY LTNGIM
