PI4KB_XENLA
ID PI4KB_XENLA Reviewed; 804 AA.
AC Q6GN16;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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; BC073706; AAH73706.1; -; mRNA.
DR RefSeq; NP_001086017.1; NM_001092548.1.
DR AlphaFoldDB; Q6GN16; -.
DR SMR; Q6GN16; -.
DR DNASU; 444446; -.
DR GeneID; 444446; -.
DR KEGG; xla:444446; -.
DR CTD; 444446; -.
DR Xenbase; XB-GENE-997616; pi4kb.L.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 444446; Expressed in internal ear and 19 other tissues.
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:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
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..804
FT /note="Phosphatidylinositol 4-kinase beta"
FT /id="PRO_0000365170"
FT DOMAIN 55..245
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 523..789
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 69..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..535
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 656..664
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 675..699
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 87..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 90455 MW; 9E56D98498F8A128 CRC64;
MGDTMVEPVP VKLSDQSLVL RGNGGSALCV ITEGVGEASL VIDPDVAQKA CQEVLEKVKM
IHGSSVESLD KVDGGDAGDG GSLANGDTEP KLTNTGHTST SSRINEEESP LDINSVKNAR
RRQKNNSAKQ SWLLRLFECK LFDVSMAISY LYNSKEPGVQ AYIGNRLFCF RYEDVDFYLP
QLLNMYIHMD EDVGDAIKPY VVHRCRQSIN FSLQCAWLLG AYSSDMHIST QRHSRGTKLR
KLILSDELKP AHKKREIPPL SLAPDTGLSP SKRTHQRSKS DATVSISLSS NLKRTSSNPK
VENDDEPVRL APEREFIKSL MGIGKRLATL PTKEQKTQRL ISELSLLNHK LPARVWLPTA
GFDHHVVRVP HTQAVVLNSK DKAPYLIYVE VLECENFETS LVPVRIPENR IRSTRSVENL
PECGITHEQR ASSFTTVPNY DNDDEAWSVD DIGELQVELP ELHTNSCDNI SQFSVDSITS
QESKDPVFIA AGDIRRRLSE QLAHTPTTFR RDPEDPSAVA LKEPWEEKVR RIREGSPYGH
FPNWRLLSVI VKCGDDLRQE LLASQVLKQL QSIWESERVP LWIRPYKILV ISGDSGMIEP
VVNAVSIHQV KKQSQLSLLH YFLQEHGSCT TEAFLTAQRN FVQSCAAYCL VCYLLQVKDR
HNGNILLDAE GHIIHIDFGF ILSSSPRNLG FETSAFKLTA EFVDVMGGLN GDMFNYYKML
MLQGLIAARK HMDKVVQVVE IMQQGSQLPC FHGSSTIRNL KERFHMNMTE EQLQILVEQM
VDGSMRSITT KLYDGFQYLT NGIM
