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Database: UniProt
Entry: A0A1S3WLI1_ERIEU
LinkDB: A0A1S3WLI1_ERIEU
Original site: A0A1S3WLI1_ERIEU 
ID   A0A1S3WLI1_ERIEU        Unreviewed;       822 AA.
AC   A0A1S3WLI1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN   Name=PI4KB {ECO:0000313|RefSeq:XP_016046999.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016046999.1};
RN   [1] {ECO:0000313|RefSeq:XP_016046999.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036767};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC         Evidence={ECO:0000256|ARBA:ARBA00036767};
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00004308}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004394}. Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004450}. Rough endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00037860}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00037860}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   RefSeq; XP_016046999.1; XM_016191513.1.
DR   AlphaFoldDB; A0A1S3WLI1; -.
DR   CTD; 5298; -.
DR   OrthoDB; 147843at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd22246; PI4KB_NTD; 1.
DR   CDD; cd05168; PI4Kc_III_beta; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 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; IPR049160; PI4KB-PIK1_PIK.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   3: Inferred from homology;
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          42..242
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          520..807
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   822 AA;  91889 MW;  67BFBE042BA3DCBB CRC64;
     MGDTVVESAP LKPASEPASG SPGSNGGSLL SVITEGVGEL SVIDPEVAQK ACQEVLEKVK
     LLHGGVAVSS RDTPLELVNG DGVGTEIRCL DDPPAQIREE EEELEAAVAS GTAKGARRRR
     QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL
     NMYIHMDEDV GDAIKPYIVH RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI
     LSDELKPAHR KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN
     EDEPIRLAPE REFIKSLMAI GKRLATLPTK EQKTQRLISE LSLLNHKLPA RVWLPTASFD
     HHVVRVPHTQ AVVLNSKDKA PYLIYVEVLE CENFDTTNVP ARIPENRIRS TRSVENLPEC
     GITHEQRAGS FSTVPNYDND DEAWSVDDIG ELQVELPEVH TNSCDNISQF SVDSITSQES
     KEPVFIAAGD IRRRLSEQLA HTPTAFKRDP EDPSAVALKE PWQEKVRRIR EGSPYGHLPN
     WRLLSVIVKC GDDLRQELLA FQVLKQLQAI WEQERVPLWI KPYKILVISA DSGMIEPVVN
     AVSIHQVKKQ SQLSLLDYFL QEHGSYTTEA FLSAQRNFVQ SCAGYCLVCY LLQVKDRHNG
     NILLDAEGHI IHIDFGFILS SSPRNLGFET SAFKLTTEFV DVMGGLDGDM FNYYKMLMLQ
     GLIAARKHMD KVVQIVEIMQ QGCRCCSGAS PSGPVMTVAQ VICSQLPCFH GSSTIRNLKE
     RFHMSMTEEQ LQLLVEQMVD GSMRSITTKL YDGFQYLTNG IM
//
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