ID I3LH36_PIG Unreviewed; 598 AA.
AC I3LH36;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Phosphatidylinositol 4-kinase type 2 {ECO:0000256|RuleBase:RU367084};
DE EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN Name=PI4K2B {ECO:0000313|Ensembl:ENSSSCP00000024590.2,
GN ECO:0000313|VGNC:VGNC:98190};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000024590.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000024590.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000024590.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000024590.2}
RP IDENTIFICATION.
RG Ensembl;
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: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Early endosome
CC membrane {ECO:0000256|ARBA:ARBA00004146}. Endoplasmic reticulum
CC membrane {ECO:0000256|ARBA:ARBA00004586}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004608}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004395}. Membrane
CC {ECO:0000256|RuleBase:RU367084}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU367084}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00008941,
CC ECO:0000256|RuleBase:RU367084}.
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DR AlphaFoldDB; I3LH36; -.
DR SMR; I3LH36; -.
DR STRING; 9823.ENSSSCP00000024590; -.
DR PaxDb; 9823-ENSSSCP00000025429; -.
DR Ensembl; ENSSSCT00000028294.4; ENSSSCP00000024590.2; ENSSSCG00000027340.4.
DR VGNC; VGNC:98190; PI4K2B.
DR eggNOG; KOG2381; Eukaryota.
DR GeneTree; ENSGT00390000010434; -.
DR HOGENOM; CLU_2399143_0_0_1; -.
DR InParanoid; I3LH36; -.
DR OMA; CLIPLNG; -.
DR OrthoDB; 1332545at2759; -.
DR Reactome; R-SSC-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-SSC-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-SSC-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-SSC-1660516; Synthesis of PIPs at the early endosome membrane.
DR Proteomes; UP000008227; Chromosome 8.
DR Bgee; ENSSSCG00000027340; Expressed in penis and 45 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1070.20; -; 1.
DR InterPro; IPR039756; Lsb6/PI4K2.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR PANTHER; PTHR12865:SF6; PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2-BETA; 1.
DR PANTHER; PTHR12865; PHOSPHATIDYLINOSITOL 4-KINASE TYPE-II; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU367084};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|RuleBase:RU367084};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367084};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 238..568
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 67115 MW; 9474EA1C1A761DED CRC64;
MLPSSAELNP ARPQPGFFPG PGGRWRPRPT TKAPPPAPAA LVLPRRRVLG AQWGAASGQA
GQLSCGRREG QHACEVPWVG PNDAGTQRCR GQTRVPCPSE PGSARKAQRE AMAEPSEPGR
PASAGSGSLE EEEDEEREPL LPRIVLAQPP KGAPGSAVRL VKAAEEEGAA SAGQAGDQEL
LLQPRDASLS PSLGLGRHRS SPTHRDRHRS LGSELNTFLD DPEFADTILK AEQAIEFGVF
PERISQGSSG SYFVKDPKRK IIGVFKPKSE EPYGQLNPKW TKYVHKVCCP CCFGRGCLLP
NQGYLSEAGA SLVDEKLHLD IVPKTRVVWL VSETFNYSAI DRAKSRGKKY ALEKVPKVGR
KFHRVGLPPK IGSFQLFVEG YKEAEYWLRK FEADPLPENI RKQFQSQFER LVILDYIIRN
TDRGNDNWLI KYEKKKQEKE IKEAKWTNVD KESLIKIAAI DNGLAFPFKH PDEWRAYPFH
WAWLPQAKVP FSDEIRNLVL PYISDMNFVQ DLCEDLYELF KTDKRFDKAT FERQMSVMRG
QILNLTQALR DRKSPVQLVQ MPCVIVERSQ GGGQGRIVHL SSSFTQTVHC RKPFFSSW
//
