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Database: UniProt
Entry: D0UMM5_CTELI
LinkDB: D0UMM5_CTELI
Original site: D0UMM5_CTELI 
ID   D0UMM5_CTELI            Unreviewed;       173 AA.
AC   D0UMM5;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Phosphatidylinositol 4-kinase type 2 {ECO:0000256|RuleBase:RU367084};
DE            EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
DE   Flags: Fragment;
OS   Ctenolepisma lineatum (Four-lined silverfish) (Lepisma lineata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Zygentoma;
OC   Lepismatidae; Ctenolepisma.
OX   NCBI_TaxID=27553 {ECO:0000313|EMBL:ACY43991.1};
RN   [1] {ECO:0000313|EMBL:ACY43991.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20147900; DOI=10.1038/nature08742;
RA   Regier J.C., Shultz J.W., Zwick A., Hussey A., Ball B., Wetzer R.,
RA   Martin J.W., Cunningham C.W.;
RT   "Arthropod relationships revealed by phylogenomic analysis of nuclear
RT   protein-coding sequences.";
RL   Nature 463:1079-1083(2010).
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|RuleBase:RU367084};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU367084};
CC       Peripheral membrane protein {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   EMBL; GQ886418; ACY43991.1; -; mRNA.
DR   AlphaFoldDB; D0UMM5; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR039756; Lsb6/PI4K2.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   PANTHER; PTHR12865:SF1; PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2; 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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|RuleBase:RU367084};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|RuleBase:RU367084, ECO:0000313|EMBL:ACY43991.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367084};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW   Transferase {ECO:0000256|RuleBase:RU367084}.
FT   DOMAIN          1..173
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACY43991.1"
FT   NON_TER         173
FT                   /evidence="ECO:0000313|EMBL:ACY43991.1"
SQ   SEQUENCE   173 AA;  20178 MW;  6C4EE28065284E7B CRC64;
     GRSCLIPNQG YLSEAGASVV DQKLQLNIVP KTRVVKLVSE TFNYLRIDRQ KSRVKQAVQE
     RFPNVGRHFH RIGLPPKIGS FQLFVEGYKD ADYWLRRFET EQPSQSIQQQ FQFQFERLVV
     LDYIIRNTDR GNDNWLIKYE NPNLETNQNE GEEDWNLVQP PEIKIAAIDN GLA
//
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