ID D0UMQ8_9MYRI Unreviewed; 172 AA.
AC D0UMQ8;
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 Polyxenus fasciculatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Diplopoda;
OC Penicillata; Polyxenida; Polyxenidae; Polyxenus.
OX NCBI_TaxID=58786 {ECO:0000313|EMBL:ACY44024.1};
RN [1] {ECO:0000313|EMBL:ACY44024.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GQ886451; ACY44024.1; -; mRNA.
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 Gene3D; 1.10.1070.20; -; 1.
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:ACY44024.1};
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..172
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACY44024.1"
FT NON_TER 172
FT /evidence="ECO:0000313|EMBL:ACY44024.1"
SQ SEQUENCE 172 AA; 19808 MW; A76024AE0B2B43A5 CRC64;
GRSCLVPNQG YLSESGASLV DQKLQLNIVP KTKVVRLASE TFNYLAIDRA KSRAKRNVSE
RFPSVGRRFN RIGLPLKTGS FQLYVQGYKT ADYWIRRFES ESLPESALKQ FQMQFEKIVV
LDYIIRNTDR NNDNWLIRYE KSEVEESVKE YGDWSVVKPP EIKIAAIDXG LA
//