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Database: UniProt
Entry: A9Y024_9HEXA
LinkDB: A9Y024_9HEXA
Original site: A9Y024_9HEXA 
ID   A9Y024_9HEXA            Unreviewed;       170 AA.
AC   A9Y024;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   Podura aquatica (water springtail).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Poduromorpha; Poduroidea; Poduridae; Podura.
OX   NCBI_TaxID=50589 {ECO:0000313|EMBL:ABW04846.1};
RN   [1] {ECO:0000313|EMBL:ABW04846.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Paq {ECO:0000313|EMBL:ABW04846.1};
RX   PubMed=19085333; DOI=10.1080/10635150802570791;
RA   Regier J.C., Shultz J.W., Ganley A.R., Hussey A., Shi D., Ball B.,
RA   Zwick A., Stajich J.E., Cummings M.P., Martin J.W., Cunningham C.W.;
RT   "Resolving arthropod phylogeny: exploring phylogenetic signal within 41 kb
RT   of protein-coding nuclear gene sequence.";
RL   Syst. Biol. 57:920-938(2008).
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; EU026232; ABW04846.1; -; mRNA.
DR   AlphaFoldDB; A9Y024; -.
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:ABW04846.1};
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..170
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABW04846.1"
FT   NON_TER         170
FT                   /evidence="ECO:0000313|EMBL:ABW04846.1"
SQ   SEQUENCE   170 AA;  19798 MW;  AE871EC0A4DD28F0 CRC64;
     GRSCLVPNQG YLSEAGASLV DQKLQLNVVP KTKVVGLVSE TFNYLRIDRE KARAKRAVFE
     RFPVLGRRFH RIGLPPKKGS FQLFVEGYKD ADYWLRRFET EPLTESVDRE FQLQFERLVV
     LDYIIRNTDR GNDNWLIKYE KPDVRESVDE EWNVVRPPEI RVAAIDNGLA
//
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