ID   A6QLN5_BOVIN            Unreviewed;       479 AA.
AC   A6QLN5;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   02-SEP-2026, entry version 121.
DE   RecName: Full=Phosphatidylinositol 4-kinase type 2 {ECO:0000256|RuleBase:RU367084};
DE            EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN   Name=PI4K2A {ECO:0000313|EMBL:AAI48029.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI48029.1};
RN   [1] {ECO:0000313|EMBL:AAI48029.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI48029.1};
RC   TISSUE=Uterus {ECO:0000313|EMBL:AAI48029.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:ARBA00001686,
CC         ECO:0000256|RuleBase:RU367084};
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC       {ECO:0000256|ARBA:ARBA00004279}. Cytoplasmic vesicle
CC       {ECO:0000256|ARBA:ARBA00004541}. Endosome
CC       {ECO:0000256|ARBA:ARBA00004177}. Golgi apparatus, trans-Golgi network
CC       membrane {ECO:0000256|ARBA:ARBA00037864}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00037864}. Membrane raft
CC       {ECO:0000256|ARBA:ARBA00004285}. Membrane
CC       {ECO:0000256|RuleBase:RU367084}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU367084}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173}. Perikaryon
CC       {ECO:0000256|ARBA:ARBA00004484}. Presynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034111}. Synapse, synaptosome
CC       {ECO:0000256|ARBA:ARBA00034102}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00008941,
CC       ECO:0000256|RuleBase:RU367084}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00269}.
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DR   EMBL; BC148028; AAI48029.1; -; mRNA.
DR   RefSeq; NP_001093786.1; NM_001100316.1.
DR   AlphaFoldDB; A6QLN5; -.
DR   SMR; A6QLN5; -.
DR   STRING; 9913.ENSBTAP00000002604; -.
DR   PaxDb; 9913-ENSBTAP00000002604; -.
DR   GeneID; 507860; -.
DR   KEGG; bta:507860; -.
DR   CTD; 55361; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002010; -.
DR   eggNOG; KOG2381; Eukaryota.
DR   GeneTree; ENSGT00390000010434; -.
DR   HOGENOM; CLU_032516_1_0_1; -.
DR   OMA; IKCDCPL; -.
DR   OrthoDB; 3349449at2759; -.
DR   Reactome; R-BTA-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-BTA-1660514; Synthesis of PIPs at the Golgi membrane.
DR   Reactome; R-BTA-1660516; Synthesis of PIPs at the early endosome membrane.
DR   Bgee; ENSBTAG00000002010; Expressed in retina and 103 other cell types or tissues.
DR   GO; GO:0031083; C:BLOC-1 complex; IEA:Ensembl.
DR   GO; GO:0060198; C:clathrin-sculpted vesicle; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0031901; C:early endosome membrane; IEA:Ensembl.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
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:0035651; F:AP-3 adaptor complex binding; IEA:Ensembl.
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:0006661; P:phosphatidylinositol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR039756; Lsb6/PI4K2.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   PANTHER; PTHR12865:SF7; PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2-ALPHA; 1.
DR   PANTHER; PTHR12865; PHOSPHATIDYLINOSITOL 4-KINASE TYPE-II; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU367084};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW   ProRule:PRU00269}; Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367084};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU367084}; Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Synaptosome {ECO:0000256|ARBA:ARBA00022599};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00269}.
FT   DOMAIN          124..453
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..136
FT                   /note="G-loop"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00269"
FT   REGION          305..313
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00269"
FT   COMPBIAS        31..45
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  54084 MW;  921F79A639E8B749 CRC64;
     MDETSPLVSP ERAQPPDYTF PSGSSAHFPQ VPGGAVRVAA AAGPVSSPPG SPGHDRERQP
     LLDRARGAAA QGQTQTVAAQ AQALAAQAAA AAHAAQAHRE RNEFPEDPEF EAVVRQAELA
     IERGIFPERI YQGSSGSYFV KDPQGKIIAV FKPKNEEPYG QLNPKWTKWL QKLCCPCCFG
     RDCLVLNQGY LSEAGASLVD QKLELNIVPR TKVVYLASET FNYSAIDRVK SRGKRLALEK
     VPKVGQRFNR IGLPPKVGSF QLFVESYKDA DYWLRRFEAE PLPENTNRQL LLQFERLVVL
     DYIIRNTDRG NDNWLIKYDC PMDSSNSRDT DWVVVKEPVI KVAAIDNGLA FPLKHPDSWR
     AYPFYWAWLP QAKVPFSQEI KDLILPKISD PNFVKDLEED LYELFKKDPG FDRGQFHKQI
     AVMRGQILNL TQALKDNKCP LHLVQMPPVI VETARSHQRS SSESYTQSFQ SRKPFFSWW
//