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Database: UniProt
Entry: A8X2T9_CAEBR
LinkDB: A8X2T9_CAEBR
Original site: A8X2T9_CAEBR 
ID   A8X2T9_CAEBR            Unreviewed;       406 AA.
AC   A8X2T9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Phosphatidylinositol 4-kinase type 2 {ECO:0000256|RuleBase:RU367084};
DE            EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN   ORFNames=CBG06673 {ECO:0000313|EMBL:CAP26949.2,
GN   ECO:0000313|WormBase:CBG06673}, CBG_06673
GN   {ECO:0000313|EMBL:CAP26949.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP26949.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP26949.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP26949.2,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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; HE601320; CAP26949.2; -; Genomic_DNA.
DR   RefSeq; XP_002647585.1; XM_002647539.1.
DR   AlphaFoldDB; A8X2T9; -.
DR   STRING; 6238.A8X2T9; -.
DR   EnsemblMetazoa; CBG06673.1; CBG06673.1; WBGene00028916.
DR   GeneID; 8589583; -.
DR   WormBase; CBG06673; CBP32211; WBGene00028916; -.
DR   eggNOG; KOG2381; Eukaryota.
DR   HOGENOM; CLU_032516_3_0_1; -.
DR   InParanoid; A8X2T9; -.
DR   OMA; CLIPLNG; -.
DR   OrthoDB; 1332545at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR039756; Lsb6/PI4K2.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   PANTHER; PTHR12865:SF5; PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2; 1.
DR   PANTHER; PTHR12865; PHOSPHATIDYLINOSITOL 4-KINASE TYPE-II; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   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:UP000008549};
KW   Transferase {ECO:0000256|RuleBase:RU367084}.
FT   DOMAIN          50..353
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   406 AA;  46406 MW;  B1B1A9F31976D035 CRC64;
     MSANSSLSQV EPETDSSSIY DLTSSLEHRK KVDDEFQLVF RKAQDAINKG IQPSLIPEGS
     SGSYFVYGLE GEILGVFKPK DEEPFASLNP KWPKFFQRML CFCCFGRACL IPNTGYLSEA
     AASIVSEMLQ LDVVPTTRIV KLASPSFFYS RFFGHYDVRP KEGSFQLYVN GYESGNTVFA
     RWNYDKNLLS EEEEAKFQLL FQKMCIVDYV IRNTDRHMDN LLVRHVPGHE INLAAIDNGL
     AFPVRHPECT SRFRSFPFRW SNLPWAQAEF DQTLRRHVLS LLTPQFVHRL CVDLKKLFRH
     GIASSNYMLV NSQLRVVRGQ IWNLRQALIA NESPCDMARR DPIIVSRSSD IEMRNPPPHR
     GMIGLLSSRL ATPTSNYAEV TTTKTAIEFV EEPKKVPEDD NLLINF
//
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