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Database: UniProt
Entry: Q5F3P4_CHICK
LinkDB: Q5F3P4_CHICK
Original site: Q5F3P4_CHICK 
ID   Q5F3P4_CHICK            Unreviewed;      1046 AA.
AC   Q5F3P4;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE            EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
GN   ORFNames=RCJMB04_11a21 {ECO:0000313|EMBL:CAH65240.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|EMBL:CAH65240.1};
RN   [1] {ECO:0000313|EMBL:CAH65240.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CB {ECO:0000313|EMBL:CAH65240.1};
RC   TISSUE=Bursa {ECO:0000313|EMBL:CAH65240.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836,
CC         ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.153;
CC         Evidence={ECO:0000256|ARBA:ARBA00023981};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293;
CC         Evidence={ECO:0000256|ARBA:ARBA00023981};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004805}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   EMBL; AJ851606; CAH65240.1; -; mRNA.
DR   RefSeq; NP_001012714.1; NM_001012696.1.
DR   AlphaFoldDB; Q5F3P4; -.
DR   GeneID; 419444; -.
DR   KEGG; gga:419444; -.
DR   CTD; 5293; -.
DR   VEuPathDB; HostDB:geneid_419444; -.
DR   PhylomeDB; Q5F3P4; -.
DR   UniPathway; UPA00220; -.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
DR   GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:InterPro.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd08693; C2_PI3K_class_I_beta_delta; 1.
DR   CDD; cd05174; PI3Kc_IA_delta; 1.
DR   Gene3D; 3.10.20.770; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR002420; PI3K-type_C2_dom.
DR   InterPro; IPR003113; PI3K_ABD.
DR   InterPro; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR000341; PI3K_Ras-bd_dom.
DR   InterPro; IPR037703; PI3Kdelta_dom.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10048:SF35; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT DELTA ISOFORM; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF02192; PI3K_p85B; 1.
DR   Pfam; PF00794; PI3K_rbd; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00143; PI3K_p85B; 1.
DR   SMART; SM00144; PI3K_rbd; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51547; C2_PI3K; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51544; PI3K_ABD; 1.
DR   PROSITE; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   2: Evidence at transcript level;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          16..105
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          187..278
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          319..476
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          500..677
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          748..1029
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1046 AA;  120279 MW;  826602503C32DF45 CRC64;
     MPRGIYCPME FWSKGENQNI QVDFLLPTGI YLNLSVPCNA SLDTIKQVVW KHAQYEPLYH
     MLSDPEAYVF TCINQTAEQQ ELEDEQRRLC DIQPFLPVLR LVAREGDRVK KLINSQISLL
     IGKGLHEFDS VQDPEVNDFR TKMCQFCEER AAKRQQLSWA AWMEYNFPLQ LEPMAKGLGT
     GLLHTPIKNI FVNVKFQSGG ESFTFQISPN EFPITLMSYA VKKQATVFRH ETMENPEDYT
     LQVNGKYEYL YGNYPLYQFQ YIRSCLHRGL TPHLTMVHSS TIIAMRDEQV NSIANPPKMA
     VKPPPLPKKK PNYGSLWSLE QSFYIELVQG SKVNADERMK LVVQAGLFHG NEMLCKTVSS
     SEVNMCSEPV WKQRLDFDIN ICDLPRMARL CFALYAVIEK AKKARSTKKK SKKADCPIAW
     VNVMLFDYKD QLKTGECCLH MWSSFPDEKG ELLNPMGTVQ CNPNTESAAA LVICFPNVAS
     HPVYYPSFEQ LLELGRNGEQ PRSAPEDPEE KLQLKEILER RNHTELYEHE KDLVWKMRYD
     IRDQYPQALA KLLTITKWNK HEDVAQMISL LQTWPELPVL NALELLDFSF PDRYVGSFAI
     NSLKKLTDHE LFQYLLQLVQ VLKYESYLDC ELTKFLLDRA LSNRKIGHFL FWHLRSEMHV
     PAVALRFGLI LEAYCRGSTH HMKVLMKQGE ALSKMKALNE FVKLSSPKAT KPQAKEMMHV
     CMKQETYLEA LSHLQSPLNP SIILTEVCVD QCTFMDSKMK PLWIVFNNEE TGGGGVGIIF
     KNGGDLRQDM LTLQMIQLMD VLWKQEGLDL RMTPYGCLST GDKTGLIEVV MHSDTIANIQ
     LNKSNMAATA AFNKDALLNW LKSKNPGDAL EQAIEEFTLS CAGYCVATYV LGIGDRHSDN
     IMIRETGQLF HIDFGHFLGN FKTKFGINRE RVPFILTYDF VHVIQQGKTN NSEKFERFRG
     YCEKAYMILR RHGPLFLHLF ALMKAAGLPE LTCSKDIQYL KDSLALGKTD EEALKHFRLK
     FNEALRESWK TKVNWLAHNV SKDNRQ
//
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