ID A0A2I0LW23_COLLI Unreviewed; 1066 AA.
AC A0A2I0LW23;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010};
DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010};
GN Name=PIK3CB {ECO:0000313|EMBL:PKK21607.1};
GN ORFNames=A306_00012570 {ECO:0000313|EMBL:PKK21607.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK21607.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK21607.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK21607.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK21607.1}.
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; AKCR02000077; PKK21607.1; -; Genomic_DNA.
DR RefSeq; XP_005505110.1; XM_005505053.2.
DR AlphaFoldDB; A0A2I0LW23; -.
DR STRING; 8932.A0A2I0LW23; -.
DR GeneID; 102083735; -.
DR KEGG; clv:102083735; -.
DR CTD; 5291; -.
DR InParanoid; A0A2I0LW23; -.
DR OrthoDB; 10350at2759; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
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; cd00872; PI3Ka_I; 1.
DR CDD; cd05173; PI3Kc_IA_beta; 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; IPR037702; PI3Kbeta_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF33; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT BETA 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; PS00915; PI3_4_KINASE_1; 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 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PKK21607.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..109
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 188..280
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 322..491
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 520..697
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 768..1049
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1066 AA; 122062 MW; 1B17FA5A0313B479 CRC64;
MPPAVTDSLD IWAVDSQIGA DGSISVDFLL PTGIYINLDV PRDATISHIK QLLWKQAHSY
PLFHLLMEID SYMFSCVNQT AVHEELEDET RRLCDVRPFL PVLKLVTRNC DPGEKLDSKI
GVLIGKGLHE FDALQDPEVN DFRAKMRKIS EEKIQSLVGL SWMDWLKHTY PPEQEPVIPE
SFQDKLYNGN IVVAVHFDNC QDVFSFQVSP NMNPIKLNEL AIRKRLTIHG KDDEEVDPAD
YVLQVSGRLE YVFGDHPLIQ FQYIRNCVMN RTLPQLTLVE CCTIKKMCEQ EMIAVEAAIH
RKSSNLPLPL PPKKTRATTS VWDISNPFKI ILLKGNKLNT EENAKVHVRA GLFHGTELLC
KTIVSTEISG RSDHVWNEVL EFEINVCDLP RMARLCFAVY AVMDKMKTKK STKAMNPSKY
QTIRKAGKVH YPVAWVNTMV FDYKGQLKNG ELVLHSWSSF PDELEEMLNP MGTVQTNPYT
ENATALHIRF QEYSKQPINY PPFDKILEKA AEIARNSDNA AMTGRGGKKF YIVLKEIMER
DPLSQLCENE MDLIWTLRYD CRENFPQSLP KLLLSLKWNK LEDVAQLQAL LQIWPKLLPR
EALELLDFNY PDQYVREYAV GCLKQMSDEE LSQYLLQLVQ VLKYEPFLDC ALSRFLLERA
LANRRIGQML FWHLRSEVHI PAVSVQFGLI LEAYCRGSVA HMKVLAKQVE ALNKMKTLNS
LIKLNAMKQS KAKGKDAMHT CLKQNAYREA LSDLQSPLNP SVILSELHVE KCRYMDSKMK
PLWIVYNNKM FGGDLVGIIF KNGDDLRQDM LTLQILRLMD ILWKEAGLDL RILPYGCLAT
GDHSGLIEAV SSSETIADIQ LNSSNVAAAA AFNKDALLNW LKEYNLGDDL DRAIEEFTLS
CAGYCVATYV LGIGDRHSDN IMVRKNGQLF HIDFGHILGN FKSKFGIKRE RVPFILTYDF
IHVIQQGKTG NIEKFGRFRQ YCEEAYLILR KHGNLFITLF ALMLTAGLPE LTSVKDIQYL
KDSLALGKSE EEALKQFKQK FDEALRESWT TKVNWMAHTV RKDYRS
//
