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Database: UniProt
Entry: G1SMR9_RABIT
LinkDB: G1SMR9_RABIT
Original site: G1SMR9_RABIT 
ID   G1SMR9_RABIT            Unreviewed;      1070 AA.
AC   G1SMR9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 88.
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|Ensembl:ENSOCUP00000004241.2};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000004241.2, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000004241.2, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000004241.2,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000004241.2}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000004241.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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; AAGW02015310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02015311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02015312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_002716594.1; XM_002716548.3.
DR   AlphaFoldDB; G1SMR9; -.
DR   SMR; G1SMR9; -.
DR   STRING; 9986.ENSOCUP00000004241; -.
DR   PaxDb; 9986-ENSOCUP00000004241; -.
DR   Ensembl; ENSOCUT00000004901.4; ENSOCUP00000004241.2; ENSOCUG00000004899.4.
DR   eggNOG; KOG0904; Eukaryota.
DR   GeneTree; ENSGT00940000157522; -.
DR   HOGENOM; CLU_002191_1_3_1; -.
DR   InParanoid; G1SMR9; -.
DR   OMA; CVEWNDH; -.
DR   OrthoDB; 10350at2759; -.
DR   TreeFam; TF102031; -.
DR   UniPathway; UPA00220; -.
DR   Proteomes; UP000001811; Chromosome 14.
DR   Bgee; ENSOCUG00000004899; Expressed in blood and 15 other cell types or tissues.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; IEA:Ensembl.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:Ensembl.
DR   GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; IEA:Ensembl.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl.
DR   GO; GO:0001952; P:regulation of cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; IEA:Ensembl.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          26..115
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          194..285
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          327..496
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          524..701
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          772..1053
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1070 AA;  122718 MW;  948CAE0671346FFC CRC64;
     MCFSFIMPPA MADILDIWAV DSQIASDGSI PVDFLLPTGI YIQLEVPREA TISYIKQLLW
     KQVHNYPMFN LLMEIDAYMF ACVNQTAVYE ELEDETRRLC DVRPFLPVLK LVTRSCDPGE
     KLDSKIGVLI GKGLHEFDAL KDPEVNEFRR KMRKFSEEKI QSLVGLSWID WLKQTYPPEH
     DPSSLENLED KLYGGKLIVA VHFENSQDVF SFQVSPNMNP IKINELAIQK RLTIHGKEDE
     ASPYDYVLQV SGRVEYVFGD HPLIQFQYIR NCVMNRTLPH FILVECCKIK KMYEQEMIAI
     EAAINRNSSN LPLPLPPKKT RITSHVWENN NPFQIVLVKG NKLNTEETVK VHVRAGLFHG
     TELLCKTIVS SEISGKNDHI WNEPLEFDIN TCDLPRMARL CFAVYAVLDK VKTKKSTKTI
     NPSKYQTIRK AGKVHYPVAW VNTMVFDFKG QLRSGDVILH SWSSFPDELE EMLNPMGTVQ
     TNPYTENATA LHIKFPENKK QPYYYPPFDK IIEKAAEIAS NDSANVSSRG GKKFLAVLKE
     ILDRDPLSQL CENEMDLIWT LRQDCRENFP QSLPKLLLSI KWNKLEDVAQ LQALLQIWPK
     LPPREALELL DFNYPDQYVR EYAVGCLRQM SDEELSQYLL QLVQVLKYEP FLDCALSRFL
     LERALANRRI GQFLFWHLRS EVHIPAVSVQ FGVILEAYCR GSVGHMKVLS KQVEALNKLK
     TLNSLIKLNA VKLNRAKGKE AMHTCLKQNA YREALSDLQS PLNPCVILSE LYVEKCKYMD
     SKMKPLWLVY NNKVFGEDSV GVIFKNGDDL RQDMLTLQML RLMDLLWKEA GLDLRMLPYG
     CLATGDRSGL IEVVSTSETI ADIQLNSSNV AAAAAFNKDA LLNWLKEYNS GDDLDRAIEE
     FTLSCAGYCV ASYVLGIGDR HSDNIMVKKT GQLFHIDFGH ILGNFKSKFG IKRERVPFIL
     TYDFIHVIQQ GKTGNTEKFG RFRQCCEDAY LILRRHGNLF ITLFALMLTA GLPELTSVKD
     IQYLKDSLAL GKSEEEALKQ FKQKFDEALR ESWTTKVNWM AHTVRKDYRS
//
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