ID H0YZT0_TAEGU Unreviewed; 1010 AA.
AC H0YZT0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 24-JAN-2024, entry version 85.
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=PIK3CD {ECO:0000313|Ensembl:ENSTGUP00000003815.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000003815.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000003815.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000003815.2}
RP IDENTIFICATION.
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 AlphaFoldDB; H0YZT0; -.
DR STRING; 59729.ENSTGUP00000019923; -.
DR Ensembl; ENSTGUT00000003857.2; ENSTGUP00000003815.2; ENSTGUG00000003652.2.
DR GeneTree; ENSGT00940000159079; -.
DR HOGENOM; CLU_002191_1_3_1; -.
DR TreeFam; TF102031; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000007754; Chromosome 21.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08693; C2_PI3K_class_I_beta_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; 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 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
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 668..993
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1010 AA; 115653 MW; 622EA84BBF549ABE CRC64;
MPPGIYCPTE FWSKGENQNI QVDFLLPTGI YLNLSVPCNA SLGTIKQVLW KHAQYEPLFH
MLSDPEAYVF TCINQTAEQQ ELEDEQRRLC DIQPFLPVLR LVAREGDRAK KVINSQISLL
IGKGLHEFDS VQDPEVSDFR TKMCQFCEEK AAKRQQLSWA AWMEYNFPLQ LEPVAKGLGV
GSLQIPTKNI FVNIKFQSGG ESFTFQISPW EFPITLMSYA IKKQATVFRH ETVQKPEDYT
LQVNGKCEYL YGNYPLYQFQ HIRSCLQRGR TPHLTMVHSS AIIAMRDEQT NGITSPPKAA
PKPPPLPKKK PNYGSLWSLE QPFYIELVQG SKVNADERMK LVVQAGLFHG TEMLCKTVSS
SEVSVCSEPV WRQRLDFDIS VCDLPRMARL CLALYAVVEK AKKARSTKKK SKKADCPIAW
VNVMLFDYKD QLKTGECCLH MWSSFPDEKG ELLNPMGTVQ CNPNTESAAA LVICFPSVAA
HPVYYPSFEQ LLELGRNGEQ PRAAPEDSEE KLQLREILER RSHTELYEHE KDLVWKMRYD
IRDQYPQALA KLLVITKWNK HEDVAQMISL LQTWPELPVL NALELLDFSF PDRYVGSFAV
NSLKKLTDDD VFQYLLQLVQ VLKYESYLDC ELTKFLLERA LSNRKIGHFL FWHLRSEMHV
PAVALRFGLI LEAYCRGSTH HMKVLMKQGE ALNKMKALND FVKVSSQKAT KPQTKEMMHM
CMKQETYREA LSHLQNPLNP NIILAEVCVD QCTFMDSKMK PLWIVFNNEE TGGGGVGIIF
KNGDGDKTGL IEVVMHSDTI ANIQLNKSNM VATAAFNKDA LLNWLKSKNP GDALDQAIEE
FTLSCAGYCV ATYVLGIGDR HSDNIMVRET GQLFHIDFGH FLGNFKTKFG INRERVPFIL
TYDFVHVIQQ GKTNNNEKFE RFRGYCERAY MILRRHGLLF LHLFALMKAA GLPELSCSKD
IQYLKDSLAL GKTDEEALKH FRVKFNEALR ESWKTKVNWL AHNVSKDNRQ
//