ID A0A2K6M6K6_RHIBE Unreviewed; 1619 AA.
AC A0A2K6M6K6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 alpha {ECO:0000313|Ensembl:ENSRBIP00000031409.1};
GN Name=PIK3C2A {ECO:0000313|Ensembl:ENSRBIP00000031409.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000031409.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000031409.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000031409.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
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-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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 Ensembl; ENSRBIT00000055375.1; ENSRBIP00000031409.1; ENSRBIG00000039528.1.
DR GeneTree; ENSGT00940000157813; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd00869; PI3Ka_II; 1.
DR CDD; cd05176; PI3Kc_C2_alpha; 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 Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
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; IPR037705; PI3K-C2-alpha_dom.
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; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF28; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 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; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 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; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 421..509
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 810..986
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1054..1332
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1488..1611
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1619 AA; 182963 MW; 265470DB9FD06D88 CRC64;
MAQISSNSGF KECPSSHPEP TRANDVDKEE ALQMEAEALA KLQKDRQVTD NQKSFELSSS
TRKKAQVYNK QDYDLMVFPE SDSQKRALDI DVEKLTQAEL EKLLLDDSFE TRKTPVLPAT
PVLSPSFSAQ LYFRPTIQRG QWPPGLSGPS TYTLPSIYPS TYSKQAAFQN GFNPRMPTFP
STEPIYLSLP GQSPYFSYPL TPATPFHPQG SLPIYRPVVS PDMAKLFDKI ASTSEFLKNG
KARTDLEITD SKVSNIQVSP KSEDISKFDW LDLDPLSKPK VDNVEVLDHE EEKNVSSLLA
KDPWDAVLLE ERSPANCHLE RKVNGKSLSV ATVTRSQSLN IRTTQLAKAQ GHIFQKDPNG
TSNLPTGSSL LQEVEVQNEE MAAFCRSITK LKTKFPYTNH RTNPGYLLSP VTAQRNICGE
NASVKVSIEI EGFQLPVTFT CDVSSTVEII IMQALCWVHD DLNQVDVGSY VLKVCGQEEV
LQNNHCLGSH EHIQNCRKWD TEIRLQLLTF SAMCQYLART AEDDETPVDL NKHLYQIEKP
YKEAMTRHPV EELLDSYHNQ VELALQIENQ HRAVDQVIKA VRKICSALDG VETLAITESV
KKLKRAVNLP RSKTADVTSL FGEEDTSKNS TRGSLNPENP VQVSINQLTA AIYDLLRLHA
NSGRSPTDCA QSSKSAKEAW TTTEQLQFTI FAAHGISSNW DLFKPDSSKE GGTYKNFFYL
IKCMNYITIS SGSSPDSNKQ RKGPEALGKV LTCGTKLLYL WTSSHTNSIP GTVTKKGYVM
ERIVLQVDFP SPAFDVIYTT PQVDRNIIQQ HNLETLENDI KGKLLDILHK DSSLGLSKED
KAFLWEKRYY CFKHPNCLPK ILASAPNWKW VNLAKTYSLL HQWPPLYPLI ALELLDSKFA
DQEVRSLAVT WIEAISDDEL TDLLPQFVQA LKYEIYLNSP LVQFLLSRAL GNIQIAHSLY
WLLKDALHDV QFSTRYEHVL GALLSVGGKR LREELLKQTK LVQLLGGVAE KVRQASGSAR
QVVLQRSMER VQSFFQKNKC RLPLKPSLVA KELNIKSCSF FSSNAVPLKV TMVNADPMGE
EINVMFKVGE DLRQDMLALQ MIKIMDKIWL KEGLDLRMVI FKCLSTGRDR GMVELVPASD
TLRKIQVEYG VTGSFKDKPL AEWLRKYNPS EEEYEKASEN FIYSCAGCCV ATYVLGICDR
HNDNIMLRST GHMFHIDFGK FLGHAQMFGS FKRDRAPFVL TSDMAYVING GEKPTIRFQL
FVDLCCQAYN LIRKQTNLFL NLLSLMIPSG LPELTSIQDL KYVRDALQPQ TTDAEATIFF
TRLIESSLGS IATKFNFFIH NLAQLRFSGL PSNDEPILSF SPKTYSFRQD GRIKEVSVFT
YHKKYNPDKH YVSLISIFIN NHRNHKKLLI LFYFEMDFPN KMVLGRTHIK DVAAKRKIEL
NSYLQSLMNA STDVAECDLV CTFFHPLLRD EKAEGIARSA DAGSFSPTAG QIGGAVKLSI
SYRNGTLFIM VMHIKDLVTE DGADPNPYVK TYLLPDNHKT SKRKTKISRK TRNPTFNEML
VYSGYSKETL RQRELQLSVL SAESLRENFF LGGVTLPLKD FNLSKETVKW YQLTAATYL
//
