PK3C3_XENLA
ID PK3C3_XENLA Reviewed; 886 AA.
AC Q6AZN6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3;
DE Short=PI3-kinase type 3;
DE Short=PI3K type 3;
DE Short=PtdIns-3-kinase type 3;
DE EC=2.7.1.137 {ECO:0000250|UniProtKB:Q8NEB9};
DE AltName: Full=Phosphoinositide-3-kinase class 3;
GN Name=pik3c3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the PI3K complex that mediates formation
CC of phosphatidylinositol 3-phosphate; different complex forms are
CC believed to play a role in multiple membrane trafficking pathways.
CC Involved in the transport of lysosomal enzyme precursors to lysosomes.
CC Required for transport from early to late endosomes (By similarity).
CC {ECO:0000250|UniProtKB:O88763, ECO:0000250|UniProtKB:Q8NEB9}.
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:0000250|UniProtKB:Q8NEB9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB9};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB9};
CC -!- SUBUNIT: Component of the PI3K (PI3KC3/PI3K-III/class III
CC phosphatidylinositol 3-kinase) complex the core of which is composed of
CC the catalytic subunit pik3c3, the regulatory subunit pik3r4 and becn1
CC associating with additional regulatory/auxilliary subunits to form
CC alternative complex forms. {ECO:0000250|UniProtKB:Q8NEB9}.
CC -!- SUBCELLULAR LOCATION: Midbody {ECO:0000250|UniProtKB:Q8NEB9}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00880}.
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DR EMBL; BC077528; AAH77528.1; -; mRNA.
DR RefSeq; NP_001086836.1; NM_001093367.1.
DR AlphaFoldDB; Q6AZN6; -.
DR SMR; Q6AZN6; -.
DR IntAct; Q6AZN6; 1.
DR PRIDE; Q6AZN6; -.
DR GeneID; 446671; -.
DR KEGG; xla:446671; -.
DR CTD; 446671; -.
DR Xenbase; XB-GENE-6085232; pik3c3.L.
DR OMA; GRQKCKI; -.
DR OrthoDB; 204282at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 446671; Expressed in testis and 19 other tissues.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR Gene3D; 2.60.40.150; -; 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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR008290; PI3K_Vps34.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 2.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 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; PS51545; PIK_HELICAL; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Autophagy; Cell cycle; Cell division; Kinase;
KW Lipid metabolism; Manganese; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..886
FT /note="Phosphatidylinositol 3-kinase catalytic subunit type
FT 3"
FT /id="PRO_0000088806"
FT DOMAIN 35..184
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 283..519
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 604..870
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 414..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..616
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 739..747
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 758..779
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 424..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 101157 MW; FBAFB8847FBB60A9 CRC64;
MGESDRFCYV YSCDLDISVR LKIGSLEGKR EQKSYKAVLE DPMLKFSGLY QETCSDLYVT
CQVFAEGKPL ALPVRTSYKA FSTRWNWNEW LKLPVKYADL PRSAQVALTI WDVYGPGKAI
PVGGATVSLF GKYGMFRQGM HDLKVWPNIE ADGSELTKTP GRTNSSASED QMSRLAKLTK
AHRQGHMVKV DWLDRLTFRE IEMINESEKR SSNFMYLMVE FPCVKCDEKE YGIVYYEKDG
DESTPISTSS EIVRVPDPQM SMENLVEIKH HKLARSLRSG PSDHDLKPNA ATRDQLNIIV
SYPPTKQLTS EEQDLVWKFR SYLTSQEKAL TKFLKCVNWD LPQEAKQALE LLGKWKPMDV
EDSLELLSSH FTNPTVRRYA VARLQQADDE DLLMYLLQLV QALKYENFED IKSGLEPTKK
DSQGPMLESM TTSGINPETD SSQILSNPLP AVSSPAPPSK TKDGLDAETL EQDLCTFLIS
RACKNSTLAN YLYWYVIVEC EDQDTQLRDP KTHEMYLNVM RRFSQALLKG DKSVRVMRSL
LATQQTFVDR LVHLMKAVQR ESGNRKKKNE RLQALLGDNE KMNLSEFEPI PLPLEPQVKI
RGIIPEKATL FKSALMPAKL YFKTEDGGKY PVIFKNGDDL RQDQLILQII SLMDKLLRKE
NLDLKLTPYK VLATSTKHGF MQFIQSVPVA EVLATEGSIQ NFFRKYSPSE KGPYGISAEV
MDTYVKSCAG YCVITYILGV GDRHLDNLLL TKTGKLFHID FGYILGRDPK PLPPPMKLNK
EMVEGMGGTQ SEQYQAFRKQ CYTAFLHLRR YSNLILNLFS LMVDANIPDI ALEPDKTVKK
VQDKFRLDLS DEEAVHYMQT LIDDSVNALF AAVVEQIHKF AQYWRR
