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   27-MAR-2024, entry version 103.
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   GeneID; 446671; -.
DR   KEGG; xla:446671; -.
DR   AGR; Xenbase:XB-GENE-6085232; -.
DR   CTD; 446671; -.
DR   Xenbase; XB-GENE-6085232; pik3c3.L.
DR   OMA; LHKFAQY; -.
DR   OrthoDB; 10350at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 446671; Expressed in testis and 19 other cell types or 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR   CDD; cd08397; C2_PI3K_class_III; 1.
DR   CDD; cd00870; PI3Ka_III; 1.
DR   CDD; cd00896; PI3Kc_III; 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; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR008290; PI3K_Vps34.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
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; ARM repeat; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-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; 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
//