Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O88763 (PK3C3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 3-kinase catalytic subunit type 3

Short name=PI3-kinase type 3
Short name=PI3K type 3
Short name=PtdIns-3-kinase type 3
EC=2.7.1.137
Alternative name(s):
Phosphoinositide-3-kinase class 3
Gene names
Name:Pik3c3
Synonyms:Vps34
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate which plays a key role in initiation and maturation of autophagosomes. Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for the abcission step in cytokinesis. Required for transport from early to late endosomes By similarity. Ref.1

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate.

Cofactor

Manganese By similarity.

Subunit structure

Heterodimer. This subunit, part of a complex composed of regulatory and catalytic subunits, associates with regulatory subunit PIK3R4. Interacts with AMBRA1 By similarity. Forms a complex with BECN1, PIK3R4 and either UVRAG and KIAA0226/Rubicon, or with ATG14. In this complex, presence of UVRAG and ATG14 are mutually exclusive By similarity. Part of a complex composed of PIK3R4 and PIK3CB By similarity. Interacts with RAB7A in the presence of PIK3R4. Interacts with BECN1P1/BECN2 By similarity.

Subcellular location

Midbody By similarity. Late endosome By similarity. Note: Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme By similarity.

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 C2 PI3K-type domain.

Contains 1 PI3K/PI4K domain.

Contains 1 PIK helical domain.

Ontologies

Keywords
   Biological processAutophagy
Cell cycle
Cell division
   Cellular componentEndosome
   LigandATP-binding
Manganese
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processautophagic vacuole assembly

Inferred from mutant phenotype PubMed 12453151. Source: RGD

cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome to late endosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

endosome organization

Inferred from mutant phenotype PubMed 12453151. Source: RGD

phosphatidylinositol-mediated signaling

Inferred from direct assay PubMed 12244116. Source: RGD

protein processing

Inferred from mutant phenotype Ref.1. Source: RGD

regulation of protein secretion

Inferred from mutant phenotype Ref.1. Source: RGD

response to leucine

Inferred from expression pattern PubMed 19015198. Source: RGD

   Cellular_componentaxoneme

Inferred from sequence or structural similarity. Source: UniProtKB

late endosome

Inferred from sequence or structural similarity. Source: UniProtKB

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol 3-kinase complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_function1-phosphatidylinositol-3-kinase activity

Inferred from direct assay PubMed 12244116. Source: RGD

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol 3-kinase activity

Inferred from mutant phenotype Ref.1. Source: RGD

protein binding

Inferred from physical interaction Ref.1. Source: RGD

protein kinase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 887887Phosphatidylinositol 3-kinase catalytic subunit type 3
PRO_0000088805

Regions

Domain35 – 184150C2 PI3K-type
Domain283 – 520238PIK helical
Domain631 – 885255PI3K/PI4K

Amino acid modifications

Modified residue2611Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
O88763 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 73822786C889035A

FASTA887101,534
        10         20         30         40         50         60 
MGEAEKFHYI YSCDLDINVQ LKIGSLEGKR EQKSYKAVLE DPMLKFSGLY QETCSDLYVT 

        70         80         90        100        110        120 
CQVFAEGKPL ALPVRTSYKP FSTRWNWNEW LKLPVKYPDL PRNAQVALTI WDVYGPGRAV 

       130        140        150        160        170        180 
PVGGTTVSLF GKYGMFRQGM HDLKVWPNVE ADGSEPTRTP GRTSSTLSED QMSRLAKLTK 

       190        200        210        220        230        240 
AHRQGHMVKV DWLDRLTFRE IEMINESEKR SSNFMYLMVE FRCVKCDDKE YGIVYYEKDG 

       250        260        270        280        290        300 
DESSPILTSF ELVKVPDPQM SMENLVESKH HKLARSLRSG PSDHDLKPNA TTRDQLNIIV 

       310        320        330        340        350        360 
SYPPTKQLTY EEQDLVWKFR YYLTNQEKAL TKFLKCVNWD LPQEAKQALE LLGKWKPMDV 

       370        380        390        400        410        420 
EDSLELLSSH YTNPTVRRYA VARLRQADDE DLLMYLLQLV QALKYENFDD IKNGLEPTKK 

       430        440        450        460        470        480 
DSQASVSESL SSSGVSSADI DSSQIITNPL PPVASPPPAS KSKEVSDGEN LEQDLCTFLI 

       490        500        510        520        530        540 
SRACKNSTLA NYLYWYVIVE CEDQDTQQRD PKTHEMYLNV MRRFSQALLK GDKSVRVMRS 

       550        560        570        580        590        600 
LLAAQQTFVD RLVHLMKAVQ RESGNRKKKN ERLQALLGDN EKMNLSDVEL IPLPLEPQVK 

       610        620        630        640        650        660 
IRGIIPETAT LFKSALMPAQ LFFKTEDGGK YPVIFKHGDD LRQDQLILQI ISLMDKLLRK 

       670        680        690        700        710        720 
ENLDLKLTPY KVLATSTKHG FMQFIQSVPV AEVLDTEGSI QNFFRKYAPS ETGPNGISAE 

       730        740        750        760        770        780 
VMDTYVKSCA GYCVITYILG VGDRHLDNLL LTKTGKLFHI DFGYILGRDP KPLPPPMKLN 

       790        800        810        820        830        840 
KEMVEGMGGT QSEQYQEFRK QCYTAFLHLR RYSNLILNLF SLMVDANIPD IALEPDKTVK 

       850        860        870        880 
KVQDKFRLDL SDEEAVHYMQ SLIDESVHAL FAAVVEQIHK FAQYWRK 

« Hide

References

« Hide 'large scale' references
[1]"Overexpression of a rat kinase-deficient phosphoinositide 3-kinase, Vps34p, inhibits cathepsin D maturation."
Row P.E., Reaves B.J., Domin J., Luzio J.P., Davidson H.W.
Biochem. J. 353:655-661(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ006710 mRNA. Translation: CAA07199.1.
BC061981 mRNA. Translation: AAH61981.1.
RefSeqNP_075247.1. NM_022958.2.
UniGeneRn.30010.

3D structure databases

ProteinModelPortalO88763.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000060791.

PTM databases

PhosphoSiteO88763.

Proteomic databases

PaxDbO88763.
PRIDEO88763.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000066816; ENSRNOP00000060791; ENSRNOG00000017840.
GeneID65052.
KEGGrno:65052.
UCSCRGD:620899. rat.

Organism-specific databases

CTD5289.
RGD620899. Pik3c3.

Phylogenomic databases

eggNOGCOG5032.
GeneTreeENSGT00620000087805.
HOGENOMHOG000174003.
HOVERGENHBG082145.
InParanoidO88763.
KOK00914.
OMAYLMVEFP.
OrthoDBEOG7PP55Z.
PhylomeDBO88763.

Gene expression databases

GenevestigatorO88763.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.70. 2 hits.
2.60.40.150. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR002420. PI3K_C2_dom.
IPR008290. PI3K_Vps34.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]
PANTHERPTHR10048. PTHR10048. 1 hit.
PfamPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
PIRSFPIRSF000587. PI3K_Vps34. 1 hit.
SMARTSM00239. C2. 1 hit.
SM00142. PI3K_C2. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio613903.
PROO88763.

Entry information

Entry namePK3C3_RAT
AccessionPrimary (citable) accession number: O88763
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: November 1, 1998
Last modified: June 11, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families