VPS34_ENCCU
ID VPS34_ENCCU Reviewed; 446 AA.
AC Q8SR56;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable phosphatidylinositol 3-kinase VPS34 homolog;
DE Short=PI3-kinase VPS34;
DE Short=PI3K VPS34;
DE Short=PtdIns-3-kinase VPS34;
DE EC=2.7.1.137;
GN Name=VPS34; OrderedLocusNames=ECU10_0590;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GB-M1;
RX PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT "Identification of transcriptional signals in Encephalitozoon cuniculi
RT widespread among Microsporidia phylum: support for accurate structural
RT genome annotation.";
RL BMC Genomics 10:607-607(2009).
CC -!- FUNCTION: Phosphatidylinositol 3-kinase required for cytoplasm to
CC vacuole transport (Cvt) and autophagy as a part of the autophagy-
CC specific VPS34 PI3-kinase complex I. Also involved in endosome-to-Golgi
CC retrograde transport as part of the VPS34 PI3-kinase complex II (By
CC similarity). {ECO:0000250}.
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;
CC -!- SUBUNIT: Component of the autophagy-specific VPS34 PI3-kinase complex I
CC composed; and of the VPS34 PI3-kinase complex II. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; AL590449; CAD25778.2; -; Genomic_DNA.
DR RefSeq; NP_586174.1; NM_001042007.1.
DR AlphaFoldDB; Q8SR56; -.
DR SMR; Q8SR56; -.
DR STRING; 284813.Q8SR56; -.
DR GeneID; 859823; -.
DR KEGG; ecu:ECU10_0590; -.
DR VEuPathDB; MicrosporidiaDB:ECU10_0590; -.
DR HOGENOM; CLU_618240_0_0_1; -.
DR InParanoid; Q8SR56; -.
DR OrthoDB; 1327842at2759; -.
DR Proteomes; UP000000819; Chromosome X.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1070.11; -; 1.
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; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Endosome; Golgi apparatus; Kinase; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Transferase;
KW Transport.
FT CHAIN 1..446
FT /note="Probable phosphatidylinositol 3-kinase VPS34
FT homolog"
FT /id="PRO_0000388438"
FT DOMAIN 177..430
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 183..189
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 302..310
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 321..342
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 446 AA; 52007 MW; 1750449946A5C2F8 CRC64;
MEEWDGDVFT WNAGKEDIYT LIESILRLLK NGCKGMENMV VKYLGTGATD SLYMYFPWLR
GRDLESRLSV EHQIDRFWKI RFELHEERTN SMDRYEDIVS SFLALDTKCG ILGKLEGQMA
LVDEIRRIYS ITSQGSPRKK RLREYRLHGT LCLHPGAGSM RLYASLFSLD ATVKEIIFPE
IEIFPSSTFP ILVPLRTDRG VSRIIYKKGD DLTRDLFVLE TIRYMSRLMG VDLVTYKVIP
LSRKEGIVEV VDGIDFTRIR SRKDLEMYIE EDRDPRHQES FEKRKVFVST LCGYSVACYV
MGIGDRNPGN MMVTRDGKFF HIDFSHVFGR DPKPISSRIT IARPIRDYLV NDELIYQDFL
ARSGEAFLQI RRSCRKIFVL WCILAQNRIF QFDLNEIIPF AQARLRMEMS EQRALELFEK
EIRGAVGSLK TSVAHLINRV GMFLRR
