VPS34_SCHPO
ID VPS34_SCHPO Reviewed; 801 AA.
AC P50520; Q9P3W3; Q9URD2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Phosphatidylinositol 3-kinase vps34;
DE Short=PI3-kinase vps34;
DE Short=PI3K vps34;
DE Short=PtdIns-3-kinase vps34;
DE EC=2.7.1.137 {ECO:0000269|PubMed:7772832, ECO:0000269|PubMed:8719881};
DE AltName: Full=Vacuolar protein sorting-associated protein 34;
GN Name=vps34; ORFNames=SPAC458.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8719881; DOI=10.1242/jcs.108.12.3745;
RA Takegawa K., Dewald D.B., Emr S.E.;
RT "Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-specific PI 3-
RT kinase essential for normal cell growth and vacuole morphology.";
RL J. Cell Sci. 108:3745-3756(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 138-801, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7772832; DOI=10.1271/bbb.59.678;
RA Kimura K., Miyake S., Makuuchi M., Morita R., Usui T., Yoshida M.,
RA Horinouchi S., Fukui Y.;
RT "Phosphatidylinositol-3 kinase in fission yeast: a possible role in stress
RT responses.";
RL Biosci. Biotechnol. Biochem. 59:678-682(1995).
CC -!- FUNCTION: Phosphatidylinositol 3-kinase homolog required for vacuolar
CC sorting and segregation. {ECO:0000269|PubMed:7772832,
CC ECO:0000269|PubMed:8719881}.
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:0000269|PubMed:7772832,
CC ECO:0000269|PubMed:8719881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000269|PubMed:7772832};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00880}.
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DR EMBL; U32583; AAC49133.1; -; mRNA.
DR EMBL; CU329670; CAB93847.1; -; Genomic_DNA.
DR PIR; PC4002; PC4002.
DR PIR; T52538; T52538.
DR RefSeq; NP_594699.1; NM_001020127.2.
DR AlphaFoldDB; P50520; -.
DR SMR; P50520; -.
DR BioGRID; 279864; 9.
DR STRING; 4896.SPAC458.05.1; -.
DR MaxQB; P50520; -.
DR PaxDb; P50520; -.
DR PRIDE; P50520; -.
DR EnsemblFungi; SPAC458.05.1; SPAC458.05.1:pep; SPAC458.05.
DR GeneID; 2543444; -.
DR KEGG; spo:SPAC458.05; -.
DR PomBase; SPAC458.05; -.
DR VEuPathDB; FungiDB:SPAC458.05; -.
DR eggNOG; KOG0906; Eukaryota.
DR HOGENOM; CLU_004869_0_0_1; -.
DR InParanoid; P50520; -.
DR OMA; GRQKCKI; -.
DR PhylomeDB; P50520; -.
DR BRENDA; 2.7.1.137; 5613.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR Reactome; R-SPO-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-SPO-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-SPO-1660517; Synthesis of PIPs at the late endosome membrane.
DR Reactome; R-SPO-5668599; RHO GTPases Activate NADPH Oxidases.
DR PRO; PR:P50520; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IMP:PomBase.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IDA:PomBase.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IDA:PomBase.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0031321; P:ascospore-type prospore assembly; IMP:PomBase.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:PomBase.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IDA:PomBase.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..801
FT /note="Phosphatidylinositol 3-kinase vps34"
FT /id="PRO_0000088817"
FT DOMAIN 14..166
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 257..439
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 515..785
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 521..527
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 654..662
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 673..694
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT CONFLICT 164
FT /note="K -> Q (in Ref. 1; AAC49133)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="L -> I (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="S -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 801 AA; 92135 MW; 520571E1475CC341 CRC64;
MDRLVFSYCP SSKVTARFLV KFCFIEYQDS QEPCICTIQL FSGNESGSLM QKCFVSKIPN
KSLLPTELSK ISTHEWLDFG VTVSELSLNA KFVVSAWKPS FNDEEVYEFV GCTTYRLFDE
NNLLRQGLQK IPLQTSKEIK KYSPTSLELE QVKEINRLDG LLLKLQLGDV PSVNWLDDIS
FGKIKDFRSK HMSLVTIPIL YLDFLQFSFP VVFQRSYYPK SENRVYYSSF DLELNLDSPA
ELKHRRLVRS QRNGPLDKDL KPNSKIRKEL ESILSYPPSE ELSLEEKDLI WKFRFYLTRN
KKAMTKFLKS VVWTDSSEVN QALSLLDSWT EIDIDDALEL LSPSFVHPKV RAYAVSRLET
ASNEELLLYL LQLVQALRYD NPISSDERFQ PSPLALFLVN RAISSPSIGN DLYWYLVVEI
EDEPVSKLFS SVMFLFQKEL SKSVEGRLIR ETLSAQAKFV EKLLRISKSV QSFRGTRLKK
IEYLKVLLED HKYHLLDFHA LPLPLDPSVN IVGIIPDACT VFKSTMQPLR LLFKCQDGSK
YPIIFKNGDD LRQDQLVIQI LTLMDKLLKK EKLDLHLKPY RILATGPTHG AVQFVPSKTL
ATILAEYHGS VLAYLRENNP DDGLNSANYG IDPVAMDNYV RSCAGYCVIT YLLGVGDRHL
DNLLITKDGH FFHADFGYIL GRDPKLFSPA MKLSKEMVEG MGGYNSPFYQ QFKSYCYTTF
TALRKSSNLI LNLFSLMVDA NIPDIKFDKE KVVYKVKERF CLQMSESDAI KYFEQLINDS
VSALFPQIID RMHNLAQYMR S
