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   27-MAR-2024, entry version 174.
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; 10.
DR   STRING; 284812.P50520; -.
DR   MaxQB; P50520; -.
DR   PaxDb; 4896-SPAC458-05-1; -.
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; LHKFAQY; -.
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: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:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0016236; P:macroautophagy; IMP:PomBase.
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   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   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
//