PIK1_SCHPO
ID PIK1_SCHPO Reviewed; 851 AA.
AC Q10366;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Phosphatidylinositol 4-kinase pik1;
DE Short=PI4-kinase;
DE Short=PtdIns-4-kinase;
DE EC=2.7.1.67;
GN Name=pik1; ORFNames=SPAC22E12.16c;
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 [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 [2]
RP INTERACTION WITH CDC4.
RX PubMed=11087749; DOI=10.1074/jbc.m008715200;
RA Desautels M., Den Haese J.P., Slupsky C.M., McIntosh L.P., Hemmingsen S.M.;
RT "Cdc4p, a contractile ring protein essential for cytokinesis in
RT Schizosaccharomyces pombe, interacts with a phosphatidylinositol 4-
RT kinase.";
RL J. Biol. Chem. 276:5932-5942(2001).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-219; SER-222;
RP SER-235 AND TYR-236, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP INTERACTION WITH CAM2.
RX PubMed=21693583; DOI=10.1242/jcs.067850;
RA Sammons M.R., James M.L., Clayton J.E., Sladewski T.E., Sirotkin V.,
RA Lord M.;
RT "A calmodulin-related light chain from fission yeast that functions with
RT myosin-I and PI 4-kinase.";
RL J. Cell Sci. 124:2466-2477(2011).
CC -!- FUNCTION: Acts on phosphatidylinositol (PI) in the first committed step
CC in the production of the second messenger inositol 1,4,5,-
CC trisphosphate. PIK1 is part of a nuclear phosphoinositide cycle and
CC could control cytokinesis through the actin cytoskeleton (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 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67;
CC -!- SUBUNIT: Interacts with cdc4 and cam2. {ECO:0000269|PubMed:11087749,
CC ECO:0000269|PubMed:21693583}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16823372}.
CC Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; CU329670; CAA93903.1; -; Genomic_DNA.
DR PIR; T38173; T38173.
DR RefSeq; NP_594842.1; NM_001020271.2.
DR AlphaFoldDB; Q10366; -.
DR SMR; Q10366; -.
DR BioGRID; 278377; 3.
DR STRING; 4896.SPAC22E12.16c.1; -.
DR iPTMnet; Q10366; -.
DR MaxQB; Q10366; -.
DR PaxDb; Q10366; -.
DR PRIDE; Q10366; -.
DR EnsemblFungi; SPAC22E12.16c.1; SPAC22E12.16c.1:pep; SPAC22E12.16c.
DR GeneID; 2541887; -.
DR KEGG; spo:SPAC22E12.16c; -.
DR PomBase; SPAC22E12.16c; pik1.
DR VEuPathDB; FungiDB:SPAC22E12.16c; -.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_002446_2_0_1; -.
DR InParanoid; Q10366; -.
DR OMA; CGLIETI; -.
DR PhylomeDB; Q10366; -.
DR Reactome; R-SPO-1660514; Synthesis of PIPs at the Golgi membrane.
DR PRO; PR:Q10366; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; ISO:PomBase.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
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 InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021601; Phosphatidylino_kinase_fungi.
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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 2.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF11522; Pik1; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 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 Golgi apparatus; Kinase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..851
FT /note="Phosphatidylinositol 4-kinase pik1"
FT /id="PRO_0000088848"
FT DOMAIN 1..123
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 558..836
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 384..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..570
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 706..714
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 725..749
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 236
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 851 AA; 96658 MW; A991F3C7E3D980BE CRC64;
MPSSNSGNEL LLRFFESAHF TSQLCVAYLS RYPNNIGIHH FLCEKLATFP YEEIEFFIPQ
LIHLVLNKDS ESVALEEFII SQCEQNTQCA LITFWYLQAH MVDLGLQPHS SCFKICKRLY
NRIQILVFMS SSSLIQSQQK ISENVTPALI LSGIMLGGVC VPELLKKAGP IAIAQGRKAP
RQDPDESDVD VLRRLSTEPR YSLDVLRSSL NNSIVEQHSE VSLRLKAPEL TRTHSYQSSA
TLSIDEQRRV LRSNYFQQEI QFLFALQDIS IRLIIVPRQA RLSSLRAELA LLNNNLPADV
NIPLLRSYHK EVSHKIVRID PKEATILNSA ERVPYLIMVE VLSGELSFEP QSKKNKAKVQ
KIVSHKNQRK RWFDLTDVDP YTNLQDSTDN DISESESEGG DLSMSPLIKG LVPDTLSLSK
SFSSFGNVSL QVPSSHRDTD VVLLSGRHSD SDGNGALKRS KIYASEITAR MRAAATMLSQ
LDAEGSRRPK AETERIKNSI ILDMQRLEEE RLNEPSIYPV SVDISCAEDL RFGKETQKAE
RKGDRDDPSA ATFQEDWYAK KERIRKSSPY GHYPNWDLVS VIVKTGADLR QETFACQLIY
AFQRVWLECK EKVWVRRMKI LVTGDNSGLI ETITNAISVH SIKKNLTKQL REAELAQGKI
AGKNVVTLKD YFIKQFGDPN SSRYRQAQTN FLQSLVAYSI ISYLLQLKDR HNGNVLIDSE
GHIIHIDFGF LLTNTPGNVG FESAPFKLTA DYLEILDDRF DEYRSLMKAA FKSVRKNADQ
IILLVEVMQN NSTMPCFRAG ENTSAQLLQR FQLQLGDKEC DDFVDLLIQK ANCSVWTRLY
DLFQNITNGI Y
