LKH1_SCHPO
ID LKH1_SCHPO Reviewed; 690 AA.
AC Q10156; Q9C3Y9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Dual specificity protein kinase lkh1;
DE EC=2.7.12.1;
GN Name=lkh1; Synonyms=kic1; ORFNames=SPAC1D4.11c;
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], AND FUNCTION.
RX PubMed=11741326; DOI=10.1006/bbrc.2001.6128;
RA Kim K.-H., Cho Y.-M., Kang W.-H., Kim J.-H., Byun K.-H., Park Y.-D.,
RA Bae K.-S., Park H.-M.;
RT "Negative regulation of filamentous growth and flocculation by Lkh1, a
RT fission yeast LAMMER kinase homolog.";
RL Biochem. Biophys. Res. Commun. 289:1237-1242(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND AUTOPHOSPHORYLATION.
RX PubMed=12565823; DOI=10.1016/s0014-4827(02)00022-8;
RA Tang Z., Mandel L.L., Yean S.-L., Lin C.X., Chen T., Yanagida M.,
RA Lin R.-J.;
RT "The kic1 kinase of schizosaccharomyces pombe is a CLK/STY orthologue that
RT regulates cell-cell separation.";
RL Exp. Cell Res. 283:101-115(2003).
RN [3]
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).
CC -!- FUNCTION: Protein kinase that may act as a negative regulator of
CC filamentous growth and flocculation. Appears to have a role in normal
CC cell wall and septum formation and in cell separation. May have
CC antagonistic function in the regulation of beta-glucan distribution
CC between the sites for cell wall and septum assembly.
CC {ECO:0000269|PubMed:11741326, ECO:0000269|PubMed:12565823}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- INTERACTION:
CC Q10156; O13759: csx1; NbExp=3; IntAct=EBI-7486409, EBI-1562021;
CC -!- PTM: Autophosphorylates on all three types of residues. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. Lammer subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK12335.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF334941; AAK12335.1; ALT_INIT; mRNA.
DR EMBL; CU329670; CAD29835.2; -; Genomic_DNA.
DR PIR; JC7794; JC7794.
DR RefSeq; NP_001018187.2; NM_001018423.3.
DR AlphaFoldDB; Q10156; -.
DR SMR; Q10156; -.
DR BioGRID; 280608; 83.
DR IntAct; Q10156; 2.
DR MINT; Q10156; -.
DR STRING; 4896.SPAC1D4.11c.1; -.
DR iPTMnet; Q10156; -.
DR PaxDb; Q10156; -.
DR PRIDE; Q10156; -.
DR EnsemblFungi; SPAC1D4.11c.1; SPAC1D4.11c.1:pep; SPAC1D4.11c.
DR GeneID; 3361532; -.
DR KEGG; spo:SPAC1D4.11c; -.
DR PomBase; SPAC1D4.11c; lkh1.
DR VEuPathDB; FungiDB:SPAC1D4.11c; -.
DR eggNOG; KOG0671; Eukaryota.
DR HOGENOM; CLU_000288_5_7_1; -.
DR InParanoid; Q10156; -.
DR OMA; KHICIVT; -.
DR PhylomeDB; Q10156; -.
DR BRENDA; 2.7.12.1; 5613.
DR PRO; PR:Q10156; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0061987; P:negative regulation of transcription from RNA polymerase II promoter by glucose; IMP:PomBase.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..690
FT /note="Dual specificity protein kinase lkh1"
FT /id="PRO_0000086236"
FT DOMAIN 362..682
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 39..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 488
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 368..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 690 AA; 77494 MW; AE85C3A27E4DE03E CRC64;
MHSLKRRRNH APDWQDFYKN GVPQEVIVIE DSASPRLTPN LPPPFSVHQL QSFVPPQPPS
SSSPSTTGTV AVPINGANAV YPSTNSVSLP QSYDPWLDAN GVVPLPHDVA SHPSYMVQSP
TSYHACSNNQ SPFPHSHHPP LHNPLPVSCQ PVLRPPPVPQ VPSHWYPVSL PSPNLPHQPI
SKPPVIPNLP KLQVHPNRLP HPIHNHPYSS PTSYPPPLCP ATYCPSNPPQ LAPATAIAPS
SQSSQHKSVN YSVTPSSINN HTAVPLSPTL AVWLPMTQPT FQPPSANVYQ PASNANQVIT
PVSISDYRPP KKRKRAAWPP YKKVDRVNVP VVHDTTAFDP STFDDDDGHY KVVPNSKFAN
RYTVVRLLGH GTFGKVIQCY DQSTGRHCAI KVTRAIPKYR EASLIELRVL QTIAHSDPTN
ENKCIQLRDY FDYRKHICIV TDLFGWSVFD FLKNNNYIPF PLKHIQMLSQ QLFKSVAFLH
SLGLVHTDLK PENVLLVSNA SRTIRLPYRN YSQKVLNSCE IRLIDFGSAT FEDEYHSSVV
STRHYRAPEI ILGLGWSYPC DVWSIGCILV ELFTGQALFQ THEDSEHLCM MEKILGPFDR
NMISRSSRTS QRFFKSDGKV RYPLSNTPKK SINYLQSLQT LEQIFAVSSP EVALLLDLLK
KVFVYDPKRR ITAKEALWHP FFTQPISSNL
