CLA4_YEAST
ID CLA4_YEAST Reviewed; 842 AA.
AC P48562; D6W0P6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Serine/threonine-protein kinase CLA4;
DE EC=2.7.11.1;
GN Name=CLA4; OrderedLocusNames=YNL298W; ORFNames=N0450;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K1107;
RX PubMed=7649470; DOI=10.1101/gad.9.15.1817;
RA Cvrckova F., de Virgilio C., Manser E., Pringle J.R., Nasmyth K.;
RT "Ste20-like protein kinases are required for normal localization of cell
RT growth and for cytokinesis in budding yeast.";
RL Genes Dev. 9:1817-1830(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553702; DOI=10.1002/yea.320111311;
RA Maurer K.C.T., Urbanus J.H.M., Planta R.J.;
RT "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV
RT carrying a ribosomal protein gene cluster, the genes encoding a plasma
RT membrane protein and a subunit of replication factor C, and a novel
RT putative serine/threonine protein kinase gene.";
RL Yeast 11:1303-1310(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-425, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-351 AND SER-367, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in budding and cytokinesis.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBUNIT: Interacts with CDC42.
CC -!- INTERACTION:
CC P48562; P29366: BEM1; NbExp=9; IntAct=EBI-4750, EBI-3508;
CC P48562; P11433: CDC24; NbExp=5; IntAct=EBI-4750, EBI-4220;
CC P48562; Q04439: MYO5; NbExp=3; IntAct=EBI-4750, EBI-11687;
CC P48562; Q12163: NBP2; NbExp=3; IntAct=EBI-4750, EBI-34713;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; X82499; CAA57879.1; -; Genomic_DNA.
DR EMBL; U23084; AAC49100.1; -; Genomic_DNA.
DR EMBL; Z71574; CAA96216.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10262.1; -; Genomic_DNA.
DR PIR; S60402; S60402.
DR RefSeq; NP_014101.1; NM_001183136.1.
DR AlphaFoldDB; P48562; -.
DR SMR; P48562; -.
DR BioGRID; 35540; 741.
DR ComplexPortal; CPX-3462; CLA4-BEM1-CDC24 polarity complex.
DR DIP; DIP-2276N; -.
DR IntAct; P48562; 42.
DR MINT; P48562; -.
DR STRING; 4932.YNL298W; -.
DR iPTMnet; P48562; -.
DR MaxQB; P48562; -.
DR PaxDb; P48562; -.
DR PRIDE; P48562; -.
DR EnsemblFungi; YNL298W_mRNA; YNL298W; YNL298W.
DR GeneID; 855418; -.
DR KEGG; sce:YNL298W; -.
DR SGD; S000005242; CLA4.
DR VEuPathDB; FungiDB:YNL298W; -.
DR eggNOG; KOG0578; Eukaryota.
DR GeneTree; ENSGT00940000176572; -.
DR HOGENOM; CLU_000288_26_2_1; -.
DR InParanoid; P48562; -.
DR OMA; RYNPSRP; -.
DR BioCyc; YEAST:G3O-33286-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-SCE-5627123; RHO GTPases activate PAKs.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
DR PRO; PR:P48562; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P48562; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IMP:SGD.
DR GO; GO:0120157; C:PAR polarity complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IDA:SGD.
DR GO; GO:0016301; F:kinase activity; IDA:SGD.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0000282; P:cellular bud site selection; IC:ComplexPortal.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IC:ComplexPortal.
DR GO; GO:0019236; P:response to pheromone; IGI:SGD.
DR GO; GO:0031106; P:septin ring organization; IMP:SGD.
DR GO; GO:0035376; P:sterol import; IMP:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 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.
FT CHAIN 1..842
FT /note="Serine/threonine-protein kinase CLA4"
FT /id="PRO_0000085865"
FT DOMAIN 61..179
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 184..197
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 546..825
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 12..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 693
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 552..560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 390
FT /note="Y -> I (in Ref. 1; CAA57879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 842 AA; 93909 MW; 3A2AB86414561DC6 CRC64;
MSLSAAANKI SDNDFQNIGP APRPPSSNSQ GRTCYNQTQP ITKLMSQLDL TSASHLGTST
SKKKSGWVSY KDDGILSFIW QKRYLMLHDS YVALYKNDKQ NDDAILKIPL TSIISVSRTQ
LKQYCFELVR CSDRNSVSSG SSSSLNVSSD SNSKKSIYIA TKTESDLHSW LDAIFAKCPL
LSGVSSPTNF THKVHVGFDP ETGSFVGMPT NWEKLLKHSR ITGEDWNNNS AAVIQVLQFY
QEYNGAGNPT NTLDKPQSGE TSSSQKSLPN SYNDNKLRNN SVNSKSSSGV SSSMVSQRKT
SQPPNTKSPV SLGSGSLPPI NTKLPTSQSN IPRHLQNVPN QQYPKMRNGH SPTNGQFPRG
PMHPNNSQRS LQQQQQQQQQ QKQQHQQYPY HHQGPSPSPS PSPSPLNPYR PHHNMINPYS
KQPQSPLSSQ STQNQAIPRY AQNSSPTAAH FQPQRTAPKP PISAPRAPYP SNQNATSNTH
VQPVAPKNDQ STPQTMRQAP KRPDADVAQP GGVAKPKKPA RPTMSTAEIM SKLKKVTVNA
DPSQCFKVIE KAGQGASGSV YLAERTHIPT ESNMIELINN DIDEPHVGDK VAIKQMVLSK
QPRKELIVNE ILVMKDSRHK NIVNFLEAYL RTDDDLWVVM EFMEGGSLTD IIENSPTNDN
SHSPLTEPQI AYIVRETCQG LKFLHDKHII HRDIKSDNVL LDTRARVKIT DFGFCARLTD
KRSKRATMVG TPYWMAPEVV KQREYDEKID VWSLGIMTIE MLEGEPPYLN EDPLKALYLI
ATNGTPKLKH PESLSLEIKR FLSVCLCVDV RYRASTEELL HHGFFNMACD PKDLTSLLEW
KE
