COT1_NEUCR
ID COT1_NEUCR Reviewed; 598 AA.
AC P38679; P79080; Q7S972;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Serine/threonine-protein kinase cot-1;
DE EC=2.7.11.1;
DE AltName: Full=Colonial temperature-sensitive protein 1;
GN Name=cot-1; ORFNames=NCU07296;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1534751; DOI=10.1002/j.1460-2075.1992.tb05275.x;
RA Yarden O., Plamann M., Ebbole D.J., Yanofsky C.;
RT "cot-1, a gene required for hyphal elongation in Neurospora crassa, encodes
RT a protein kinase.";
RL EMBO J. 11:2159-2166(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION, AND ALTERNATIVE INITIATION.
RC STRAIN=74-OR23-1VA / FGSC 2489;
RX PubMed=9680960; DOI=10.1006/fgbi.1998.1038;
RA Lauter F.-R., Marchfelder U., Russo V.E.A., Yamashiro C.T., Yatzkan E.,
RA Yarden O.;
RT "Photoregulation of cot-1, a kinase-encoding gene involved in hyphal growth
RT in Neurospora crassa.";
RL Fungal Genet. Biol. 23:300-310(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Protein kinase required for hyphal elongation.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=P38679-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P38679-2; Sequence=VSP_018837;
CC -!- MISCELLANEOUS: [Isoform Long]: Produced preferentially in dark grown
CC mycelia.
CC -!- MISCELLANEOUS: [Isoform Short]: Produced preferentially in illuminated
CC mycelia. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. COT1 subfamily. {ECO:0000305}.
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DR EMBL; X97657; CAA66253.1; -; mRNA.
DR EMBL; X97657; CAA66254.1; -; mRNA.
DR EMBL; CM002239; EAA32914.2; -; Genomic_DNA.
DR PIR; S22711; S22711.
DR PIR; T47254; T47254.
DR PIR; T47255; T47255.
DR RefSeq; XP_962150.2; XM_957057.2. [P38679-1]
DR AlphaFoldDB; P38679; -.
DR SMR; P38679; -.
DR STRING; 5141.EFNCRP00000007107; -.
DR PRIDE; P38679; -.
DR EnsemblFungi; EAA32914; EAA32914; NCU07296. [P38679-1]
DR GeneID; 3878299; -.
DR KEGG; ncr:NCU07296; -.
DR VEuPathDB; FungiDB:NCU07296; -.
DR HOGENOM; CLU_000288_67_5_1; -.
DR InParanoid; P38679; -.
DR BRENDA; 2.7.11.1; 3627.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005938; C:cell cortex; IEA:EnsemblFungi.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IDA:CACAO.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007118; P:budding cell apical bud growth; IEA:EnsemblFungi.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IEA:EnsemblFungi.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IEA:EnsemblFungi.
DR GO; GO:0050708; P:regulation of protein secretion; IEA:EnsemblFungi.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IEA:EnsemblFungi.
DR InterPro; IPR000961; AGC-kinase_C.
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; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative initiation; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..598
FT /note="Serine/threonine-protein kinase cot-1"
FT /id="PRO_0000024318"
FT DOMAIN 214..518
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 519..598
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 220..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018837"
SQ SEQUENCE 598 AA; 68017 MW; 13B9FB4AF3859893 CRC64;
MDNTNRPHLN LGTNDTRMAP NDRTYPTTPS TFPQPVFPGQ QAGGSQQYNQ AYAQSGNYYQ
QNHNDPNTGL AHQFAHQNIG SAGRASPYGS RGPSPAQRPR TSGNSGQQQT YGNYLSAPMP
SNTQTEFAPA PERNPDKYGP NANNNQKKCS QLASDFFKDS VKRARERNQR QSEMEQKLGE
TNDARRRESI WSTAGRKEGQ YLRFLRTKDK PENYQTIKII GKGAFGEVKL VQKKADGKVY
AMKSLIKTEM FKKDQLAHVR AERDILAESD SPWVVKLYTT FQDANFLYML MEFLPGGDLM
TMLIKYEIFS EDITRFYIAE IVLAIDAVHK LGFIHRDIKP DNILLDRGGH VKLTDFGLST
GFHKLHDNNY YTQLLQGKSN KPRDNRNSVA IDQINLTVSN RAQINDWRRS RRLMAYSTVG
TPDYIAPEIF TGHGYSFDCD WWSLGTIMFE CLVGWPPFCA EDSHDTYRKI VNWRHSLYFP
DDITLGVDAE NLIRSLICNT ENRLGRGGAH EIKSHAFFRG VEFDSLRRIR APFEPRLTSA
IDTTYFPTDE IDQTDNATLL KAQQAARGAA APAQQEESPE LSLPFIGYTF KRFDNNFR
