ID   ERK1_CANAL              Reviewed;         421 AA.
AC   Q5A1D3; A0A1D8PMK1; O13435; P28869; P87079; P87080; P87081; P87082; P87083;
AC   P87084; P87085; P87086; P87322; Q6LC13;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 3.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Extracellular signal-regulated kinase 1;
DE            Short=ERK1;
DE            EC=2.7.11.24;
DE   AltName: Full=MAP kinase 1;
DE            Short=MAPK 1;
GN   Name=CEK1; Synonyms=ERK1; OrderedLocusNames=CAALFM_C406480CA;
GN   ORFNames=CaO19.10404, CaO19.2886;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RC   STRAIN=ATCC 36232, ATCC 60193 / S-24, R-2436, R-2535, R-2540, R-2607,
RC   R-2617, R-2621, R-2624, R-2777, and R-2805;
RX   PubMed=9544777; DOI=10.1111/j.1574-695x.1998.tb01116.x;
RA   Metzgar D., Field D., Haubrich R., Wills C.;
RT   "Sequence analysis of a compound coding-region microsatellite in Candida
RT   albicans resolves homoplasies and provides a high-resolution tool for
RT   genotyping.";
RL   FEMS Immunol. Med. Microbiol. 20:103-109(1998).
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=2.7.11.24;
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=2.7.11.24;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by tyrosine and threonine
CC       phosphorylation. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q5A1D3; P32917: STE5; Xeno; NbExp=2; IntAct=EBI-8783371, EBI-18373;
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-230 and Tyr-232, which activates the
CC       enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR   EMBL; CP017626; AOW29372.1; -; Genomic_DNA.
DR   EMBL; U95784; AAB88588.1; -; Genomic_DNA.
DR   EMBL; U95785; AAB88589.1; -; Genomic_DNA.
DR   EMBL; U95786; AAB88590.1; -; Genomic_DNA.
DR   EMBL; U95787; AAB88591.1; -; Genomic_DNA.
DR   EMBL; U95788; AAB88592.1; -; Genomic_DNA.
DR   EMBL; U95789; AAB88593.1; -; Genomic_DNA.
DR   EMBL; U95790; AAB88594.1; -; Genomic_DNA.
DR   EMBL; U95791; AAB88595.1; -; Genomic_DNA.
DR   EMBL; U95792; AAB88596.1; -; Genomic_DNA.
DR   EMBL; U95793; AAB88597.1; -; Genomic_DNA.
DR   EMBL; U95794; AAB88598.1; -; Genomic_DNA.
DR   EMBL; U95795; AAB88599.1; -; Genomic_DNA.
DR   EMBL; U95796; AAB88600.1; -; Genomic_DNA.
DR   EMBL; U95797; AAB88601.1; -; Genomic_DNA.
DR   EMBL; U95798; AAB88602.1; -; Genomic_DNA.
DR   RefSeq; XP_715542.2; XM_710449.2.
DR   AlphaFoldDB; Q5A1D3; -.
DR   SMR; Q5A1D3; -.
DR   BioGRID; 1225837; 9.
DR   IntAct; Q5A1D3; 2.
DR   STRING; 237561.Q5A1D3; -.
DR   EnsemblFungi; C4_06480C_A-T; C4_06480C_A-T-p1; C4_06480C_A.
DR   GeneID; 3642789; -.
DR   KEGG; cal:CAALFM_C406480CA; -.
DR   CGD; CAL0000176774; CEK1.
DR   VEuPathDB; FungiDB:C4_06480C_A; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; Q5A1D3; -.
DR   OMA; PYVAAYH; -.
DR   OrthoDB; 158564at2759; -.
DR   PHI-base; PHI:10021; -.
DR   PHI-base; PHI:107; -.
DR   PHI-base; PHI:11018; -.
DR   PHI-base; PHI:6837; -.
DR   PHI-base; PHI:7663; -.
DR   PRO; PR:Q5A1D3; -.
DR   Proteomes; UP000000559; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR   GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:CGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:1990277; P:parasexual reproduction with cellular fusion; IMP:CGD.
DR   GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR   GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR   CDD; cd07849; STKc_ERK1_2_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   PANTHER; PTHR24055:SF590; MITOGEN-ACTIVATED PROTEIN KINASE KSS1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01351; MAPK; 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; Cell cycle; Cell division; Kinase; Mitosis;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..421
FT                   /note="Extracellular signal-regulated kinase 1"
FT                   /id="PRO_0000186325"
FT   DOMAIN          70..375
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOTIF           230..232
FT                   /note="TXY"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         76..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         230
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         232
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         32..35
FT                   /note="Missing (in strain: ATCC 60193 / S-24; in allele 237
FT                   B)"
FT   VARIANT         33
FT                   /note="Q -> QA (in strain: R-2617; in allele 249 D)"
FT   VARIANT         34..35
FT                   /note="QQ -> AQAQA (in strain: R-2805; in allele 255 A)"
FT   VARIANT         34
FT                   /note="Q -> A (in strain: R-2617, R-2624, R-2777 and
FT                   R-2805; in allele 246 D, 249 E, 249 C and 246 E)"
FT   VARIANT         38..43
FT                   /note="Missing (in strain: ATCC 36232; in allele 225 A)"
FT   VARIANT         38..41
FT                   /note="Missing (in strain: R-2621; in allele 237 A)"
FT   VARIANT         41
FT                   /note="Q -> QQ (in strain: R-2621; in allele 249 B)"
FT   VARIANT         41
FT                   /note="Missing (in strain: R-2540; in allele 243 A)"
FT   VARIANT         52
FT                   /note="A -> T (in strain: R-2617; in allele 246 D)"
SQ   SEQUENCE   421 AA;  48536 MW;  EC070EC9E6501B52 CRC64;
     MNIDQHHQLQ QQHQQQMLQQ QAQAQAQAQA QAQQQQQQQQ QAAAAAAAAN AAATTSSSPR
     QVSFNVSDHY QILEIVGEGA YGIVCSAIHK PSQQKVAIKK IEPFERSMLC LRTLRELKLL
     KHFNHENIIS ILAIQRPINY ESFNEIYLIQ ELMETDLHRV IRTQNLSDDH IQYFIYQTLR
     ALKAMHSANV LHRDLKPSNL LLNSNCDLKI CDFGLARSIA SQEDNYGFMT EYVATRWYRA
     PEIMLTFQEY TTAIDVWSVG CILAEMLSGR PLFPGRDYHN QLWLIMEVLG TPNMEDYYNI
     KSKRAREYIR SLPFCKKIPF SELFANTNNN TSTSTSNTGG RTNINPLALD LLEKLLIFNP
     AKRITVEDAL KHPYLQLYHD PNDEPISDKI PEDFFDFDKM KDQLTIEDLK KLLYEEIMKP
     L
//