E2AK1_SCHPO
ID E2AK1_SCHPO Reviewed; 704 AA.
AC O13889;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Eukaryotic translation initiation factor 2-alpha kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase;
DE AltName: Full=Heme-regulated inhibitor 1;
GN Name=hri1; ORFNames=SPAC20G4.03c;
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], FUNCTION, INDUCTION, AUTOPHOSPHORYLATION, AND
RP MUTAGENESIS OF LYS-253.
RC STRAIN=SP223;
RX PubMed=12242291; DOI=10.1128/mcb.22.20.7134-7146.2002;
RA Zhan K., Vattem K.M., Bauer B.N., Dever T.E., Chen J.-J., Wek R.C.;
RT "Phosphorylation of eukaryotic initiation factor 2 by heme-regulated
RT inhibitor kinase-related protein kinases in Schizosaccharomyces pombe is
RT important for resistance to environmental stresses.";
RL Mol. Cell. Biol. 22:7134-7146(2002).
RN [2]
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: Mediates down-regulation of protein synthesis in response to
CC stress conditions by the phosphorylation of the alpha subunit of eIF-2
CC (tif211) on 'Ser-52'. Protein synthesis is inhibited at the level of
CC initiation. Activity is inhibited in the presence of heme.
CC {ECO:0000269|PubMed:12242291}.
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 -!- INDUCTION: By heat shock and arsenic. {ECO:0000269|PubMed:12242291}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. GCN2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF536223; AAN04053.1; -; mRNA.
DR EMBL; CU329670; CAB11253.1; -; Genomic_DNA.
DR PIR; T38117; T38117.
DR RefSeq; NP_594738.1; NM_001020166.2.
DR AlphaFoldDB; O13889; -.
DR BioGRID; 278222; 26.
DR STRING; 4896.SPAC20G4.03c.1; -.
DR iPTMnet; O13889; -.
DR MaxQB; O13889; -.
DR PaxDb; O13889; -.
DR PRIDE; O13889; -.
DR EnsemblFungi; SPAC20G4.03c.1; SPAC20G4.03c.1:pep; SPAC20G4.03c.
DR GeneID; 2541728; -.
DR KEGG; spo:SPAC20G4.03c; -.
DR PomBase; SPAC20G4.03c; hri1.
DR VEuPathDB; FungiDB:SPAC20G4.03c; -.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_000288_134_1_1; -.
DR InParanoid; O13889; -.
DR OMA; CLYIQMA; -.
DR PhylomeDB; O13889; -.
DR PRO; PR:O13889; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IDA:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IMP:PomBase.
DR GO; GO:0023052; P:signaling; IC: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; 2.
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 Protein synthesis inhibitor; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..704
FT /note="Eukaryotic translation initiation factor 2-alpha
FT kinase 1"
FT /id="PRO_0000085949"
FT DOMAIN 224..667
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 491
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 230..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 253
FT /note="K->M: No activity."
FT /evidence="ECO:0000269|PubMed:12242291"
SQ SEQUENCE 704 AA; 79064 MW; F3C0DD8CFDA1300C CRC64;
MLGTSTKCSK RDCNYAKENI SRIMPTIGLG YKQNFEKKTA DTQSSCKLLL VALLESFCKH
SDQTPEQSKQ MFLYVAHSLQ NSGIIDFEFS EELEPIRNAY ADSLHNLLSK AFRSTLPMSS
TKDSKKSRYS SPDGVLAKTA SFLSVLSDGG YEDDVMNVKP SVNVLSNRLN HLPVEALESC
FPQTTLESST FADFCEHKDG TGNLSFSNFD SFPTVQRSRY ASDFEELELL GKGGYGSVYK
ARNKFDGVEY ALKKIPLRLR SFSTSSNIFR ESRTLARLNH PNVIRFFSSW VELLPSSEKQ
IEEEPLASAD ETLSQSADID NFMFDMDTGL LQHTYPSSVQ ILFQEDSVAD DLTPCYSTKN
STCNLTDLFK KEADQDYAES HDCSSTTSQV DTLGKLAPTK SASEMLLMDS FLSEREEDEC
SNIPSFDQQP LCLYIQMALC EETLEKHINR RNKHIHGVMS KGLRNCYILL FARILEGVLY
LHDAMHLVHR DLKPRNIFLS SGVHSEPCSV CLPNFSDEDN VEVSNAYEPV NQRTLCVVPK
IGDFGLVLSQ SDNLEEGTNS SAESSFVGTS TYAAPELFSK HMRSVMNNNS STDIYALGIL
FFELLYPFNT RMERASAIAN LKKGIFPHDF LDSMPEEASL IRSMLSSSNK RPTAAQLLTS
NLFHDLVVNE LHVYQALLED AEKRNNNLKA ELNILRVLNP NYDC
