GCN1_SCHPO
ID GCN1_SCHPO Reviewed; 2670 AA.
AC Q10105;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=eIF-2-alpha kinase activator gcn1 {ECO:0000250|UniProtKB:P33892};
DE AltName: Full=Translational activator gcn1 {ECO:0000250|UniProtKB:P33892};
GN Name=gcn1 {ECO:0000312|PomBase:SPAC18G6.05c}; ORFNames=SPAC18G6.05c;
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 [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: Acts as a positive activator of the gcn2 protein kinase
CC activity in response to amino acid starvation. Component of the gcn1-
CC gcn20 complex that forms a complex with gcn2 on translating ribosomes;
CC during this process, gcn1 seems to act as a chaperone to facilitate
CC delivery of uncharged tRNAs that enter the A site of ribosomes to the
CC tRNA-binding domain of gcn2, and hence stimulating gcn2 kinase
CC activity. Participates in the repression of global protein synthesis
CC and in gene-specific mRNA translation activation, such as the
CC transcriptional activator fil1, by promoting the gcn2-mediated
CC phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-
CC alpha/tif211) on 'Ser-52', and hence allowing fil1-mediated
CC reprogramming of amino acid biosynthetic gene expression to alleviate
CC nutrient depletion. {ECO:0000250|UniProtKB:P33892}.
CC -!- SUBUNIT: Interacts (via N- and C-terminus) with gcn2 (via N-terminal
CC RWD domain); this interaction stimulates gcn2 kinase activity in a
CC gcn20-dependent manner in response to amino acid starvation. Interacts
CC (via C-terminus) with gcn20 (via N-terminus); this interaction
CC stimulates gcn2 kinase activity in response to amino acid starvation.
CC The gcn1-gcn20 complex interacts with gcn2 on translating ribosomes in
CC amino acid-starved cells; gcn1 may bind near the ribosomal A-site and
CC promotes the transfer of uncharged tRNAs from the A-site to the tRNA-
CC binding domain in gcn2 for its subsequent kinase activation, and hence
CC allowing fil1 translational activation and derepression of amino acid
CC biosynthetic genes. Interacts (via C-terminus) with yih1 (via N-
CC terminus); this interaction reduces the gcn1-gcn20 complex formation
CC and prevents the interaction of gcn1 with gcn2 and gcn2 kinase
CC activation in amino acid-starved cells. {ECO:0000250|UniProtKB:P33892}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P33892}.
CC -!- DOMAIN: The EF3-like region is necessary and sufficient for interaction
CC with gcn20. {ECO:0000250|UniProtKB:P33892}.
CC -!- SIMILARITY: Belongs to the GCN1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA92385.1; -; Genomic_DNA.
DR PIR; T37919; T37919.
DR RefSeq; NP_593669.1; NM_001019101.2.
DR AlphaFoldDB; Q10105; -.
DR BioGRID; 278707; 25.
DR STRING; 4896.SPAC18G6.05c.1; -.
DR iPTMnet; Q10105; -.
DR MaxQB; Q10105; -.
DR PaxDb; Q10105; -.
DR PRIDE; Q10105; -.
DR EnsemblFungi; SPAC18G6.05c.1; SPAC18G6.05c.1:pep; SPAC18G6.05c.
DR GeneID; 2542235; -.
DR KEGG; spo:SPAC18G6.05c; -.
DR PomBase; SPAC18G6.05c; gcn1.
DR VEuPathDB; FungiDB:SPAC18G6.05c; -.
DR eggNOG; KOG1242; Eukaryota.
DR HOGENOM; CLU_000504_2_0_1; -.
DR InParanoid; Q10105; -.
DR OMA; DQWRSKK; -.
DR PhylomeDB; Q10105; -.
DR PRO; PR:Q10105; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR GO; GO:0030295; F:protein kinase activator activity; IMP:PomBase.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:1904689; P:negative regulation of cytoplasmic translational initiation; IDA:PomBase.
DR GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033173; Gcn1.
DR InterPro; IPR022716; Gcn1_N.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR23346:SF7; PTHR23346:SF7; 1.
DR Pfam; PF12074; Gcn1_N; 1.
DR Pfam; PF02985; HEAT; 1.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
DR PROSITE; PS50077; HEAT_REPEAT; 4.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; Reference proteome; Repeat; Stress response;
KW Translation regulation.
FT CHAIN 1..2670
FT /note="eIF-2-alpha kinase activator gcn1"
FT /id="PRO_0000116458"
FT REPEAT 32..69
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 89..129
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 143..181
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 185..227
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 273..310
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 315..352
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 397..434
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 474..513
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 548..586
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 722..757
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 758..794
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 934..972
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 978..1018
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1025..1062
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1063..1099
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1224..1261
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REPEAT 1276..1316
FT /note="HEAT 17"
FT /evidence="ECO:0000255"
FT REPEAT 1319..1356
FT /note="HEAT 18"
FT /evidence="ECO:0000255"
FT REPEAT 1397..1435
FT /note="HEAT 19"
FT /evidence="ECO:0000255"
FT REPEAT 1439..1476
FT /note="HEAT 20"
FT /evidence="ECO:0000255"
FT REPEAT 1478..1514
FT /note="HEAT 21"
FT /evidence="ECO:0000255"
FT REPEAT 1518..1555
FT /note="HEAT 22"
FT /evidence="ECO:0000255"
FT REPEAT 1557..1593
FT /note="HEAT 23"
FT /evidence="ECO:0000255"
FT REPEAT 1595..1632
FT /note="HEAT 24"
FT /evidence="ECO:0000255"
FT REPEAT 1637..1674
FT /note="HEAT 25"
FT /evidence="ECO:0000255"
FT REPEAT 1676..1713
FT /note="HEAT 26"
FT /evidence="ECO:0000255"
FT REPEAT 1714..1751
FT /note="HEAT 27"
FT /evidence="ECO:0000255"
FT REPEAT 1755..1792
FT /note="HEAT 28"
FT /evidence="ECO:0000255"
FT REPEAT 1793..1830
FT /note="HEAT 29"
FT /evidence="ECO:0000255"
FT REPEAT 1861..1898
FT /note="HEAT 30"
FT /evidence="ECO:0000255"
FT REPEAT 1899..1939
FT /note="HEAT 31"
FT /evidence="ECO:0000255"
FT REPEAT 1941..1977
FT /note="HEAT 32"
FT /evidence="ECO:0000255"
FT REPEAT 1982..2019
FT /note="HEAT 33"
FT /evidence="ECO:0000255"
FT REPEAT 2020..2055
FT /note="HEAT 34"
FT /evidence="ECO:0000255"
FT REPEAT 2057..2090
FT /note="HEAT 35"
FT /evidence="ECO:0000255"
FT REPEAT 2092..2128
FT /note="HEAT 36"
FT /evidence="ECO:0000255"
FT REPEAT 2171..2208
FT /note="HEAT 37"
FT /evidence="ECO:0000255"
FT REPEAT 2239..2276
FT /note="HEAT 38"
FT /evidence="ECO:0000255"
FT REPEAT 2319..2361
FT /note="HEAT 39"
FT /evidence="ECO:0000255"
FT REPEAT 2379..2416
FT /note="HEAT 40"
FT /evidence="ECO:0000255"
FT REPEAT 2625..2662
FT /note="HEAT 41"
FT /evidence="ECO:0000255"
FT REGION 1365..1675
FT /note="EF3-like region"
FT /evidence="ECO:0000250|UniProtKB:P33892"
SQ SEQUENCE 2670 AA; 297338 MW; 948E9316D56D74C3 CRC64;
MSVEEPGIEA HGHKDRMLYA MLLSKDTSLA FLGSKKIMID ILQHICRTQD IDEESAIAAL
EDIFETLPRN LSRDARKQIE ITINHLVSRL PSIVLPFLVR RLTTIAGRLD RFRSTVSVSF
DCLNWVNSMI PNLPEKELQY WILELLPLQS SFLSYALRDG KPSVADSAIK STRRCYRSLF
CKKMDSLKKL VSFLLTETEN AILPPKSLPL YGVIISTCYY FHQSPNPRNE ISQQAELFSK
IMAQNVLMAK PALEKYLYHE FCYSLGLLLS VDQLKLYLLP SIEKALLRSP EIIFSGILSS
LAHGFADSKV DASSLILSSV LTSFVNGLKS SNAEVRRNCF QTFKDLSANA SDNESLSRVA
SELITSLRTG KVTASDQRVL FVDALSSLSL KHIDASMLLN ELLPLFTKAK ESDFNSLASL
IVKTLKFLLM NGRNPGDKIY DFLSKSLQRP VAHESMFWLT SLATMAWDLP ASDDVQIEFI
NFFLNNLSIL TEKALMSVSG ATQNGTYLAP IIYLSFGVNK LSVWNSERIS HTLELQDILV
KLSTPKNNDV FIFSSKITNK LNDDQSKLWY FQGLCDFAKV SDNLLFSNFV ERWFQSVIGV
FSFASRENSN RALKILKSAI LYRPHLRMSI CSQLWNYHAD FEKSKSVGKF DSAKYDEISS
LFQSLILSSM SADTSNFSNQ ELVDFDKYLV ELLFLSFAFK DKFDWIRFCQ VSKRDPATLV
SERIHSIIEE IELLLSSAIK DSKETAAIAS ISMIVFVAPE ESIPLFVNVF RNQLLHLNIS
SVSSTDLEIW KTPEGVLWDN VLEKKSSKKL DKNTKDYETK RWEAEVRAKQ SAKKPAKLSK
DQQALVDAQL DAEAKIRSRV NLIALSLERG LGIIRSLGEA VQLAPALWVE DAIDVLLFHN
VLKYSEPFLK NLAYDTFLLT LKASGFSERL GDRSYSSSLA SILAHTFSVN SSENIKELTK
SILYKLRFAI EQNYFEPQMF ACIFPLLYDL TFNITNSDEE DEAELQLLVT EILEFQALYS
ASLRRMRSKL IKSLLHLLEI APTQYQENKN SLLSLCEGLH STYTDEELNL LLSNLFHPES
SIRSAVLQAL QAFDLSRFEF IKEIFLELYD DNETNASIAH QISTQNGLDA TETSFFELQI
FFTQDSDYLQ QIIGKSLIDL LDEFEELGQF IPKELMRTYR ENALPSAPEY DEYGIIKKET
IGRDLGRIAR ESVAVSFFHI SKYLSSNLLL PFLEFLLTAS EAEAQIPVTD ASQKVSSKML
EAGKLAIFQS GAHQVEALME LFEQKLNVDS LPTDANDRLR EATVVLFGTV AQHLPSNDPR
LAVVMDSLLS VLSTPSESVQ LAVAVCLPPL VKKSLGKSKE YYELLSNKLM NSTSLADQKG
AAYGLAGLVK GYGIKAFQDF NILDSLSELI SNRQNATHRQ VALFAVEAFS RILGIYFEPY
LPDLLPLLLT SFGDNANEVR EATMDAVKQI MSQLSAFGVK LLLPTLLDGL NEYNWRSKKA
SVEILGLMSY MAPKQLSVFL PTIIPKLSEV LTDSHSQVRN TANKSLLRFG DVISNPEIQT
LVPTLLKALS DCTRYTDDAL EALLKTSFVH YLDPPSLALV IPILKYGLRE RNAGTKRQSA
KIFGLMASLT EPENLAVYLE SLMPRLREVL IDPVPDTRAT AAKALGSLIE KLGEKKFPTL
IPELFNVLRS ECSEVDRQGA AQGLSEILAG LGLARLEDVL PEILKNTSSP VPHIRESFIS
LLIYLPATFG SRFQPYLARA IPPILSGLAD DSELVQTASL RAAKMIVNNY ATKSVDLLLP
ELEKGLFDNA WRIRLSSVQL VGDLVFKLAG INRKALQEDE EEEGTHSDVS RKALLDIIGQ
ERHDRILSTL YIVRQDIAAV VRTPAIQIWK AIVVNTPRTV REILPTLTSI IVSNLNSSSN
DRRTMCVKSL GDLLKKAGFD VLPQLLPVLK QGLESANSGD RIGVCIALEE LINSATPEQL
EIYSDDFVYA VRRALMDGDL EVRETAAEAF DSLQSILGDR AVDDVLPQLL KLLESENQSE
QALSALREII SRRSSTIFPV LIPTLIKKPV SAFNARALSS LAQVAGVTLN KRLPSILNAL
MESSLASTGD DLVALNGAID KVNLSVKDQE GLQILMAHFY SFSESEDFRK RLFAAEHMLV
FFQNCKLDYY RYVGDWVRHF ITLFEDKSQD VVVAAVAAQN TLVSALRKDQ LDSLVSIAYH
SLRDVGSQGV NLPAFEVAQG VNSILPIFLY GLMHGTMDQR EQSALGIADI VLKTEPSKLR
PFVTQITGPL IRIIGERFPV EVKCAILYTL NIILSKISTF LRPFLPQLQR TFAKCLGDPS
SEVIRSRAAT ALGTLITLQT RLAPIITELV SGARTPDAGV RKAMLNALFA VVSKSGQNMN
EASAEAIEQL LDEISAESSE HMVICAKLYG ALFSHLPDAQ AKQLLESKVL SLEIQSEFSV
LILNAAVKFG SQKIIELKLS DIVCSIISTA SLQKEVTIAE NGILALGKAL LADIPQSFGN
AKNLVEALKV NIEAPPSTSQ DSRRLALLII RVVSKENYSL IKPHISILAP AIFGCVRAIV
IPVKLAAEAA FLALFQLVED DSVLNKYIET LEGPRARSFV DYSRRVAVKL AAAERDRINS
GSERVKLEEV EDLAEINAVG RDNEVSTNDP
