YIH1_SCHPO
ID YIH1_SCHPO Reviewed; 280 AA.
AC O13997;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein IMPACT homolog;
GN Name=yih1; ORFNames=SPAC27E2.02;
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: Translational regulator that ensures constant high levels of
CC translation under amino acid starvation. Plays a role as a negative
CC regulator of the gcn2 kinase activity; impairs gcn1-mediated gcn2
CC activation, and hence gcn2-mediated eIF-2-alpha phosphorylation in
CC amino acid-starved cells and subsequent down-regulation of protein
CC synthesis. In normal conditions, it resides in a actin complex and has
CC no activity. {ECO:0000250|UniProtKB:P25637}.
CC -!- SUBUNIT: Interacts (via N-terminus) with gcn1 (via C-terminus); this
CC interaction reduces the gcn1-gcn20 complex formation and prevents the
CC interaction of gcn1 with gcn2 protein kinase and gcn2 activation in
CC amino acid-starved cells. Interacts (via C-terminus) with act1; this
CC interaction occurs in a gcn1-independent manner. Interacts with rpl39;
CC this interaction occurs in a gcn1-independent manner. Associates (via
CC middle region) with ribosomes; this association occurs in a gcn1-
CC independent manner and persists under amino acid starvation conditions.
CC {ECO:0000250|UniProtKB:P25637}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IMPACT family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11676.1; -; Genomic_DNA.
DR PIR; T38449; T38449.
DR RefSeq; NP_594402.1; NM_001019833.2.
DR AlphaFoldDB; O13997; -.
DR SMR; O13997; -.
DR BioGRID; 278315; 16.
DR STRING; 4896.SPAC27E2.02.1; -.
DR iPTMnet; O13997; -.
DR MaxQB; O13997; -.
DR PaxDb; O13997; -.
DR PRIDE; O13997; -.
DR EnsemblFungi; SPAC27E2.02.1; SPAC27E2.02.1:pep; SPAC27E2.02.
DR GeneID; 2541824; -.
DR KEGG; spo:SPAC27E2.02; -.
DR PomBase; SPAC27E2.02; yih1.
DR VEuPathDB; FungiDB:SPAC27E2.02; -.
DR eggNOG; KOG3299; Eukaryota.
DR HOGENOM; CLU_045276_0_1_1; -.
DR InParanoid; O13997; -.
DR OMA; WNVMVVV; -.
DR PhylomeDB; O13997; -.
DR PRO; PR:O13997; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0004860; F:protein kinase inhibitor activity; TAS:PomBase.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:PomBase.
DR GO; GO:1990611; P:regulation of cytoplasmic translational initiation in response to stress; ISS:PomBase.
DR GO; GO:0006446; P:regulation of translational initiation; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; IC:PomBase.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.230.30; -; 1.
DR InterPro; IPR023582; Impact.
DR InterPro; IPR001498; Impact_N.
DR InterPro; IPR036956; Impact_N_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR16301; PTHR16301; 1.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF01205; UPF0029; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
PE 3: Inferred from homology;
KW Actin-binding; Cytoplasm; Nucleus; Reference proteome; Repressor;
KW Stress response; Translation regulation.
FT CHAIN 1..280
FT /note="Protein IMPACT homolog"
FT /id="PRO_0000316614"
FT DOMAIN 9..109
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
SQ SEQUENCE 280 AA; 31485 MW; 90FDE06A14091219 CRC64;
MENNEEFQDE LLALESIYPS CLLPISEQSF TYTLSIPDSS VRLNIQFPLD YPNSAPTVLD
AYGIDKTLAE DVLLSVATGD VCIFSYMDLL KELVDIDAEQ AAAERESKLQ EESDKETPVM
LNKSHYVAKT PEIQDEPWKP KFDWKESEPI TDRKSTFMAH ATRVYSTEEV REALEDLYMD
KKVAKANHNM VAYRIISPNG NVIQDNDDDG ESAAGSRMSH LLTMMSAENV FVCVSRWFGG
VHIGPDRFKH INSSAREAVL LTDAAPSQKK GTEHGKKKKK
