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IF4E1_SCHPO
ID   IF4E1_SCHPO             Reviewed;         218 AA.
AC   P78954;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=Eukaryotic translation initiation factor 4E-1;
DE            Short=eIF-4E-1;
DE            Short=eIF4E-1;
DE   AltName: Full=eIF-4F 25 kDa subunit 1;
DE   AltName: Full=mRNA cap-binding protein 1;
GN   Name=tif451; Synonyms=tif1, tif45; ORFNames=SPAC16E8.15;
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 [GENOMIC DNA].
RC   STRAIN=DSM 70576;
RX   PubMed=8955119; DOI=10.1074/jbc.271.51.32818;
RA   Ptushkina M., Fierro-Monti I., van den Heuvel J.J., Vasilescu S.,
RA   Birkenhaeger R., Mita K., McCarthy J.E.G.;
RT   "Schizosaccharomyces pombe has a novel eukaryotic initiation factor 4F
RT   complex containing a cap-binding protein with the human eIF4E C-terminal
RT   motif KSGST.";
RL   J. Biol. Chem. 271:32818-32824(1996).
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: Recognizes and binds the 7-methylguanosine-containing mRNA
CC       cap during an early step in the initiation of protein synthesis and
CC       facilitates ribosome binding by inducing the unwinding of the mRNAs
CC       secondary structures.
CC   -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC       varies with external and internal environmental conditions. It is
CC       composed of at least eIF4A, eIF4E and eIF4G. eIF4E is also known to
CC       interact with other partners.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC       {ECO:0000305}.
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DR   EMBL; X99444; CAA67807.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11043.1; -; Genomic_DNA.
DR   PIR; T43287; T43287.
DR   RefSeq; NP_594228.1; NM_001019651.2.
DR   AlphaFoldDB; P78954; -.
DR   SMR; P78954; -.
DR   BioGRID; 278201; 7.
DR   ELM; P78954; -.
DR   STRING; 4896.SPAC16E8.15.1; -.
DR   MaxQB; P78954; -.
DR   PaxDb; P78954; -.
DR   EnsemblFungi; SPAC16E8.15.1; SPAC16E8.15.1:pep; SPAC16E8.15.
DR   GeneID; 2541706; -.
DR   KEGG; spo:SPAC16E8.15; -.
DR   PomBase; SPAC16E8.15; -.
DR   VEuPathDB; FungiDB:SPAC16E8.15; -.
DR   eggNOG; KOG1670; Eukaryota.
DR   HOGENOM; CLU_043552_2_2_1; -.
DR   InParanoid; P78954; -.
DR   OMA; EEFWAIV; -.
DR   PhylomeDB; P78954; -.
DR   PRO; PR:P78954; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR   GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; ISO:PomBase.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; ISO:PomBase.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:PomBase.
DR   Gene3D; 3.30.760.10; -; 1.
DR   InterPro; IPR023398; TIF_eIF4e-like.
DR   InterPro; IPR001040; TIF_eIF_4E.
DR   InterPro; IPR019770; TIF_eIF_4E_CS.
DR   PANTHER; PTHR11960; PTHR11960; 1.
DR   Pfam; PF01652; IF4E; 1.
DR   SUPFAM; SSF55418; SSF55418; 1.
DR   PROSITE; PS00813; IF4E; 1.
PE   3: Inferred from homology;
KW   Initiation factor; Protein biosynthesis; Reference proteome; RNA-binding;
KW   Translation regulation.
FT   CHAIN           1..218
FT                   /note="Eukaryotic translation initiation factor 4E-1"
FT                   /id="PRO_0000193651"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   218 AA;  24958 MW;  80EFA94221311613 CRC64;
     MQTEQPPKES QTENTVSEPQ EKALRTVFDD KINFNLKHPL ARPWTLWFLM PPTPGLEWNE
     LQKNIITFNS VEEFWGIHNN INPASSLPIK SDYSFFREGV RPEWEDVHNK TGGKWAFQNK
     GRGGNALDEM WLTTVLAAIG ETLDPTGQEV MGVVINMRKG FYRLAVWTKS CNNREVLMEI
     GTRFKQVLNL PRSETIEFSA HEDSSKSGST RAKTRMSV
 
 
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