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EIF3J_SCHPO
ID   EIF3J_SCHPO             Reviewed;         274 AA.
AC   P87128;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable eukaryotic translation initiation factor 3 subunit J;
DE            Short=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009};
DE   AltName: Full=Eukaryotic translation initiation factor 3 30 kDa subunit;
DE            Short=eIF-3 30 kDa;
GN   ORFNames=SPAC3A12.13c;
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).
RN   [2]
RP   INTERACTION WITH SAD1.
RX   PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA   Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT   "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT   membrane-bound components of the spindle pole body in fission yeast.";
RL   Mol. Genet. Genomics 270:449-461(2004).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03009}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. The eIF-3 complex appears to include tif32/eif3a,
CC       SPAC25G10.08/eif3b, tif33/eif3c, SPBC4C3.07/eif3f, tif35/eif3g and
CC       sum1/eif3i. This set of common subunits may also associate exclusively
CC       with either moe1/eif3d and int6/eif3e, or with SPAC821.05/eif3h and
CC       SPAC1751.03/eif3m. The eIF-3 complex may also include
CC       SPAC3A12.13c/eif3j (By similarity). Interacts with sad1
CC       (PubMed:14655046). {ECO:0000255|HAMAP-Rule:MF_03009,
CC       ECO:0000269|PubMed:14655046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit J family. {ECO:0000255|HAMAP-
CC       Rule:MF_03009}.
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DR   EMBL; CU329670; CAB08741.1; -; Genomic_DNA.
DR   PIR; T38681; T38681.
DR   RefSeq; NP_593339.1; NM_001018771.2.
DR   AlphaFoldDB; P87128; -.
DR   BioGRID; 279540; 45.
DR   IntAct; P87128; 1.
DR   STRING; 4896.SPAC3A12.13c.1; -.
DR   iPTMnet; P87128; -.
DR   MaxQB; P87128; -.
DR   PaxDb; P87128; -.
DR   PRIDE; P87128; -.
DR   EnsemblFungi; SPAC3A12.13c.1; SPAC3A12.13c.1:pep; SPAC3A12.13c.
DR   GeneID; 2543108; -.
DR   KEGG; spo:SPAC3A12.13c; -.
DR   PomBase; SPAC3A12.13c; -.
DR   VEuPathDB; FungiDB:SPAC3A12.13c; -.
DR   eggNOG; KOG4813; Eukaryota.
DR   HOGENOM; CLU_1016189_0_0_1; -.
DR   InParanoid; P87128; -.
DR   OMA; MDSWEDF; -.
DR   Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SPO-72649; Translation initiation complex formation.
DR   Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-SPO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR   PRO; PR:P87128; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; ISO:PomBase.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:PomBase.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IDA:PomBase.
DR   GO; GO:0019843; F:rRNA binding; ISO:PomBase.
DR   GO; GO:0003743; F:translation initiation factor activity; ISO:PomBase.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:PomBase.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; ISO:PomBase.
DR   Gene3D; 1.10.246.60; -; 1.
DR   HAMAP; MF_03009; eIF3j; 1.
DR   InterPro; IPR023194; eIF3-like_dom_sf.
DR   InterPro; IPR013906; eIF3j.
DR   PANTHER; PTHR21681; PTHR21681; 1.
DR   Pfam; PF08597; eIF3_subunit; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..274
FT                   /note="Probable eukaryotic translation initiation factor 3
FT                   subunit J"
FT                   /id="PRO_0000116638"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   274 AA;  30532 MW;  E34EC5F6D4E48805 CRC64;
     MDSWEDFLVE DPAKPAEFDF PLGKDSQSSS KPKKRFDDEE DEDEEENKES LQNDSHSVSQ
     KSSSSSQNDQ GSNKMTRIQQ KIQERNFEKA IKASEAAAKE ESLESSKEAM RQAEIDSDLA
     NAMDLFDIVD KNSASANRSK QADQRQLKTK ADYAAFQADI LKKVKNCQTT AEYNNFVQDL
     IPLLLTGLNA TNLKAVQKSV NKLVVNKEQQ EKTQSKRGAA APAAKPVSTA APSKKGGKPT
     VNVNSKKTVA DKSAYEDYIE DEYDDYADDF DDFM
 
 
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