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EIF3L_CAEBR
ID   EIF3L_CAEBR             Reviewed;         537 AA.
AC   A8X419;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit L {ECO:0000255|HAMAP-Rule:MF_03011};
DE            Short=eIF3l {ECO:0000255|HAMAP-Rule:MF_03011};
GN   Name=eif-3.L {ECO:0000255|HAMAP-Rule:MF_03011};
GN   ORFNames=CBG06959 {ECO:0000312|WormBase:CBG06959};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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_03011}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03011}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03011}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit L family. {ECO:0000255|HAMAP-
CC       Rule:MF_03011}.
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DR   EMBL; HE600960; CAP27379.1; -; Genomic_DNA.
DR   RefSeq; XP_002632106.1; XM_002632060.1.
DR   AlphaFoldDB; A8X419; -.
DR   SMR; A8X419; -.
DR   STRING; 6238.CBG06959; -.
DR   EnsemblMetazoa; CBG06959.1; CBG06959.1; WBGene00029140.
DR   GeneID; 8574104; -.
DR   KEGG; cbr:CBG_06959; -.
DR   CTD; 8574104; -.
DR   WormBase; CBG06959; CBP15837; WBGene00029140; Cbr-eif-3.L.
DR   eggNOG; KOG3677; Eukaryota.
DR   HOGENOM; CLU_029210_1_0_1; -.
DR   InParanoid; A8X419; -.
DR   OMA; AGWFIRN; -.
DR   OrthoDB; 393910at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   HAMAP; MF_03011; eIF3l; 1.
DR   InterPro; IPR019382; eIF3l.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR13242; PTHR13242; 1.
DR   Pfam; PF10255; Paf67; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..537
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   L"
FT                   /id="PRO_0000364237"
FT   DOMAIN          297..485
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  62504 MW;  2C24E1E444FE8AF4 CRC64;
     MSRRVEFDMS HEDHTDRRRT NTFSSEEDGV PNEVADYLVY FSRMIDEQNV PEILTLYDQA
     FPDLTERFFR DRMWPDENVV ERIIGPGNKL FIILYKELYY RQLYARNARG PLLVHRYESF
     MNYQELFSEL LSSKDPIPLS LPNVWLWDII DEFVYQFQAF CLYKANPGKR NADEVEDLIN
     IEENQNAWNI YPVLNILYSL LSKSQIVEQL KALKEKRNPD SVADEFGQSD LYFKLGYFAL
     IGLLRTHVLL GDYHQALKTV QYVDIDPKGI YNTVPTCLVT LHYFVGFSHL MMRNYGEATK
     MFVNCLLYIQ RTKTVQSQQP SKKNFQYDVI GKTWDQLFYL LAICLAVQPQ RIDESIASQL
     AERCGERMMH MANGNVDEFR NAFSTGCPKF LSPTTVVYEG VNQSKEPLLR QTQSFLEGIE
     SQMALPVLRG YLKLYTTLPT KKLASFMDVD EENYDSFLGK LLTYKMIVNE LGKEAGPSTV
     DDDEPQTDID FYVDRDMINI ADTKVARHVG EHFLRHIQKL QEVQDVLKRL DSAGQKP
 
 
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