EIF3L_CAEEL
ID EIF3L_CAEEL Reviewed; 537 AA.
AC Q95QW0; Q8MQD4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=C17G10.9 {ECO:0000312|WormBase:C17G10.9a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C17G10.9a};
CC IsoId=Q95QW0-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C17G10.9b};
CC IsoId=Q95QW0-2; Sequence=VSP_036437;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit L family. {ECO:0000255|HAMAP-
CC Rule:MF_03011}.
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DR EMBL; FO080593; CCD64961.1; -; Genomic_DNA.
DR EMBL; FO080593; CCD64962.1; -; Genomic_DNA.
DR RefSeq; NP_001293503.1; NM_001306574.1. [Q95QW0-1]
DR RefSeq; NP_001293504.1; NM_001306575.1. [Q95QW0-2]
DR AlphaFoldDB; Q95QW0; -.
DR SMR; Q95QW0; -.
DR DIP; DIP-25447N; -.
DR IntAct; Q95QW0; 1.
DR STRING; 6239.C17G10.9a; -.
DR EPD; Q95QW0; -.
DR PaxDb; Q95QW0; -.
DR PeptideAtlas; Q95QW0; -.
DR EnsemblMetazoa; C17G10.9a.1; C17G10.9a.1; WBGene00015920. [Q95QW0-1]
DR EnsemblMetazoa; C17G10.9b.1; C17G10.9b.1; WBGene00015920. [Q95QW0-2]
DR GeneID; 24104220; -.
DR KEGG; cel:CELE_C17G10.9; -.
DR UCSC; C17G10.9a.1; c. elegans.
DR CTD; 24104220; -.
DR WormBase; C17G10.9a; CE27702; WBGene00015920; eif-3.L. [Q95QW0-1]
DR WormBase; C17G10.9b; CE30870; WBGene00015920; eif-3.L. [Q95QW0-2]
DR eggNOG; KOG3677; Eukaryota.
DR GeneTree; ENSGT00390000000411; -.
DR InParanoid; Q95QW0; -.
DR OMA; AGWFIRN; -.
DR PhylomeDB; Q95QW0; -.
DR Reactome; R-CEL-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-CEL-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-CEL-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-CEL-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:Q95QW0; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00015920; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q95QW0; baseline and differential.
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 Alternative splicing; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..537
FT /note="Eukaryotic translation initiation factor 3 subunit
FT L"
FT /id="PRO_0000364238"
FT DOMAIN 299..487
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..30
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"
FT VAR_SEQ 26..27
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_036437"
SQ SEQUENCE 537 AA; 62476 MW; CB0E46A93BE23410 CRC64;
MSRRVEFDLS TEDHSDRRRT NTFSSSADED GVPNEVADYL VYFSRMVDEQ NVPEILTLYD
QAFPDLTERF FRDRMWPDEN VVERIIGPGN KLFIILYKEL YYRQLYARNT RGPLLVHRYE
SFMNYQELFS ELLSSKDPIP LSLPNVWLWD IIDEFVYQFQ AFCLYKANPG KRNADEVEDL
INIEENQNAW NIYPVLNILY SLLSKSQIVE QLKALKEKRN PDSVADEFGQ SDLYFKLGYF
ALIGLLRTHV LLGDYHQALK TVQYVDIDPK GIYNTVPTCL VTLHYFVGFS HLMMRNYGEA
TKMFVNCLLY IQRTKSVQNQ QPSKKNFQYD VIGKTWDQLF HLLAICLAIQ PQRIDESIAS
QLSERCGERM MHMANGNIDE FRNAFATGCP KFLSPTTVVY EGVNQSKEPL LRQTQSFLEG
IESQMALPVL RGYLKLYTTL PTKKLASFMD VDDEHYDSFI GKLLTYKMIV NELGKEAGPS
SADDDEPQTD IDFYVDRDMI NIADTKVARH VGEHFIRHIQ KLQEVQDVLK RLDIQKP
