Q5F428

PR
Gene name
EIF3L
Protein name
Eukaryotic translation initiation factor 3 subunit L
Names
eIF3l
Species
Gallus gallus (Chicken)
KEGG Pathway
gga:418033
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-65 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q5F428

Entry ID Method Resolution Chain Position Source
AF-Q5F428-F1 Predicted AlphaFoldDB

12 variants for Q5F428

Variant ID(s) Position Change Description Diseaes Association Provenance
rs732125402 51 V>G No Ensembl
rs314669895 195 Q>L No Ensembl
rs731886322 266 Y>S No Ensembl
rs1060136783 316 Y>C No Ensembl
rs732709418 368 H>P No Ensembl
rs737474399 376 T>P No Ensembl
rs735364983 380 M>T No Ensembl
rs739312259 442 Q>H No Ensembl
rs738583552 459 T>P No Ensembl
rs739881559 474 K>Q No Ensembl
rs1059156593 482 T>I No Ensembl
rs731616410 492 V>G No Ensembl

No associated diseases with Q5F428

1 regional properties for Q5F428

Type Name Position InterPro Accession
domain Proteasome component (PCI) domain 331 - 537 IPR000717

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
eukaryotic 43S preinitiation complex A protein complex composed of the 40S ribosomal subunit plus eIF1A, eIF3, and eIF2-GTP-bound methionyl-initiator methionine tRNA.
eukaryotic 48S preinitiation complex A protein complex composed of the small ribosomal subunit, eIF3, eIF1A, methionyl-initiatior methionine and a capped mRNA. The complex is initially positioned at the 5'-end of the capped mRNA.
eukaryotic translation initiation factor 3 complex A complex of several polypeptides that plays at least two important roles in protein synthesis: First, eIF3 binds to the 40S ribosome and facilitates loading of the Met-tRNA/eIF2.GTP ternary complex to form the 43S preinitiation complex. Subsequently, eIF3 apparently assists eIF4 in recruiting mRNAs to the 43S complex. The eIF3 complex contains five conserved core subunits, and may contain several additional proteins; the non-core subunits are thought to mediate association of the complex with specific sets of mRNAs.

1 GO annotations of molecular function

Name Definition
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.

2 GO annotations of biological process

Name Definition
formation of cytoplasmic translation initiation complex Joining of the large subunit, with release of IF2/eIF2 and IF3/eIF3. This leaves the functional ribosome at the AUG, with the methionyl/formyl-methionyl-tRNA positioned at the P site.
translational initiation The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3ZCK1 EIF3L Eukaryotic translation initiation factor 3 subunit L Bos taurus (Bovine) PR
A5A6M4 EIF3L Eukaryotic translation initiation factor 3 subunit L Pan troglodytes (Chimpanzee) PR
Q9Y262 EIF3L Eukaryotic translation initiation factor 3 subunit L Homo sapiens (Human) PR
Q8QZY1 Eif3l Eukaryotic translation initiation factor 3 subunit L Mus musculus (Mouse) PR
Q6P878 eif3l Eukaryotic translation initiation factor 3 subunit L Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
Q7T2A5 eif3l Eukaryotic translation initiation factor 3 subunit L Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MAYPGEDYDN DAAYDPYAYS NDYDMHTGDP KQDLAYERQY EQQTYQVIPE VIKNFIQYFH
70 80 90 100 110 120
KTVSDLIDQK VYELQASRVS SDVIDQKVYE IQDIYENSWT KLTERFFKNT PWPEAEAIAP
130 140 150 160 170 180
QVGNDAVFLI LYKELYYRHI YAKVSGGPTL EQRFESYYNY CNLFNYILNA DGPAPLELPN
190 200 210 220 230 240
QWLWDIIDEF IYQFQSFSQY RCKTAKKSEE EIDFLRSNPK IWNVHSVLNV LHSLVDKSNI
250 260 270 280 290 300
NRQLEVYTSG GDPESVAGEY GRHSLYKMLG YFSLVGLLRL HSLLGDYYQA IKVLENIELN
310 320 330 340 350 360
KKSMYSRVPE CQVTTYYYVG FAYLMMRRYQ DAIRVFANIL LYIQRTKSMF QRTTYKYEMI
370 380 390 400 410 420
NKQNEQMHAL LAIALTMYPM RIDESIHLQL REKYGDKMLR MQKGDAQVYE ELFSYACPKF
430 440 450 460 470 480
LSPVVPNYDN VHPNYHKEPF LQQLKVFADE VQQQAQLSTI RSFLKLYTTM PVAKLAGFLD
490 500 510 520 530 540
LTEQEFRIQL LVFKHKMKNL VWTSGISALD GEFQSASEVD FYIDKDMIHI ADTKVARRYG
550 560
DFFIRQIHKF EELNRTLKKM GQRP