ID   5MP1_MUSMM              Reviewed;         419 AA.
AC   Q2L4X1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=eIF5-mimic protein 1 {ECO:0000250|UniProtKB:Q9Y6E2};
DE   AltName: Full=Basic leucine zipper and W2 domain-containing protein 2;
DE   AltName: Full=Brain development-related molecule 2;
GN   Name=Bzw2; Synonyms=5mp1 {ECO:0000250|UniProtKB:Q9Y6E2}, Bdm2;
OS   Mus musculus molossinus (Japanese house mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=57486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Tashiro H., Moriguchi A., Noguchi M., Shirasaki R., Yoshida N.,
RA   Shirafuji N.;
RT   "Isolation and characterization of murine cDNA clones using newly
RT   constructed gene trap vector.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Translation initiation regulator which represses non-AUG
CC       initiated translation and repeat-associated non-AUG (RAN) initiated
CC       translation by acting as a competitive inhibitor of eukaryotic
CC       translation initiation factor 5 (EIF5) function (By similarity).
CC       Increases the accuracy of translation initiation by impeding EIF5-
CC       dependent translation from non-AUG codons by competing with it for
CC       interaction with EIF2S2 within the 43S pre-initiation complex (PIC) in
CC       an EIF3C-binding dependent manner (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y6E2}.
CC   -!- SUBUNIT: Interacts with EIF3E, EIF2S2 and EIF3C.
CC       {ECO:0000250|UniProtKB:Q9Y6E2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6E2}.
CC   -!- SIMILARITY: Belongs to the BZW family. {ECO:0000305}.
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DR   EMBL; AB244988; BAE79268.1; -; mRNA.
DR   CCDS; CCDS25884.1; -.
DR   AlphaFoldDB; Q2L4X1; -.
DR   SMR; Q2L4X1; -.
DR   PRIDE; Q2L4X1; -.
DR   MGI; MGI:1914162; Bzw2.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR   CDD; cd11560; W2_eIF5C_like; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR043510; W2_BZW1/2.
DR   InterPro; IPR003307; W2_domain.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51363; W2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Translation regulation.
FT   CHAIN           1..419
FT                   /note="eIF5-mimic protein 1"
FT                   /id="PRO_0000254621"
FT   DOMAIN          248..415
FT                   /note="W2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         117
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6E2"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6E2"
FT   MOD_RES         414
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6E2"
FT   MOD_RES         419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTT7"
SQ   SEQUENCE   419 AA;  48063 MW;  996FC462B50EAF6F CRC64;
     MNKHQKPVLT GQRFKTRKRD EKEKFEPTVF RDTLVQGLNE AGDDLEAVAK FLDSTGSRLD
     YRRYADTLFD ILVAGSMLAP GGTRIDDGDK TKMTNHCVFS ANEDHETIRN YAQVFNKLIR
     RYKYLEKAFE DEMKKLLLFL KAFSEAEQTK LAMLSGILLG NGTLPATILT SLFTDSLVKE
     GIAASFAVKL FKAWMAEKDA NSVTSSLRKA NLDKRLLELF PVNRQSVDHF AKYFTDAGLK
     ELSDFLRVQQ SLGTRKELQK ELQERLSQEC PIKEVVLYVK EEMKRNDLPE TAVIGLLWTC
     IMNAVEWNKK EELVAEQALK HLKQYAPLLA VFSSQGQSEL VLLQKVQEYC YDNIHFMKAF
     QKIVVLFYKA DVLSEEAILK WYKEAHAAKG KSVFLDQMKK FVEWLQNAEE ESESEGEES