ID   5MP1_MACFA              Reviewed;         419 AA.
AC   Q4R6R4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=eIF5-mimic protein 1 {ECO:0000250|UniProtKB:Q9Y6E2};
DE   AltName: Full=Basic leucine zipper and W2 domain-containing protein 2;
GN   Name=BZW2; Synonyms=5MP1 {ECO:0000250|UniProtKB:Q9Y6E2};
GN   ORFNames=QtsA-17345;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-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; AB169116; BAE01210.1; -; mRNA.
DR   AlphaFoldDB; Q4R6R4; -.
DR   SMR; Q4R6R4; -.
DR   STRING; 9541.XP_005550109.1; -.
DR   eggNOG; KOG2297; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
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; Reference proteome;
KW   Translation regulation.
FT   CHAIN           1..419
FT                   /note="eIF5-mimic protein 1"
FT                   /id="PRO_0000254619"
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"
SQ   SEQUENCE   419 AA;  48090 MW;  7ABC87A51501E721 CRC64;
     MNKHQKPVLT GQRFKTRKRD EKEKFEPTVF RDTLVQGLNE AGDDLEAVAK FLDSTGSRLD
     YRRYADTLFD ILVAGSMLAP GGTRIDDGDK TKMTNHCVFS ANEDHETIRN YAQVFNKLIR
     RYKYLEKAFE DEMKKLLLFL KAFSETEQTK LAMLSGILLG NGTLPATILT SLFTDSLVKE
     GIAASFAVKL FKAWMAEKDA NSVTSSLRKA NLDKRLLELF PVNRQSVDHF AKYFTDAGLK
     ELSDFLRVQQ SLGTRKELQK ELQERLSQEC PIKEVVLYVK EEMKRNDLPE TAVIGLLWTC
     IMNAVEWNKK EELVAEQALK HLKQYAPLLA VFSSQGQSEL ILLQKVQEYC YDNIHFMKAF
     QKIVVLFYKA DVLSEEAILK WYKEAHVAKG KSVFLDQMKK FVEWLQNAEE ESESEGEGN