ID   5MP2_PONAB              Reviewed;         419 AA.
AC   Q5R7L4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=eIF5-mimic protein 2 {ECO:0000250|UniProtKB:Q7L1Q6};
DE   AltName: Full=Basic leucine zipper and W2 domain-containing protein 1;
GN   Name=BZW1; Synonyms=5MP2 {ECO:0000250|UniProtKB:Q7L1Q6};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Translation initiation regulator which represses repeat-
CC       associated non-AUG (RAN) initiated translation probably by acting as a
CC       competitive inhibitor of eukaryotic translation initiation factor 5
CC       (EIF5) function (By similarity). Enhances histone H4 gene transcription
CC       but does not seem to bind DNA directly (By similarity).
CC       {ECO:0000250|UniProtKB:Q7L1Q6}.
CC   -!- SIMILARITY: Belongs to the BZW family. {ECO:0000305}.
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DR   EMBL; CR860101; CAH92246.1; -; mRNA.
DR   RefSeq; NP_001126313.1; NM_001132841.1.
DR   AlphaFoldDB; Q5R7L4; -.
DR   SMR; Q5R7L4; -.
DR   STRING; 9601.ENSPPYP00000014591; -.
DR   GeneID; 100173292; -.
DR   KEGG; pon:100173292; -.
DR   CTD; 9689; -.
DR   eggNOG; KOG2297; Eukaryota.
DR   InParanoid; Q5R7L4; -.
DR   Proteomes; UP000001595; Unplaced.
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; Activator; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Translation regulation; Ubl conjugation.
FT   CHAIN           1..419
FT                   /note="eIF5-mimic protein 2"
FT                   /id="PRO_0000254611"
FT   DOMAIN          247..414
FT                   /note="W2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L1Q6"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L1Q6"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L1Q6"
FT   MOD_RES         413
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L1Q6"
FT   CROSSLNK        368
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L1Q6"
SQ   SEQUENCE   419 AA;  47899 MW;  9E4EAEEA162F5A00 CRC64;
     MNNQKQQKPT LSGQRFKTRK RDEKERFDPT QFQDCIIQGL TETGTDLEAV AKFLDASGAK
     LDYRRYAETL FDILVAGGML APGGTLADDM MRTDVCVFAA QEDLETMQAF AQVFNKLIRR
     YKYLEKGFED GVKKLLLFLK GFSESERNKL AMLTGVLLAN GTLNASILNS LYNENLVKEG
     VSAAFAVKLF KSWINEKDIN AVAASLRKVS MDNRLMELFP ANKQSVEHFT KYFTEAGLKE
     LSEYVRNQQT IGARKELQKE LQEQMSRGDP FKDIILYVKE EMKKNNIPEP VVIGIVWSSV
     MSTVEWNKKE ELVAEQAIKH LKQYSPLLAA FTTQGQSELT LLLKIQEYCY DNIHFMKAFQ
     KIVVLFYKAE VLSEGPILKW YKDAHVAKGK SVFLEQMKKF VEWLKNAEEE SESEAEEGD