ID   5MP2_RAT                Reviewed;         419 AA.
AC   Q6P7P5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-413, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; BC061580; AAH61580.1; -; mRNA.
DR   RefSeq; NP_942084.1; NM_198789.2.
DR   AlphaFoldDB; Q6P7P5; -.
DR   SMR; Q6P7P5; -.
DR   STRING; 10116.ENSRNOP00000019486; -.
DR   iPTMnet; Q6P7P5; -.
DR   PhosphoSitePlus; Q6P7P5; -.
DR   jPOST; Q6P7P5; -.
DR   PaxDb; Q6P7P5; -.
DR   PRIDE; Q6P7P5; -.
DR   Ensembl; ENSRNOT00000019486; ENSRNOP00000019486; ENSRNOG00000013977.
DR   GeneID; 363232; -.
DR   KEGG; rno:363232; -.
DR   UCSC; RGD:735129; rat.
DR   CTD; 9689; -.
DR   RGD; 735129; Bzw1.
DR   eggNOG; KOG2297; Eukaryota.
DR   GeneTree; ENSGT00390000012561; -.
DR   HOGENOM; CLU_032849_0_1_1; -.
DR   InParanoid; Q6P7P5; -.
DR   OMA; KDAHMAK; -.
DR   OrthoDB; 653740at2759; -.
DR   PhylomeDB; Q6P7P5; -.
DR   TreeFam; TF324313; -.
DR   PRO; PR:Q6P7P5; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000013977; Expressed in quadriceps femoris and 19 other tissues.
DR   Genevisible; Q6P7P5; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
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   1: Evidence at protein 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_0000254612"
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:0007744|PubMed:22673903"
FT   MOD_RES         413
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
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;  48043 MW;  9E952D52F5796F60 CRC64;
     MNNQKQQKPT LSGQRFKTRK RDEKERFDPT QFQDCIIQGL TETGTDLEAV AKFLDASGAK
     LDYRRYAETL FDILVAGGML APGGTLADDM MRTDVCVFAA QEDLETMQAF AQVFNKLIRR
     YKYLEKGFED EVKKLLLFLK GFSESERNKL AMLTGVLLAN GTLNASILNS LYNENLVKEG
     VSAAFAVKLF KSWINEKDIN AVAASLRKVS MDNRLMELFP ANKQSVEHFT KYFTEAGLKE
     LSEYVRNQQT IGARKELQKE LQEQMSRGDP FKDIILYVKE EMKKNNIPEP VVIGIVWSSV
     MSTVEWNKKE ELVAEQAIKH LKQYSPLLAA FTTQGQSELT LLLKIQEYCY DNIHFMKAFQ
     KIVVLFYKAE VLSEEPILKW YKDAHVAKGK SVFLEQMKKF VEWLKNAEEE SESEAEEGD