5MP1_RAT
ID 5MP1_RAT Reviewed; 419 AA.
AC Q9WTT7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
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, Hfb2;
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Fetal brain;
RX PubMed=10727730; DOI=10.1016/s0165-3806(99)00191-1;
RA Nishinaka N., Hongo S., Zhou C.J., Shioda S., Takahashi R., Yamauchi Y.,
RA Ohashi T., Ohki T., Nakada N., Takeda F., Takeda M.;
RT "Identification of the novel developmentally regulated gene, Bdm2, which is
RT highly expressed in fetal rat brain.";
RL Brain Res. Dev. Brain Res. 120:57-64(2000).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-414 AND SER-419, 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 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 -!- TISSUE SPECIFICITY: Expressed at high levels in heart, and at lower
CC levels in skeletal muscle, spleen and lung. Expressed at low levels in
CC brain regions where nascent and immature neurons are present.
CC {ECO:0000269|PubMed:10727730}.
CC -!- DEVELOPMENTAL STAGE: Expressed at E8. In brain, expression increases
CC between E14 and E16, reaches a plateau at E18, and subsequently
CC decreases. {ECO:0000269|PubMed:10727730}.
CC -!- SIMILARITY: Belongs to the BZW family. {ECO:0000305}.
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DR EMBL; AF031483; AAD20436.1; -; mRNA.
DR EMBL; BC063149; AAH63149.1; -; mRNA.
DR RefSeq; NP_599229.1; NM_134402.3.
DR AlphaFoldDB; Q9WTT7; -.
DR STRING; 10116.ENSRNOP00000007414; -.
DR iPTMnet; Q9WTT7; -.
DR PhosphoSitePlus; Q9WTT7; -.
DR jPOST; Q9WTT7; -.
DR PaxDb; Q9WTT7; -.
DR PRIDE; Q9WTT7; -.
DR Ensembl; ENSRNOT00000007414; ENSRNOP00000007414; ENSRNOG00000005096.
DR GeneID; 171439; -.
DR KEGG; rno:171439; -.
DR UCSC; RGD:621507; rat.
DR CTD; 28969; -.
DR RGD; 621507; Bzw2.
DR eggNOG; KOG2297; Eukaryota.
DR GeneTree; ENSGT00390000012561; -.
DR HOGENOM; CLU_032849_0_1_1; -.
DR InParanoid; Q9WTT7; -.
DR OMA; ELIQCIW; -.
DR OrthoDB; 653740at2759; -.
DR PhylomeDB; Q9WTT7; -.
DR TreeFam; TF324313; -.
DR PRO; PR:Q9WTT7; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005096; Expressed in heart and 20 other tissues.
DR Genevisible; Q9WTT7; RN.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Phosphoprotein; Reference proteome;
KW Translation regulation.
FT CHAIN 1..419
FT /note="eIF5-mimic protein 1"
FT /id="PRO_0000254622"
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:0007744|PubMed:22673903"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 419 AA; 48049 MW; C66FC462AA0EA773 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
VMNAVEWNKK EELVAEQALK HLKQYAPLLA VFSSQGQSEL VLLQKVQEYC YDNIHFMKAF
QKIVVLFYKA DVLSEEAILK WYKEAHAAKG KSVFLDQMKK FVEWLQNAEE ESESEGEES
