ID   IMPTB_XENTR             Reviewed;         317 AA.
AC   A9UMG5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Protein IMPACT-B;
DE   AltName: Full=Imprinted and ancient gene protein homolog B;
GN   Name=impact-B;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Translational regulator that ensures constant high levels of
CC       translation upon a variety of stress conditions, such as amino acid
CC       starvation, UV-C irradiation, proteasome inhibitor treatment and
CC       glucose deprivation. Plays a role as a negative regulator of the
CC       EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated EIF2AK4/GCN2
CC       activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation
CC       and subsequent down-regulation of protein synthesis. Plays a role in
CC       differentiation of neuronal cells by stimulating neurite outgrowth.
CC       {ECO:0000250|UniProtKB:O55091}.
CC   -!- SUBUNIT: Interacts with GCN1; prevents the interaction of GCN1 with
CC       EIF2AK4/GCN2 and inhibits EIF2AK4/GCN2 kinase activity. Interaction
CC       with RPL39; this interaction occurs in a GCN1-independent manner.
CC       Associates with ribosomes; this interaction occurs in a GCN1-
CC       independent manner. Associates with actin; this interaction occurs in a
CC       GCN1-independent manner. {ECO:0000250|UniProtKB:O55091}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O55091}.
CC   -!- SIMILARITY: Belongs to the IMPACT family. {ECO:0000305}.
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DR   EMBL; BC157649; AAI57650.1; -; mRNA.
DR   AlphaFoldDB; A9UMG5; -.
DR   SMR; A9UMG5; -.
DR   InParanoid; A9UMG5; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR   GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
DR   GO; GO:0072755; P:cellular response to benomyl; ISS:UniProtKB.
DR   GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR   GO; GO:1990253; P:cellular response to leucine starvation; ISS:UniProtKB.
DR   GO; GO:0071494; P:cellular response to UV-C; ISS:UniProtKB.
DR   GO; GO:0140469; P:GCN2-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR   GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; ISS:UniProtKB.
DR   GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0071264; P:positive regulation of translational initiation in response to starvation; ISS:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; IBA:GO_Central.
DR   Gene3D; 3.10.110.10; -; 1.
DR   Gene3D; 3.30.230.30; -; 1.
DR   InterPro; IPR023582; Impact.
DR   InterPro; IPR001498; Impact_N.
DR   InterPro; IPR036956; Impact_N_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR020569; UPF0029_Impact_CS.
DR   PANTHER; PTHR16301; PTHR16301; 1.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF01205; UPF0029; 1.
DR   SMART; SM00591; RWD; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50908; RWD; 1.
DR   PROSITE; PS00910; UPF0029; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Differentiation; Neurogenesis; Reference proteome; Repressor;
KW   Stress response; Translation regulation.
FT   CHAIN           1..317
FT                   /note="Protein IMPACT-B"
FT                   /id="PRO_0000330857"
FT   DOMAIN          17..118
FT                   /note="RWD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT   REGION          296..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   317 AA;  35901 MW;  39C2BAB9A470507E CRC64;
     MDKLEDHDDN NLQSQIEEIE ALSSIYGEEW CVIDEAARVF CIRISETQQP KWTVCLQIIL
     PPDYPSSAPP IYQINAAWLR GQDRMTLSNS LEEIYVENAG ESILYLWVEK IREFLTEKSQ
     HSDGPDTCKT VMTEEGGHDC DEDDLPDISV LKLSSQSEQI FSPASDDEEL PLIKHGESIT
     DRRSTFQPHL SAVENPKQVQ RVLNKLYENK KIASATHNIY AYRIYCQEKN SVLQDCEDDG
     ETAAGGRLLH LLQILDVRNV LVVVSRWYGG ILLGPDRFKH INNCARTILI QEGYADSTEE
     TSKAGGKSKK PKSKKTK