IMPCT_XENLA
ID IMPCT_XENLA Reviewed; 312 AA.
AC Q9W625; Q4KLB3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Protein IMPACT;
DE AltName: Full=Imprinted and ancient gene protein homolog;
DE AltName: Full=Ximpact;
GN Name=impact;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], LACK OF IMPRINTING, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10066441; DOI=10.1006/bbrc.1999.0297;
RA Yamada Y., Hagiwara Y., Shiokawa K., Sakaki Y., Ito T.;
RT "Spatiotemporal, allelic, and enforced expression of Ximpact, the Xenopus
RT homolog of mouse imprinted gene impact.";
RL Biochem. Biophys. Res. Commun. 256:162-169(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2005) 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 -!- TISSUE SPECIFICITY: Ubiquitous both in embryo and adult.
CC {ECO:0000269|PubMed:10066441}.
CC -!- DEVELOPMENTAL STAGE: Present in oocytes as well as in early embryos.
CC {ECO:0000269|PubMed:10066441}.
CC -!- MISCELLANEOUS: In contrast to the mouse or rabbit ortholog, the IMPACT
CC locus is not imprinted in Xenopus.
CC -!- SIMILARITY: Belongs to the IMPACT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH99309.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB020319; BAA76409.1; -; mRNA.
DR EMBL; BC099309; AAH99309.1; ALT_INIT; mRNA.
DR RefSeq; NP_001079068.1; NM_001085599.1.
DR AlphaFoldDB; Q9W625; -.
DR SMR; Q9W625; -.
DR BioGRID; 96821; 1.
DR IntAct; Q9W625; 1.
DR GeneID; 373600; -.
DR KEGG; xla:373600; -.
DR CTD; 373600; -.
DR Xenbase; XB-GENE-947996; impact.L.
DR OrthoDB; 1400092at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 373600; Expressed in muscle tissue and 19 other tissues.
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 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 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.
PE 2: Evidence at transcript level;
KW Cytoplasm; Differentiation; Neurogenesis; Reference proteome; Repressor;
KW Stress response; Translation regulation.
FT CHAIN 1..312
FT /note="Protein IMPACT"
FT /id="PRO_0000330855"
FT DOMAIN 14..116
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 35640 MW; DB50881A938DB3F4 CRC64;
MADTEEENVQ RQIDEVEALT SIYGDEWCVI DEAERIFCIT ISDSSNKPTW TLCLQVILPP
DYPVASPPLY QLNAPWLRGE DRLTLSNCLE EMYLQNLGEN ILYQWVEKIR EFLVEKSQTS
DPGPSLKSTS EETDVGDDCE VSTDELTESF KNSMIFGMNY SSGVEEIPPI VHGETISDRR
STFQAHLAPV VSPYQVKLIL NKLYENKKIA TATHNIYAYR IYIKERNSFI QDCEDDGETA
AGKRMLHLMQ ILDARDVMVV VSRWYGGILL GPDRFKHINN CARNVLMEHN YCSTVEESSK
QTSKSKKSSQ RK
