IMPCT_RAT
ID IMPCT_RAT Reviewed; 317 AA.
AC Q5GFD9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein IMPACT;
DE AltName: Full=Imprinted and ancient gene protein homolog;
GN Name=Impact;
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].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=15752730; DOI=10.1016/j.bbrc.2005.02.048;
RA Okamura K., Sakaki Y., Ito T.;
RT "Comparative genomics approach toward critical determinants for the
RT imprinting of an evolutionarily conserved gene Impact.";
RL Biochem. Biophys. Res. Commun. 329:824-830(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP 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: 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. May be required to
CC regulate translation in specific neuronal cells under amino acid
CC starvation conditions by preventing GCN2 activation and therefore ATF4
CC synthesis. Through its inhibitory action on EIF2AK4/GCN2, plays a role
CC in 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; AY574213; AAS80055.1; -; mRNA.
DR RefSeq; NP_001012235.1; NM_001012235.1.
DR AlphaFoldDB; Q5GFD9; -.
DR SMR; Q5GFD9; -.
DR BioGRID; 268970; 3.
DR IntAct; Q5GFD9; 1.
DR MINT; Q5GFD9; -.
DR STRING; 10116.ENSRNOP00000064200; -.
DR iPTMnet; Q5GFD9; -.
DR PhosphoSitePlus; Q5GFD9; -.
DR SwissPalm; Q5GFD9; -.
DR jPOST; Q5GFD9; -.
DR PaxDb; Q5GFD9; -.
DR PRIDE; Q5GFD9; -.
DR Ensembl; ENSRNOT00000116602; ENSRNOP00000078372; ENSRNOG00000045844.
DR GeneID; 497198; -.
DR KEGG; rno:497198; -.
DR CTD; 55364; -.
DR RGD; 1591977; Impact.
DR eggNOG; KOG3299; Eukaryota.
DR GeneTree; ENSGT00390000017571; -.
DR HOGENOM; CLU_045276_1_0_1; -.
DR InParanoid; Q5GFD9; -.
DR OMA; IYGEDWC; -.
DR OrthoDB; 1400092at2759; -.
DR PhylomeDB; Q5GFD9; -.
DR PRO; PR:Q5GFD9; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000045844; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q5GFD9; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0043022; F:ribosome binding; ISO:RGD.
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; ISO:RGD.
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 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Differentiation; Neurogenesis; Phosphoprotein;
KW Reference proteome; Repressor; Stress response; Translation regulation.
FT CHAIN 1..317
FT /note="Protein IMPACT"
FT /id="PRO_0000330853"
FT DOMAIN 14..116
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT REGION 117..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 317 AA; 35995 MW; 7AA2ACF198271154 CRC64;
MAEVESGSNQ RQNEEIEAMA AIYGEEWCVI DEVAKIFCIR ITDDMDDPKW TLCLQVMLPS
EYPGTAPPVY QLNAPWLKGQ ERAELAKSLE EIYMKNIGES ILYQWVEKIR DALIQKSQIT
EPGPDEKKKT EEEEVEGEDD PILEHPPENP VKTWDLKISE SAPEAEELPP IAHGAPITDR
RSTFQAHLAP VVCIDQVKKV LAKLYENKKI ASATHNIYAY RIYCEDKQTF LQDSEDDGET
AAGGRLLHLM EILNVKNVMV VVSRWYGGIL LGPDRFKHIN NCARNILVEK NFTNSPEESA
KSFGKKKVKK DKKKGDH
