IMPCT_MOUSE
ID IMPCT_MOUSE Reviewed; 318 AA.
AC O55091; Q3UUR6; Q9EQH0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein IMPACT;
DE AltName: Full=Imprinted and ancient gene protein;
GN Name=Impact;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IMPRINTING, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=9256468; DOI=10.1073/pnas.94.17.9249;
RA Hagiwara Y., Hirai M., Nishiyama K., Kanazawa I., Ueda T., Sakaki Y.,
RA Ito T.;
RT "Screening for imprinted genes by allelic message display: identification
RT of a paternally expressed gene impact on mouse chromosome 18.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9249-9254(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IMPRINTING.
RC STRAIN=129/Sv;
RX PubMed=11116084; DOI=10.1101/gr.139200;
RA Okamura K., Hagiwara-Takeuchi Y., Li T., Vu T.H., Hirai M., Hattori M.,
RA Sakaki Y., Hoffman A.R., Ito T.;
RT "Comparative genome analysis of the mouse imprinted gene impact and its
RT nonimprinted human homolog IMPACT: toward the structural basis for species-
RT specific imprinting.";
RL Genome Res. 10:1878-1889(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-305.
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP IMPRINTING.
RX PubMed=15871461; DOI=10.1093/dnares/11.6.381;
RA Okamura K., Yamada Y., Sakaki Y., Ito T.;
RT "An evolutionary scenario for genomic imprinting of Impact lying between
RT nonimprinted neighbors.";
RL DNA Res. 11:381-390(2004).
RN [6]
RP FUNCTION, INTERACTION WITH GCN1, AND TISSUE SPECIFICITY.
RX PubMed=15937339; DOI=10.1074/jbc.m408571200;
RA Pereira C.M., Sattlegger E., Jiang H.-Y., Longo B.M., Jaqueta C.B.,
RA Hinnebusch A.G., Wek R.C., Mello L.E.A.M., Castilho B.A.;
RT "IMPACT, a protein preferentially expressed in the mouse brain, binds GCN1
RT and inhibits GCN2 activation.";
RL J. Biol. Chem. 280:28316-28323(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=18260151; DOI=10.1002/cne.21652;
RA Bittencourt S., Pereira C.M., Avedissian M., Delamano A., Mello L.E.A.M.,
RA Castilho B.A.;
RT "Distribution of the protein IMPACT, an inhibitor of GCN2, in the mouse,
RT rat, and marmoset brain.";
RL J. Comp. Neurol. 507:1811-1830(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH GCN1 AND RPL39, AND ASSOCIATION WITH ACTIN AND RIBOSOMES.
RX PubMed=22404850; DOI=10.1111/j.1742-4658.2012.08553.x;
RA Waller T., Lee S.J., Sattlegger E.;
RT "Evidence that Yih1 resides in a complex with ribosomes.";
RL FEBS J. 279:1761-1776(2012).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=23447528; DOI=10.1074/jbc.m113.461970;
RA Roffe M., Hajj G.N., Azevedo H.F., Alves V.S., Castilho B.A.;
RT "IMPACT is a developmentally regulated protein in neurons that opposes the
RT eukaryotic initiation factor 2alpha kinase GCN2 in the modulation of
RT neurite outgrowth.";
RL J. Biol. Chem. 288:10860-10869(2013).
RN [12]
RP FUNCTION.
RX PubMed=24333428; DOI=10.1016/j.bbrc.2013.12.021;
RA Cambiaghi T.D., Pereira C.M., Shanmugam R., Bolech M., Wek R.C.,
RA Sattlegger E., Castilho B.A.;
RT "Evolutionarily conserved IMPACT impairs various stress responses that
RT require GCN1 for activating the eIF2 kinase GCN2.";
RL Biochem. Biophys. Res. Commun. 443:592-597(2014).
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 (PubMed:15937339,
CC PubMed:23447528, PubMed:24333428). May be required to regulate
CC translation in specific neuronal cells under amino acid starvation
CC conditions by preventing GCN2 activation and therefore ATF4 synthesis
CC (PubMed:15937339, PubMed:23447528). Through its inhibitory action on
CC EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by
CC stimulating neurite outgrowth (PubMed:23447528).
CC {ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:23447528,
CC ECO:0000269|PubMed:24333428}.
CC -!- SUBUNIT: Interacts with GCN1; prevents the interaction of GCN1 with
CC EIF2AK4/GCN2 and inhibits EIF2AK4/GCN2 kinase activity
CC (PubMed:15937339, PubMed:22404850). Interaction with RPL39; this
CC interaction occurs in a GCN1-independent manner (PubMed:22404850).
CC Associates with ribosomes; this interaction occurs in a GCN1-
CC independent manner (PubMed:22404850). Associates with actin; this
CC interaction occurs in a GCN1-independent manner (PubMed:22404850).
CC {ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:22404850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23447528}.
CC -!- TISSUE SPECIFICITY: Present in neurons in most areas of the brain.
CC Present at high level in hypothalamus, particularly in the
CC suprachiasmatic nucleus (at protein level) (PubMed:15937339,
CC PubMed:18260151). Preferentially expressed in brain, with a weaker
CC expression in other tissues (PubMed:9256468).
CC {ECO:0000269|PubMed:15937339, ECO:0000269|PubMed:18260151,
CC ECO:0000269|PubMed:9256468}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos at 7, 11, 15, and 17 dpc. At
CC 16 dpc, predominantly expressed in the central nervous system (at
CC protein level). Strongly up-regulated during brain development from 17
CC dpc up to at least postnatal days 14 (at protein level). In N2a
CC neuroblastoma cell line model and in primary cultures of hippocampal
CC neurons, up-regulated during neuronal differentiation induced by serum
CC reduction (at protein level). {ECO:0000269|PubMed:23447528,
CC ECO:0000269|PubMed:9256468}.
CC -!- INDUCTION: Up-regulated after serum withdrawal during neuronal
CC differentiation (PubMed:23447528). {ECO:0000269|PubMed:23447528}.
CC -!- MISCELLANEOUS: The Impact locus is imprinted. Paternal inherited gene
CC is expressed, while the maternal inherited gene is silenced. In
CC contrast with most imprinted genes, neighboring genes are apparently
CC not imprinted.
CC -!- SIMILARITY: Belongs to the IMPACT family. {ECO:0000305}.
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DR EMBL; D87973; BAA35139.1; -; mRNA.
DR EMBL; AF232228; AAG23916.1; -; Genomic_DNA.
DR EMBL; BC020524; AAH20524.1; -; mRNA.
DR EMBL; AK138136; BAE23558.1; -; mRNA.
DR CCDS; CCDS29068.1; -.
DR RefSeq; NP_032404.1; NM_008378.2.
DR AlphaFoldDB; O55091; -.
DR SMR; O55091; -.
DR BioGRID; 200653; 8.
DR IntAct; O55091; 2.
DR MINT; O55091; -.
DR STRING; 10090.ENSMUSP00000025290; -.
DR iPTMnet; O55091; -.
DR PhosphoSitePlus; O55091; -.
DR EPD; O55091; -.
DR jPOST; O55091; -.
DR MaxQB; O55091; -.
DR PaxDb; O55091; -.
DR PeptideAtlas; O55091; -.
DR PRIDE; O55091; -.
DR ProteomicsDB; 301651; -.
DR Antibodypedia; 22092; 122 antibodies from 19 providers.
DR DNASU; 16210; -.
DR Ensembl; ENSMUST00000025290; ENSMUSP00000025290; ENSMUSG00000024423.
DR GeneID; 16210; -.
DR KEGG; mmu:16210; -.
DR UCSC; uc008eda.1; mouse.
DR CTD; 55364; -.
DR MGI; MGI:1098233; Impact.
DR VEuPathDB; HostDB:ENSMUSG00000024423; -.
DR eggNOG; KOG3299; Eukaryota.
DR GeneTree; ENSGT00390000017571; -.
DR HOGENOM; CLU_045276_1_0_1; -.
DR InParanoid; O55091; -.
DR OMA; IYGEDWC; -.
DR OrthoDB; 1400092at2759; -.
DR PhylomeDB; O55091; -.
DR TreeFam; TF314823; -.
DR BioGRID-ORCS; 16210; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Impact; mouse.
DR PRO; PR:O55091; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; O55091; protein.
DR Bgee; ENSMUSG00000024423; Expressed in paraventricular nucleus of hypothalamus and 253 other tissues.
DR ExpressionAtlas; O55091; baseline and differential.
DR Genevisible; O55091; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005844; C:polysome; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
DR GO; GO:0072755; P:cellular response to benomyl; IDA:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:1990253; P:cellular response to leucine starvation; IDA:UniProtKB.
DR GO; GO:0071494; P:cellular response to UV-C; IDA:UniProtKB.
DR GO; GO:0140469; P:GCN2-mediated signaling; IMP:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:UniProtKB.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; IDA:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; IMP:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:UniProtKB.
DR GO; GO:0071264; P:positive regulation of translational initiation in response to starvation; IMP:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:MGI.
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..318
FT /note="Protein IMPACT"
FT /id="PRO_0000330851"
FT DOMAIN 14..116
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT REGION 297..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 303
FT /note="N -> S (in Ref. 2; AAG23916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36276 MW; F3A3688D87C88A40 CRC64;
MAEEEVGNSQ RQSEEIEAMA AIYGEEWCVI DENAKIFCIR VTDFMDDPKW TLCLQVMLPS
EYPGTAPPSY QLNAPWLKGQ ERADLSNSLE EIYVHNMGES ILYQWVEKIR DALIQKSQIT
EPDPDVKKKT EEVEVESEED PILEHPPENP VKTLDLKISE ETQPETEELP PVAHGVPITD
RRSTFQAHVA PVVCPEQVKL VLAKLYENKK IASATHNIYA YRIFCEDKQT FLQDCEDDGE
TAAGGRLLHL MEILNVKNVM VVVSRWYGGI LLGPDRFKHI NNCARNILVE KNFTNTPDES
TKNLGKKKVK KDKKKNDH
