ID   IMPCT_BOVIN             Reviewed;         318 AA.
AC   A7YY45; Q52UL6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Protein IMPACT;
DE   AltName: Full=Imprinted and ancient gene protein homolog;
GN   Name=IMPACT;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 31-212 (ISOFORM 1).
RA   Ruddock N.T., Wilson K.J., French A.J., Holland M.K.;
RT   "Putative imprinted gene expression during bovine early embryo
RT   development.";
RL   Submitted (FEB-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. 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A7YY45-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A7YY45-2; Sequence=VSP_033135;
CC   -!- SIMILARITY: Belongs to the IMPACT family. {ECO:0000305}.
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DR   EMBL; BC151281; AAI51282.1; -; mRNA.
DR   EMBL; AY948549; AAX86795.1; -; mRNA.
DR   RefSeq; NP_001095971.1; NM_001102501.1. [A7YY45-2]
DR   RefSeq; XP_005224148.2; XM_005224091.3.
DR   AlphaFoldDB; A7YY45; -.
DR   SMR; A7YY45; -.
DR   STRING; 9913.ENSBTAP00000045263; -.
DR   PaxDb; A7YY45; -.
DR   PRIDE; A7YY45; -.
DR   GeneID; 517248; -.
DR   KEGG; bta:517248; -.
DR   CTD; 55364; -.
DR   eggNOG; KOG3299; Eukaryota.
DR   HOGENOM; CLU_045276_1_0_1; -.
DR   InParanoid; A7YY45; -.
DR   OrthoDB; 1400092at2759; -.
DR   TreeFam; TF314823; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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   Actin-binding; Alternative splicing; Cytoplasm; Differentiation;
KW   Neurogenesis; Phosphoprotein; Reference proteome; Repressor;
KW   Stress response; Translation regulation.
FT   CHAIN           1..318
FT                   /note="Protein IMPACT"
FT                   /id="PRO_0000330849"
FT   DOMAIN          14..116
FT                   /note="RWD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT   REGION          294..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5GFD9"
FT   VAR_SEQ         163..177
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_033135"
SQ   SEQUENCE   318 AA;  36333 MW;  6D2138ED954E3D04 CRC64;
     MAEGDTGSDQ RQNEEIEAMA AIYGEEWCVI DDCAKIFCIR ISDDIDDPKW TLCLQVMLPN
     EYPGTAPPIY QLNAPWLKGQ ERADLSNSLE EIYIQNIGES ILYLWVEKIR DVLIQKSQMT
     EPGPDVKKKT EEEDVECEDD LVLACQPENQ VKTLDFDVSE NRTEIEELPP IDHGIPITDR
     RSTFQAHLAP VVCPKQVKMV LAKLYENKKI ASATHNIYAY RIYCEDKQTF LQDCEDDGET
     AAGGRLLHLM EILNVRDVMV VVSRWYGGVL LGPDRFKHIN NCARNILVEK NYTNSPEESS
     KALGKNKKVR KDKKRSEH