ID   IMPCT_DICDI             Reviewed;         345 AA.
AC   Q54JW9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Protein IMPACT homolog;
GN   Name=impact; ORFNames=DDB_G0287757;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Translational regulator that ensures constant high levels of
CC       translation under amino acid starvation. Plays a role as a negative
CC       regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated
CC       EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha
CC       phosphorylation and subsequent down-regulation of protein synthesis.
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; AAFI02000104; EAL63525.1; -; Genomic_DNA.
DR   RefSeq; XP_637033.1; XM_631941.1.
DR   AlphaFoldDB; Q54JW9; -.
DR   STRING; 44689.DDB0302508; -.
DR   PaxDb; Q54JW9; -.
DR   PRIDE; Q54JW9; -.
DR   EnsemblProtists; EAL63525; EAL63525; DDB_G0287757.
DR   GeneID; 8626287; -.
DR   KEGG; ddi:DDB_G0287757; -.
DR   dictyBase; DDB_G0287757; -.
DR   eggNOG; KOG3299; Eukaryota.
DR   HOGENOM; CLU_805176_0_0_1; -.
DR   InParanoid; Q54JW9; -.
DR   OMA; RHICNLA; -.
DR   PhylomeDB; Q54JW9; -.
DR   PRO; PR:Q54JW9; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR   GO; GO:0060548; P:negative regulation of cell death; 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   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   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Repressor; Stress response;
KW   Translation regulation.
FT   CHAIN           1..345
FT                   /note="Protein IMPACT homolog"
FT                   /id="PRO_0000330859"
FT   DOMAIN          7..155
FT                   /note="RWD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT   REGION          191..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   345 AA;  40338 MW;  7314109C15EF5773 CRC64;
     MNEEQENEIL AISSIYPDSF SEIETIVGEE ENDGFEDNDS QYSKIYQVII TPNISCLDEN
     SLEDNNNSNN NNNNNNNNNN NGLIIDTSYD YLIYFKFKYT KEYPSNEPPI ISIKATWLQK
     SDQSILLSHL EDLWNQNELV IFQMISWLQE ESIEILNNHY KSIKKFSHYH LKKSLNTQQL
     NQNQNQFENQ NQNQNQNQNQ NQNKEKEKEK VPTIYTGQSV TEKKSKFQAH LAIVHSEREV
     QLVLNQLLSF KKIYEATHNM YAYRFQLENG EINEYYNDDG EDGAGDKMLF TLSKNQAKEI
     LIVCTRWFGG ILLGGRRYVH IVNTTKDILN LYNTNSLSQC SLEFN