ID   CSDE1_CAVPO             Reviewed;         114 AA.
AC   P29174;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Cold shock domain-containing protein E1;
DE   AltName: Full=Protein UNR;
DE   Flags: Fragment;
GN   Name=CSDE1; Synonyms=UNR;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NIH 2;
RX   PubMed=1622933;
RA   Doniger J., Landsman D., Gonda M.A., Wistow G.;
RT   "The product of unr, the highly conserved gene upstream of N-ras, contains
RT   multiple repeats similar to the cold-shock domain (CSD), a putative DNA-
RT   binding motif.";
RL   New Biol. 4:389-395(1992).
CC   -!- FUNCTION: RNA-binding protein involved in translationally coupled mRNA
CC       turnover. Implicated with other RNA-binding proteins in the cytoplasmic
CC       deadenylation/translational and decay interplay of the FOS mRNA
CC       mediated by the major coding-region determinant of instability (mCRD)
CC       domain. Required for efficient formation of stress granules.
CC       {ECO:0000250|UniProtKB:O75534}.
CC   -!- SUBUNIT: Component of a multi subunit autoregulatory ribonucleoprotein
CC       complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1.
CC       Interacts with STRAP. Part of a complex associated with the FOS mCRD
CC       domain and consisting of PABPC1, PAIP1, HNRPD and SYNCRIP. The
CC       interaction with PABPC1 is direct and RNA-independent. Interacts with
CC       EIF4ENIF1/4E-T. {ECO:0000250|UniProtKB:O75534}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75534}.
CC       Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O75534}. Cytoplasm, P-
CC       body {ECO:0000250|UniProtKB:O75534}.
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DR   EMBL; X60127; CAA42715.1; -; Genomic_DNA.
DR   PIR; A45577; A45577.
DR   AlphaFoldDB; P29174; -.
DR   SMR; P29174; -.
DR   STRING; 10141.ENSCPOP00000000471; -.
DR   eggNOG; ENOG502QSJ1; Eukaryota.
DR   HOGENOM; CLU_2126551_0_0_1; -.
DR   InParanoid; P29174; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR002059; CSP_DNA-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR024642; SUZ-C.
DR   Pfam; PF00313; CSD; 1.
DR   Pfam; PF12901; SUZ-C; 1.
DR   SMART; SM00357; CSP; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS51857; CSD_2; 1.
DR   PROSITE; PS51938; SUZ_C; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT   CHAIN           <1..114
FT                   /note="Cold shock domain-containing protein E1"
FT                   /id="PRO_0000100347"
FT   DOMAIN          <1..51
FT                   /note="CSD 9"
FT   DOMAIN          64..105
FT                   /note="SUZ-C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01287"
FT   MOD_RES         77
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O75534"
FT   NON_TER         1
SQ   SEQUENCE   114 AA;  12674 MW;  89ACED1BBF3BF287 CRC64;
     FGFINYEVGD SKKLFFHVKE VQDGIELQAG DEVEFSVILN QRTGKCSACN VWRVCEGPKA
     VAAPRPDRLV NRLKNITLDD ASAPRLMVLR QPRGPDNSMG FGAERKIRQA GVID