ID   Q80TP8_MOUSE            Unreviewed;       822 AA.
AC   Q80TP8;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   02-SEP-2026, entry version 120.
DE   RecName: Full=Cold shock domain-containing protein E1 {ECO:0000256|ARBA:ARBA00069501};
DE   Flags: Fragment;
GN   Name=Csde1 {ECO:0000313|MGI:MGI:92356};
GN   Synonyms=D3Jfr1 {ECO:0000313|MGI:MGI:92356}, mKIAA0885
GN   {ECO:0000313|EMBL:BAC65675.1};
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 {ECO:0000313|EMBL:BAC65675.1};
RN   [1] {ECO:0000313|EMBL:BAC65675.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAC65675.1};
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
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:0000256|ARBA:ARBA00057277}.
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:0000256|ARBA:ARBA00065656}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}. Cytoplasm, Stress granule
CC       {ECO:0000256|ARBA:ARBA00004210}.
CC   -!- SIMILARITY: Belongs to the UNR family. {ECO:0000256|ARBA:ARBA00044751}.
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DR   EMBL; AK122393; BAC65675.1; -; mRNA.
DR   AlphaFoldDB; Q80TP8; -.
DR   PeptideAtlas; Q80TP8; -.
DR   AGR; MGI:92356; -.
DR   MGI; MGI:92356; Csde1.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:1905172; F:RISC complex binding; IEA:UniProtKB-ARBA.
DR   CDD; cd04458; CSP_CDS; 2.
DR   FunFam; 2.40.50.140:FF:000055; Cold shock domain containing E1, RNA-binding; 1.
DR   FunFam; 2.40.50.140:FF:000088; cold shock domain-containing protein E1 isoform X1; 1.
DR   FunFam; 2.40.50.140:FF:000093; cold shock domain-containing protein E1 isoform X1; 1.
DR   FunFam; 2.40.50.140:FF:000094; cold shock domain-containing protein E1 isoform X1; 1.
DR   FunFam; 2.40.50.140:FF:000133; cold shock domain-containing protein E1 isoform X1; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 6.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR019844; CSD_CS.
DR   InterPro; IPR056400; CSDE1.
DR   InterPro; IPR002059; CSP_DNA-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR024642; SUZ-C.
DR   PANTHER; PTHR12913:SF1; COLD SHOCK DOMAIN-CONTAINING PROTEIN E1; 1.
DR   PANTHER; PTHR12913; UNR PROTEIN N-RAS UPSTREAM GENE PROTEIN; 1.
DR   Pfam; PF00313; CSD; 5.
DR   Pfam; PF23456; CSDE1; 4.
DR   Pfam; PF12901; SUZ-C; 1.
DR   SMART; SM00357; CSP; 5.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 5.
DR   PROSITE; PS00352; CSD_1; 4.
DR   PROSITE; PS51857; CSD_2; 8.
DR   PROSITE; PS51938; SUZ_C; 1.
PE   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..144
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          209..271
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          306..360
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          372..436
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          466..533
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          542..605
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          638..696
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          697..761
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   DOMAIN          772..813
FT                   /note="SUZ-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51938"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAC65675.1"
SQ   SEQUENCE   822 AA;  92143 MW;  A07E06DEF0F7649F CRC64;
     LGRSFPLALL FFFFFSFSFF FLFLNTSNFH PLELVLKKEE SANTTESAIF DYHCEMSFDP
     NLLHNNGHNG YPNGTSAALR ETGVIEKLLT SYGFIQCSER QARLFFHCSQ YNGNLQDLKV
     GDDVEFEVSS DRRTGKPIAI KLVKIKPEIH PEERMNGQEV FYLTYTSEDV EGNVQLETGD
     KINFVIDNNK HTGAVSARNI MLLKKKQARC QGVVCAMKEA FGFIERGDVV KEIFFHYSEF
     KGDLETLQPG DDVEFTIKDR NGKEVATDVR LLPQGTVIFE DISIEHFEGT VTKVIPKVPS
     KNQNDPLPGR IKVDFVIPKE LPFGDKDTKS KVTLLEGDHV RFNISTDRRD KLERATNIEV
     LSNTFQFTNE AREMGVIAAM RDGFGFIKCV DRDARMFFHF SEILDGNQLH IADEVEFTVV
     PDMLSAQRNH AIRIKKLPKG TVSFHSHSDH RFLGTVEKEA TFSNPKTTSP NKGKDKEAED
     GIIAYDDCGV KLTIAFQAKD VEGSTSPQIG DKVEFSISDK QRPGQQIATC VRLLGRNSNS
     KRLLGYVATL KDNFGFIETA NHDKEIFFHY SEFSGDVDSL ELGDMVEYSL SKGKGNKVSA
     EKVNKAHSVN GITEEANPTI YSGKVIRPLR GVDPTQIEYQ GMIEIVEEGD MKGEVYPFGI
     VGMANKGDCL QKGESVKFQL CVLGQNAQTM AYNITPLRRA TVECVKDQFG FINYEVGDSK
     KLFFHVKEVQ DGVELQAGDE VEFSVILNQR TGKCSACNVW RVCEGPKAVA APRPDRLVNR
     LKNITLDDAS APRLMVLRQP RGPDNSMGFG AERKIRQAGV ID
//