ID A0A2I3H3R2_NOMLE Unreviewed; 844 AA.
AC A0A2I3H3R2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 28-JAN-2026, entry version 41.
DE RecName: Full=Cold shock domain-containing protein E1 {ECO:0000256|ARBA:ARBA00069501};
GN Name=CSDE1 {ECO:0000313|Ensembl:ENSNLEP00000038112.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000038112.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000038112.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000038112.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSNLEP00000038112.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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; ADFV01041547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01041548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_030680651.1; XM_030824791.1.
DR AlphaFoldDB; A0A2I3H3R2; -.
DR FunCoup; A0A2I3H3R2; 2394.
DR STRING; 61853.ENSNLEP00000038112; -.
DR Ensembl; ENSNLET00000048861.1; ENSNLEP00000038112.1; ENSNLEG00000004842.2.
DR GeneID; 100590871; -.
DR CTD; 7812; -.
DR GeneTree; ENSGT00390000016950; -.
DR InParanoid; A0A2I3H3R2; -.
DR OMA; NLGACHV; -.
DR OrthoDB; 74319at2759; -.
DR Proteomes; UP000001073; Chromosome 12.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IEA:Ensembl.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; IEA:Ensembl.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0106222; F:lncRNA binding; IEA:Ensembl.
DR GO; GO:1905172; F:RISC complex binding; IEA:Ensembl.
DR GO; GO:0035613; F:RNA stem-loop binding; IEA:Ensembl.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IEA:Ensembl.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IEA:Ensembl.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IEA:Ensembl.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IEA:Ensembl.
DR GO; GO:0034063; P:stress granule assembly; IEA:Ensembl.
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; 9.
DR PROSITE; PS51938; SUZ_C; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 71..135
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 157..224
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 231..293
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 328..382
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 394..458
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 488..555
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 564..627
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 660..718
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 719..783
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 794..835
FT /note="SUZ-C"
FT /evidence="ECO:0000259|PROSITE:PS51938"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..32
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 93712 MW; F64753AE318F3371 CRC64;
MENVFTVSSD PHPSPAAPPS LSLPLSSSST SSGTKKQKRT PTYQRSMSFD PNLLHNNGHN
GYPNGTSAAL RETGVIEKLL TSYGFIQCSE RQARLFFHCS QYNGNLQDLK VGDDVEFEVS
SDRRTGKPIA VKLVKIKQEI LPEERMNGQV VCAVPHNLES KSPAAPGQSP TGSVCYERNG
EVFYLTYTPE DVEGNVQLET GDKINFVIDN NKHTGAVSAR NIMLLKKKQA RCQGVVCAMK
EAFGFIERGD VVKEIFFHYS EFKGDLETLQ PGDDVEFTIK DRNGKEVATD VRLLPQGTVI
FEDISIEHFE GTVTKVIPKV PSKNQNDPLP GRIKVDFVIP KELPFGDKDT KSKVTLLEGD
HVRFNISTDR RDKLERATNI EVLSNTFQFT NEAREMGVIA ATRDGFGFIK CVDRDVRMFF
HFSEILDGNQ LHIADEVEFT VVPDMLSAQR NHAIRIKKLP KGTVSFHSHS DHRFLGTVEK
EATFSNPKTT SPNKGKEKEA EDGIIAYDDC GVKLTIAFQA KDVEGSTSPQ IGDKVEFSIS
DKQRPGQQVA TCVRLLGRNS NSKRLLGYVA TLKDNFGFIE TANHDKEIFF HYSEFSGDVD
SLELGDMVEY SLSKGKGNKV SAEKVNKTHS VNGITEEADP TIYSGKVIRP LRSVDPTQTE
YQGMIEIVEE GDMKGEVYPF GIVGMANKGD CLQKGESVKF QLCVLGQNAQ TMAYNITPLR
RATVECVKDQ FGFINYEVGD SKKLFFHVKE VQDGIELQAG DEVEFSVILN QRTGKCSACN
VWRVCEGPKA VAAPRPDRLV NRLKNITLDD ASAPRLMVLR QPRGPDNSMG FGAERKIRQA
GVID
//
