CSDE1_MOUSE
ID CSDE1_MOUSE Reviewed; 798 AA.
AC Q91W50;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cold shock domain-containing protein E1 {ECO:0000305};
GN Name=Csde1 {ECO:0000312|MGI:MGI:92356}; Synonyms=D3Jfr1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC016898; AAH16898.1; -; mRNA.
DR EMBL; BC062097; AAH62097.1; -; mRNA.
DR CCDS; CCDS38569.1; -.
DR RefSeq; NP_659150.1; NM_144901.4.
DR RefSeq; XP_017175039.1; XM_017319550.1.
DR AlphaFoldDB; Q91W50; -.
DR SMR; Q91W50; -.
DR BioGRID; 230878; 37.
DR ComplexPortal; CPX-1078; mCRD-poly(A)-bridging complex.
DR IntAct; Q91W50; 13.
DR MINT; Q91W50; -.
DR STRING; 10090.ENSMUSP00000029446; -.
DR iPTMnet; Q91W50; -.
DR PhosphoSitePlus; Q91W50; -.
DR SwissPalm; Q91W50; -.
DR EPD; Q91W50; -.
DR MaxQB; Q91W50; -.
DR PaxDb; Q91W50; -.
DR PRIDE; Q91W50; -.
DR ProteomicsDB; 277902; -.
DR Antibodypedia; 20164; 218 antibodies from 29 providers.
DR DNASU; 229663; -.
DR Ensembl; ENSMUST00000029446; ENSMUSP00000029446; ENSMUSG00000068823.
DR Ensembl; ENSMUST00000197827; ENSMUSP00000143503; ENSMUSG00000068823.
DR GeneID; 229663; -.
DR KEGG; mmu:229663; -.
DR UCSC; uc008qsg.2; mouse.
DR CTD; 7812; -.
DR MGI; MGI:92356; Csde1.
DR VEuPathDB; HostDB:ENSMUSG00000068823; -.
DR eggNOG; ENOG502QSJ1; Eukaryota.
DR GeneTree; ENSGT00390000016950; -.
DR InParanoid; Q91W50; -.
DR OMA; PPIMNSD; -.
DR OrthoDB; 136290at2759; -.
DR PhylomeDB; Q91W50; -.
DR TreeFam; TF324707; -.
DR BioGRID-ORCS; 229663; 9 hits in 75 CRISPR screens.
DR ChiTaRS; Csde1; mouse.
DR PRO; PR:Q91W50; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q91W50; protein.
DR Bgee; ENSMUSG00000068823; Expressed in rostral migratory stream and 261 other tissues.
DR ExpressionAtlas; Q91W50; baseline and differential.
DR Genevisible; Q91W50; MM.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0035613; F:RNA stem-loop binding; ISO:MGI.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; ISO:MGI.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISO:MGI.
DR GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
DR CDD; cd04458; CSP_CDS; 2.
DR Gene3D; 2.40.50.140; -; 6.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR024642; SUZ-C.
DR Pfam; PF00313; CSD; 5.
DR Pfam; PF12901; SUZ-C; 1.
DR SMART; SM00357; CSP; 5.
DR SUPFAM; SSF50249; SSF50249; 5.
DR PROSITE; PS00352; CSD_1; 4.
DR PROSITE; PS51857; CSD_2; 9.
DR PROSITE; PS51938; SUZ_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..798
FT /note="Cold shock domain-containing protein E1"
FT /id="PRO_0000100349"
FT DOMAIN 26..87
FT /note="CSD 1"
FT DOMAIN 136..179
FT /note="CSD 2; truncated"
FT DOMAIN 186..245
FT /note="CSD 3"
FT DOMAIN 297..337
FT /note="CSD 4; truncated"
FT DOMAIN 349..410
FT /note="CSD 5"
FT DOMAIN 447..507
FT /note="CSD 6"
FT DOMAIN 519..579
FT /note="CSD 7"
FT DOMAIN 610..670
FT /note="CSD 8"
FT DOMAIN 674..735
FT /note="CSD 9"
FT DOMAIN 748..789
FT /note="SUZ-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01287"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75534"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75534"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75534"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75534"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75534"
FT MOD_RES 761
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75534"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75534"
SQ SEQUENCE 798 AA; 88791 MW; 731065F734C60009 CRC64;
MSFDPNLLHN NGHNGYPNGT SAALRETGVI EKLLTSYGFI QCSERQARLF FHCSQYNGNL
QDLKVGDDVE FEVSSDRRTG KPIAIKLVKI KPEIHPEERM NGQVVCAVPH NLESKSPAAP
GQSPTGSVCY ERNGEVFYLT YTSEDVEGNV QLETGDKINF VIDNNKHTGA VSARNIMLLK
KKQARCQGVV CAMKEAFGFI ERGDVVKEIF FHYSEFKGDL ETLQPGDDVE FTIKDRNGKE
VATDVRLLPQ GTVIFEDISI EHFEGTVTKV IPKVPSKNQN DPLPGRIKVD FVIPKELPFG
DKDTKSKVTL LEGDHVRFNI STDRRDKLER ATNIEVLSNT FQFTNEAREM GVIAAMRDGF
GFIKCVDRDA RMFFHFSEIL DGNQLHIADE VEFTVVPDML SAQRNHAIRI KKLPKGTVSF
HSHSDHRFLG TVEKEATFSN PKTTSPNKGK DKEAEDGIIA YDDCGVKLTI AFQAKDVEGS
TSPQIGDKVE FSISDKQRPG QQIATCVRLL GRNSNSKRLL GYVATLKDNF GFIETANHDK
EIFFHYSEFS GDVDSLELGD MVEYSLSKGK GNKVSAEKVN KAHSVNGITE EANPTIYSGK
VIRPLRGVDP TQIEYQGMIE IVEEGDMKGE VYPFGIVGMA NKGDCLQKGE SVKFQLCVLG
QNAQTMAYNI TPLRRATVEC VKDQFGFINY EVGDSKKLFF HVKEVQDGVE LQAGDEVEFS
VILNQRTGKC SACNVWRVCE GPKAVAAPRP DRLVNRLKNI TLDDASAPRL MVLRQPRGPD
NSMGFGAERK IRQAGVID
