ID A0A9J7YE99_CYPCA Unreviewed; 802 AA.
AC A0A9J7YE99;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE RecName: Full=Cold shock domain-containing protein E1 {ECO:0000256|ARBA:ARBA00069501};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000117163.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000117163.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000117163.1}
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 AlphaFoldDB; A0A9J7YE99; -.
DR Ensembl; ENSCCRT00000145415.1; ENSCCRP00000117163.1; ENSCCRG00000031544.2.
DR GeneTree; ENSGT00390000016950; -.
DR Proteomes; UP001108240; Unplaced.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:1905172; F:RISC complex binding; IEA:UniProtKB-ARBA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 8.
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:SF2; COLD SHOCK DOMAIN-CONTAINING PROTEIN E1 ISOFORM X1; 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; 5.
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:UP001108240};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 25..89
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 183..245
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 347..411
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 522..585
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 677..741
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 752..793
FT /note="SUZ-C"
FT /evidence="ECO:0000259|PROSITE:PS51938"
FT REGION 438..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 88897 MW; 23D67E1DF0A84080 CRC64;
MSFDPSLLHN NGHGGFANGT SMGIRETGVV EKLLASYGFI QCSERQARLF FHCSQYNGNL
QELKIGDDVE FEVSSDRRTG KPIAVKLVKI KAEMLPEERI SGQVVSAIPS HLDGKSAPGQ
VPTGSVCYER NGEVFYLTYT PEDVEGNVTL DTGDKVNFYM ETNKHTGAVS AHNIVLVKKK
QSRCQGVVCA TKEAFGFIER GDVVKEIFFH YSEFKGDLEA LQAGDDVEFS IKERNGKEVA
TDVRLLPQGT VIFEDISIET FEGTVTKVIP KVPTKNQNDP LPGRISARIN FTDKELLFGE
KDTKSKVTLL EGDHVQFNIS TDRRDKLERA TNIDILPDTF HFTKEAREMG VIAAMRDGFG
FIKCVDRDAR MFFHFSEVLE ESQLHISDEV EFTVVPDMLS AQRNHAVRIK KLPKGTVSFH
TQSELRFVGV VEKEAAPATT AKNSSPSKGK EKKKDKDAEE GLIAYEESGV KSTLPYYIKD
LEGGAYPQLG DKVEFSISEV KRTGQQSAVS LKILNRAVGT KRLLGYIATL KDNFGFIETA
NHDQEIFFHY SEVCGDVDNM DLGDTVEYTL SKGKGNKISA EKVTKVAAVN GVEEDESNTM
FLGKVIRPLR SVDPSQNDYQ GLIEITEEGA SKGQSYPFGI VGVANKGDCL QKGEMVKFQL
CTVAQTGQKM ACNIVPQRRA LVECVKDQFG FITYEVGESK KLFFHVKEVQ DGLELQAGDE
VEFSVILNQR TGKCSACNVR RVSEGPKPVA TPRPDRLVNR LKSITLDDTN APRLVIIRQP
RGPDNSKGFN VERKSHQPGV TD
//
