ID A0A8B9IWE6_9PSIT Unreviewed; 771 AA.
AC A0A8B9IWE6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Cold shock domain-containing protein E1 {ECO:0000256|ARBA:ARBA00069501};
OS Amazona collaria (yellow-billed parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=241587 {ECO:0000313|Ensembl:ENSACOP00000010376.1, ECO:0000313|Proteomes:UP000694522};
RN [1] {ECO:0000313|Ensembl:ENSACOP00000010376.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSACOP00000010376.1}
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; A0A8B9IWE6; -.
DR Ensembl; ENSACOT00000010741.1; ENSACOP00000010376.1; ENSACOG00000007230.1.
DR Proteomes; UP000694522; 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; 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; 6.
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:UP000694522};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 31..95
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 160..222
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 323..387
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 491..554
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 587..645
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 646..710
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 721..762
FT /note="SUZ-C"
FT /evidence="ECO:0000259|PROSITE:PS51938"
SQ SEQUENCE 771 AA; 86183 MW; 84D5853F9A52A7DC CRC64;
MFSFNQMSFD PNLLHNNGHN GYPNGTSAAL RETGVIEKLL TSYGFIQCSE RQARLFFHCS
QYNGNLQELK VGDDVEFEVS SDRRTGKPIA IKLVKIKPEI LPEERINGQE VFYLTYTPED
VEGNVQLETG DKINFIIDTN KHTGAVSARN IMLLKKKQAR CQGVVCAMKE AFGFIERGDV
VKEIFFHYSE FKGDLEALQP GDDVEFTIKD RNGKEVATDV RLLPQGTVIF EDISIEHFEG
TVTKVIPKVP SKNQSDPLPG RIKVDFVIPK ELPFGDKDTK SKVTLLESDH VRFNISTDRR
DKLERATNIE VLPNTFQFTN ETREMGVIAA MRDGFGFIKC VDRDARMFFH FSEIMDGNQL
HISDEVEFTV VPDMLSAQRN HAIRIKKLPK GTVSFHTQSD HRFVGTIDKE ATPAKATSPN
KGKEKEAEDG IIVYDDCGVK LTIPYQAKDV EGSANPQIGD KVEFCVCEVK RTGLQTAVSV
RMLGRNYSSK RLLGYVAALK DNFGFIETAN HDKEIFFHYS EYCGDIDSLE LGDTVEYSLS
KGKGNKVSAE KVNKTHAVNG MTEEADPTVY SGKVIRPLRS VDPTQTEYQG MIEVMEDGEM
KGEVYPFGIV GMANKGDCLQ KGETVKFQLC VLGQNGQTMA VNITPFRRAT VECVKDQFGF
INYEVGDSKK LFFHVKEVQD GVELQAGDEV EFSVILNQRT GKCSACNVWR VCEGAKAVAA
PRPDRLVNRL KSINLDDANA PRLTVVRQPR GPDNSKGFGA ERKIRQAGVI D
//
