ID A0A060WNW1_ONCMY Unreviewed; 400 AA.
AC A0A060WNW1; A0A8C7R3B3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=mRNA decay activator protein ZFP36 {ECO:0000256|RuleBase:RU369014};
DE AltName: Full=Zinc finger protein 36 {ECO:0000256|RuleBase:RU369014};
GN ORFNames=GSONMT00051391001 {ECO:0000313|EMBL:CDQ69103.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ69103.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ69103.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ69103.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSOMYP00000047561.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Zinc-finger RNA-binding protein that destabilizes several
CC cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by
CC promoting their poly(A) tail removal or deadenylation, and hence
CC provide a mechanism for attenuating protein synthesis. Acts as a 3'-
CC untranslated region (UTR) ARE mRNA-binding adapter protein to
CC communicate signaling events to the mRNA decay machinery. Functions by
CC recruiting the CCR4-NOT deadenylase complex and probably other
CC components of the cytoplasmic RNA decay machinery to the bound ARE-
CC containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation
CC and decay processes. Binds to 3'-UTR ARE of numerous mRNAs.
CC {ECO:0000256|RuleBase:RU369014}.
CC -!- SUBUNIT: Associates with the cytoplasmic CCR4-NOT deadenylase complex
CC to trigger ARE-containing mRNA deadenylation and decay processes.
CC {ECO:0000256|RuleBase:RU369014}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369014}.
CC Cytoplasm {ECO:0000256|RuleBase:RU369014}.
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DR EMBL; FR904653; CDQ69103.1; -; Genomic_DNA.
DR STRING; 8022.A0A060WNW1; -.
DR PaxDb; 8022-A0A060WNW1; -.
DR Ensembl; ENSOMYT00000051742.2; ENSOMYP00000047561.2; ENSOMYG00000021695.2.
DR GeneTree; ENSGT00940000155076; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR Proteomes; UP000694395; Chromosome 24.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IEA:UniProtKB-UniRule.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:UniProtKB-UniRule.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR InterPro; IPR045877; ZFP36-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12547; CCCH ZINC FINGER/TIS11-RELATED; 1.
DR PANTHER; PTHR12547:SF130; MRNA DECAY ACTIVATOR PROTEIN ZFP36; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU369014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleus {ECO:0000256|RuleBase:RU369014};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW Repeat {ECO:0000256|RuleBase:RU369014};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU369014};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 137..165
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 175..203
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 137..165
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 175..203
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 111..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 43027 MW; 5F37414D99F66B54 CRC64;
MEPHLKKMPY ALNTFLDLEE VMCKQLLSLD LRDASKQSTF PVRPVGYNKP WTPCSLSASS
SALSTHSTES ATMTSSHWGQ NTEASLPSRL KMSFWAERSV SMVEPSTCTL GWASTEPKQP
PASPTGGPVS GSPTSSRYKT ELCRTFAESG ICKYGGKCQF AHGFDEMRDL NRHPRYKTEP
CRTFHTIGFC PYGIRCHFVH NNEDDLGPGP ARPGPGPQTP RTRRPPLLRQ SFSFGGFPST
PPQPLEHSLP HPFLLVPSVS PPTSADITDL LSHAFSEVGC VFEPAHELQS QFLPSPDSGC
SLCGLSPVPS PSQNPCTLSE GCSLQQSQSP PCGPALRARS LSYTSLSDHE GGCGSSASSL
SGSDSSGPDG SGRRLPIFSQ LSVPDEGFSS EFCSGTSFFL
//
