ID A0A3P9A5Z4_ESOLU Unreviewed; 425 AA.
AC A0A3P9A5Z4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=mRNA decay activator protein ZFP36 {ECO:0000256|RuleBase:RU369014};
DE AltName: Full=Zinc finger protein 36 {ECO:0000256|RuleBase:RU369014};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000036600.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000036600.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000036600.1}
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 RefSeq; XP_010901799.1; XM_010903497.3.
DR AlphaFoldDB; A0A3P9A5Z4; -.
DR STRING; 8010.ENSELUP00000036600; -.
DR Ensembl; ENSELUT00000025350.2; ENSELUP00000036600.1; ENSELUG00000000600.2.
DR GeneID; 105029926; -.
DR KEGG; els:105029926; -.
DR GeneTree; ENSGT00940000161584; -.
DR InParanoid; A0A3P9A5Z4; -.
DR OMA; AFYDMDM; -.
DR OrthoDB; 23913at2759; -.
DR Proteomes; UP000265140; LG06.
DR Bgee; ENSELUG00000000600; Expressed in pharyngeal gill and 15 other cell types or tissues.
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; IPR007635; Tis11B_N.
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:SF173; MRNA DECAY ACTIVATOR PROTEIN ZFP36L2; 1.
DR Pfam; PF04553; Tis11B_N; 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 Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleus {ECO:0000256|RuleBase:RU369014};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Repeat {ECO:0000256|RuleBase:RU369014};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW 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 142..170
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 180..208
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 142..170
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 180..208
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 117..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47306 MW; DEFB973C5BDFA5E2 CRC64;
MRELLRQKTS EKEMSGTILS AFYDIDMLYK QDKSMNMNAM NHINSMLDKK AVGAPVQSSN
SCSFAPGFLR RNSTSNMEAM TNNSNKYSNS YSNFKENTTS STTAIMNKEN KFRDRAYSEN
GDRSQQLQIL QQKPGSQINS TRYKTELCRP FEENGACKYG EKCQFAHGYH ELRNLSRHPK
YKTEPCRTFH TIGFCPYGPR CHFIHNADER RPAPSNANMQ GEPKSARELC GYGQMDVVPQ
QGGYTRDRPK LHHSLSFSGF SSHHGLESPL LESPTSRTPP PPSSSSSCSP NYYEDILSPN
SMSCVNSAFN FPGQDLKDLL APLAVHTQNC YGNNQFNGAY YGNIQANMCP PSPPSYNMSH
LQSLRRLNES PVFDSPPSPP DSLSDRESYA SGSLSSSGSL SGSESPSLDA GKRLPIFSRL
SISDD
//