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Database: UniProt
Entry: A0A3Q1BSC6_AMPOC
LinkDB: A0A3Q1BSC6_AMPOC
Original site: A0A3Q1BSC6_AMPOC 
ID   A0A3Q1BSC6_AMPOC        Unreviewed;       309 AA.
AC   A0A3Q1BSC6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-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   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000017572.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000017572.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   AlphaFoldDB; A0A3Q1BSC6; -.
DR   STRING; 80972.ENSAOCP00000017572; -.
DR   Ensembl; ENSAOCT00000026887.1; ENSAOCP00000017572.1; ENSAOCG00000001644.1.
DR   GeneTree; ENSGT00940000166499; -.
DR   OMA; FGTRCNF; -.
DR   OrthoDB; 23913at2759; -.
DR   Proteomes; UP000257160; Unplaced.
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; 4.
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:SF18; PROTEIN TIS11; 1.
DR   Pfam; PF00642; zf-CCCH; 3.
DR   Pfam; PF14608; zf-CCCH_2; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; CCCH zinc finger; 4.
DR   PROSITE; PS50103; ZF_C3H1; 4.
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:UP000257160};
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          63..91
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          101..129
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          137..165
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          195..223
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         63..91
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         101..129
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         137..165
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         195..223
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          227..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   309 AA;  34159 MW;  A005757E4EFB8E5E CRC64;
     MLETSSDDLF LPSSQDEELV DNLLSSEESD VHSDGGSLSL AKALLPLAET SSPPLIPWVC
     STRYKTELCT SYSASGFCKY AERCQFAHGL HELHVPFRHP KYKTELCRSY HTTGYCYYGS
     RCLFVHNPTE QRPTLRRRRN VACRTFRSFG VCPFGSRCNF LHVEGGGVGS SVEVNEEKTA
     PAPSCQLQPP TKEWKPRGVL CRTFSSFGFC LYGTRCHFQH VLPNKLKTSN QNQSSPGSSG
     LPSSTSPKSS TSSSPSSTSP LATPSSDATA HNAFTFSSEH LNDLLLPLAL HLQQLEHTKA
     QEMWDNRGL
//
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