ID W5N9A0_LEPOC Unreviewed; 358 AA.
AC W5N9A0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=mRNA decay activator protein ZFP36 {ECO:0000256|RuleBase:RU369014};
DE AltName: Full=Zinc finger protein 36 {ECO:0000256|RuleBase:RU369014};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000017209.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000017209.1}
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 EMBL; AHAT01022134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N9A0; -.
DR STRING; 7918.ENSLOCP00000017209; -.
DR Ensembl; ENSLOCT00000017240.1; ENSLOCP00000017209.1; ENSLOCG00000013957.1.
DR eggNOG; KOG1677; Eukaryota.
DR GeneTree; ENSGT00940000155076; -.
DR InParanoid; W5N9A0; -.
DR OMA; TPYFFRP; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000013957; Expressed in zone of skin and 13 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:SF53; MRNA DECAY ACTIVATOR PROTEIN ZFP36L1; 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:UP000018468};
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 140..168
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 178..206
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 140..168
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 178..206
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 37..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 39294 MW; 2B48C9571B3EC352 CRC64;
SVSLQTLHVL VNRKLFLFQN NKMMNYNNNI LTAPHPSSVP CTGPSPPIST PSGPLLDRKA
VGTPSSSVGV YQRRHSVTLP NSKFNQNQFI NNSLKVEPSS TGGSSNKENR FRDRSYSETG
DRLLPKSAGG NGSGQVNSSR YKTELCRPFE ENGVCKYGDK CQFAHGIHEL RSLSRHPKYK
TELCRTFHTI GFCPYGPRCH FIHNAEERRG PPPLSASNKL DRPRLQHSFS FAGFPSNNGL
QDSPTSVTPP PIFHADDLQD WPSNPFTYSS QELASLFGPS LGSQADPSAP APPSPTTFFF
RAMSESPQLF ESPPSPQDSL SDQEGYQSSS GSLSGSESPV LDTTRRLPIF SRLSISDD
//
