ID A0A0U2Q2B5_MESAU Unreviewed; 502 AA.
AC A0A0U2Q2B5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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 Name=LOC101825196 {ECO:0000313|RefSeq:XP_005087909.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|EMBL:ALS88222.1};
RN [1] {ECO:0000313|EMBL:ALS88222.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Placenta {ECO:0000313|EMBL:ALS88222.1};
RX PubMed=26493225; DOI=10.1016/j.ympev.2015.10.016;
RA Gingerich T.J., Stumpo D.J., Lai W.S., Randall T.A., Steppan S.J.,
RA Blackshear P.J.;
RT "Emergence and evolution of Zfp36l3.";
RL Mol. Phylogenet. Evol. 94:518-530(2016).
RN [2] {ECO:0000313|RefSeq:XP_005087909.1}
RP IDENTIFICATION.
RG RefSeq;
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; KP245910; ALS88222.1; -; mRNA.
DR RefSeq; XP_005087909.1; XM_005087852.2.
DR STRING; 10036.ENSMAUP00000002463; -.
DR GeneID; 101825196; -.
DR KEGG; maua:101825196; -.
DR eggNOG; KOG1677; Eukaryota.
DR OrthoDB; 4850730at2759; -.
DR Proteomes; UP000189706; 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; 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:SF181; MRNA DECAY ACTIVATOR PROTEIN ZFP36L3; 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 2: Evidence at transcript level;
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:UP000189706};
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 141..169
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 179..207
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 141..169
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 179..207
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 115..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 52196 MW; CDE65812C820E483 CRC64;
MSTLLWTFYG TDIMRRNEMS LANPNLNGTL FTNGAAPSSS NFAPGFIPPP SSSNPQVLDH
LAPRAFNYTE GCSSSFLRGA NSCGNGQLGA TGSISQGAPL EPSGAYAVRQ FHPENSQHSL
QQRPPQQQKA SSSNSTVTSE RYKTELCRPF EESGICRYGH KCQFAHGSRE LRTLSRHPKY
KTEPCRTFHS VGFCPYGTRC HFIHNQQEHQ PVLSGSTSGE QSSANGCDAG HLGLNGEPQP
RLQTVSSASS SGLPSGHSHP LEAPVLVNQP TMNSGMLLPS SYPGATVPST CCAAVAAASE
AASAAAVFYR NGGVPCTTCA NNTFAFGQGM GGYMAPMTFQ NQNLAAANAA AYYHSQQQSL
AAPGQFQMPM VRPPAAVAPT AAAAIAPGAA SATFATPGTT AAAIAGPAGT AAAHATSSAT
ITDATVAEGS AQYLSLQLPD AQSESPEFDV LTSNLDSLLG TNSFDNLLSC SSSSSSPNGI
ESPSAQPSRR LPIFSRLSDS DK
//
