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Database: UniProt
Entry: A0A1S2ZSW2_ERIEU
LinkDB: A0A1S2ZSW2_ERIEU
Original site: A0A1S2ZSW2_ERIEU 
ID   A0A1S2ZSW2_ERIEU        Unreviewed;       323 AA.
AC   A0A1S2ZSW2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=mRNA decay activator protein ZFP36 {ECO:0000256|ARBA:ARBA00040871, ECO:0000256|RuleBase:RU369014};
DE   AltName: Full=Zinc finger protein 36 {ECO:0000256|RuleBase:RU369014};
GN   Name=ZFP36 {ECO:0000313|RefSeq:XP_007524046.2};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007524046.2};
RN   [1] {ECO:0000313|RefSeq:XP_007524046.2}
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: Cytoplasmic granule
CC       {ECO:0000256|ARBA:ARBA00004463}. Nucleus
CC       {ECO:0000256|RuleBase:RU369014}. Cytoplasm
CC       {ECO:0000256|RuleBase:RU369014}.
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DR   RefSeq; XP_007524046.2; XM_007523984.2.
DR   AlphaFoldDB; A0A1S2ZSW2; -.
DR   GeneID; 103114332; -.
DR   CTD; 7538; -.
DR   eggNOG; KOG1677; Eukaryota.
DR   InParanoid; A0A1S2ZSW2; -.
DR   OrthoDB; 23913at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
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:SF58; 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   Exosome {ECO:0000256|ARBA:ARBA00022835};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Nucleus {ECO:0000256|RuleBase:RU369014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
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          103..131
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          141..169
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         103..131
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         141..169
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          15..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..92
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..227
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   323 AA;  34077 MW;  B009BE8282D240A0 CRC64;
     MDLMDLTAIY ESLLSLNPEP PNHEETESSP GWASSAPWSL GSSESNRAGV TTRLPSRSTS
     LVEGRSCGWV PPPPGFAPLA PRPAPDLSPS PTSPTSTPTT SSRYKTELCR TFSESGRCRY
     GAKCQFAHGL VELRQASRHP KYKTELCHKF YLHGRCPYGS RCHFIHNPTE DLAVPGHPHM
     LRQSISFSGL PSGRRSSPPP AGLTGPSLSC SFSPSSSPPP PPGDLPLSPS AFSAAPGTPV
     ARRDPTPNCC PSCRRAAPSS VWGPLGSLAR SPSAHSLGSD PDEYASSGSS LGGSDSPVFD
     AGVLGPPVAS RRLPIFNRIS VSE
//
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