TISD_XENTR
ID TISD_XENTR Reviewed; 362 AA.
AC A4IIN5; F7CNB8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=mRNA decay activator protein ZFP36L2 {ECO:0000305};
DE AltName: Full=Zinc finger protein 36, C3H1 type-like 2;
GN Name=zfp36l2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000312|EMBL:AAI36092.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI36092.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein
CC to communicate signaling events to the mRNA decay machinery (By
CC similarity). Functions by recruiting the CCR4-NOT deadenylase complex
CC and probably other components of the cytoplasmic RNA decay machinery to
CC the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA
CC deadenylation and decay processes (By similarity). Binds to 3'-UTR ARE
CC of numerous mRNAs (By similarity). Induces also the degradation of ARE-
CC containing mRNAs even in absence of poly(A) tail (By similarity).
CC Required for tubulogenesis during pronephros development (By
CC similarity). {ECO:0000250|UniProtKB:P23949,
CC ECO:0000250|UniProtKB:P47974, ECO:0000250|UniProtKB:Q7ZXW9,
CC ECO:0000250|UniProtKB:Q805B4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P23949}. Cytoplasm
CC {ECO:0000250|UniProtKB:P23949}. Note=Shuttles between the nucleus and
CC the cytoplasm in a XPO1/CRM1-dependent manner.
CC {ECO:0000250|UniProtKB:P23949}.
CC -!- PTM: Phosphorylated (By similarity). {ECO:0000250|UniProtKB:P23949,
CC ECO:0000250|UniProtKB:P47974}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI36092.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AAMC01011930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136091; AAI36092.1; ALT_INIT; mRNA.
DR RefSeq; NP_001096423.1; NM_001102953.1.
DR RefSeq; XP_012818082.1; XM_012962628.2.
DR AlphaFoldDB; A4IIN5; -.
DR SMR; A4IIN5; -.
DR STRING; 8364.ENSXETP00000020367; -.
DR PaxDb; A4IIN5; -.
DR DNASU; 100125029; -.
DR Ensembl; ENSXETT00000020367; ENSXETP00000020367; ENSXETG00000009274.
DR GeneID; 100125029; -.
DR KEGG; xtr:100125029; -.
DR CTD; 678; -.
DR Xenbase; XB-GENE-971012; zfp36l2.
DR eggNOG; KOG1677; Eukaryota.
DR HOGENOM; CLU_033040_1_0_1; -.
DR InParanoid; A4IIN5; -.
DR OMA; PNYYEDI; -.
DR OrthoDB; 1541140at2759; -.
DR PhylomeDB; A4IIN5; -.
DR TreeFam; TF315463; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000009274; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0060216; P:definitive hemopoiesis; ISS:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; ISS:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0031086; P:nuclear-transcribed mRNA catabolic process, deadenylation-independent decay; ISS:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0048793; P:pronephros development; ISS:UniProtKB.
DR GO; GO:0045577; P:regulation of B cell differentiation; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0048103; P:somatic stem cell division; ISS:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISS:UniProtKB.
DR InterPro; IPR007635; Tis11B_N.
DR InterPro; IPR045877; ZFP36-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12547; PTHR12547; 2.
DR Pfam; PF04553; Tis11B_N; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..362
FT /note="mRNA decay activator protein ZFP36L2"
FT /id="PRO_0000397915"
FT ZN_FING 130..158
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 168..196
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 100..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..188
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT REGION 225..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 130..135
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT COMPBIAS 107..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 191
FT /note="F -> L (in Ref. 2; AAI36092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 40065 MW; 94DC5A963C219E00 CRC64;
MSTTLLSAFY DIDLLYKNEK VLNNLALSTM LDKKAVGSPV SSTNSNLFPG FLRRHSASNL
QALSGNTNPA KFCPNNNQLK EPAAGSTALL NRENKFRDRS FSENGERSQH LLHLQQQQQQ
KAGAQVNSTR YKTELCRPFE ESGACKYGEK CQFAHGFHEL RSLTRHPKYK TELCRTFHTI
GFCPYGPRCH FIHNAEERRQ APGAGERPKL HHSLSFSGFP NHSLDSPLLE SPTSRTPPPQ
SSSSLYCQEL LQLNNNNNPC ANNAFTFSGQ ELGLIAPLAI HTQNPPYCRQ PSSSPPLSFQ
PLRRVSESPV FDAPPSPPDS LSDRDSYLSG SLSSGSLSGS DSPTLDSNRR LPIFSRLSIS
DD
