TISDA_XENLA
ID TISDA_XENLA Reviewed; 363 AA.
AC Q7ZXW9; Q9W673;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=mRNA decay activator protein ZFP36L2-A {ECO:0000305};
DE AltName: Full=CCCH zinc finger protein 3-A {ECO:0000312|EMBL:AAD24209.1};
DE Short=XC3H-3 {ECO:0000303|PubMed:10072766};
DE AltName: Full=Zinc finger protein 36, C3H1 type-like 2-A;
GN Name=zfp36l2-A;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH44086.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud {ECO:0000312|EMBL:AAH44086.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD24209.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF N-TERMINUS, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Egg {ECO:0000269|PubMed:10072766};
RX PubMed=10072766; DOI=10.1016/s0378-1119(98)00617-9;
RA De J., Lai W.S., Thorn J.M., Goldsworthy S.M., Liu X., Blackwell T.K.,
RA Blackshear P.J.;
RT "Identification of four CCCH zinc finger proteins in Xenopus, including a
RT novel vertebrate protein with four zinc fingers and severely restricted
RT expression.";
RL Gene 228:133-145(1999).
RN [3]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=10751406; DOI=10.1074/jbc.m001696200;
RA Lai W.S., Carballo E., Thorn J.M., Kennington E.A., Blackshear P.J.;
RT "Interactions of CCCH zinc finger proteins with mRNA. Binding of
RT tristetraprolin-related zinc finger proteins to Au-rich elements and
RT destabilization of mRNA.";
RL J. Biol. Chem. 275:17827-17837(2000).
RN [4]
RP FUNCTION.
RX PubMed=11279239; DOI=10.1074/jbc.m100680200;
RA Lai W.S., Blackshear P.J.;
RT "Interactions of CCCH zinc finger proteins with mRNA: tristetraprolin-
RT mediated AU-rich element-dependent mRNA degradation can occur in the
RT absence of a poly(A) tail.";
RL J. Biol. Chem. 276:23144-23154(2001).
RN [5]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=12748283; DOI=10.1128/mcb.23.11.3798-3812.2003;
RA Lai W.S., Kennington E.A., Blackshear P.J.;
RT "Tristetraprolin and its family members can promote the cell-free
RT deadenylation of AU-rich element-containing mRNAs by poly(A)
RT ribonuclease.";
RL Mol. Cell. Biol. 23:3798-3812(2003).
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 (PubMed:10751406,
CC PubMed:12748283). Acts as a 3'-untranslated region (UTR) ARE mRNA-
CC binding adapter protein to communicate signaling events to the mRNA
CC decay machinery (By similarity). Functions by recruiting the CCR4-NOT
CC deadenylase complex and probably other components of the cytoplasmic
CC RNA decay machinery to the bound ARE-containing mRNAs, and hence
CC promotes ARE-mediated mRNA deadenylation and decay processes (By
CC similarity). Binds to 3'-UTR ARE of numerous mRNAs (PubMed:12748283).
CC Induces also the degradation of ARE-containing mRNAs even in absence of
CC poly(A) tail (PubMed:10751406, PubMed:11279239). Required for
CC tubulogenesis during pronephros development (By similarity).
CC {ECO:0000250|UniProtKB:P23949, ECO:0000250|UniProtKB:P47974,
CC ECO:0000250|UniProtKB:Q805B4, ECO:0000269|PubMed:10751406,
CC ECO:0000269|PubMed:11279239, ECO:0000269|PubMed:12748283}.
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 -!- TISSUE SPECIFICITY: Widely expressed in adults.
CC {ECO:0000269|PubMed:10072766}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:10072766}.
CC -!- PTM: Phosphorylated (By similarity). {ECO:0000250|UniProtKB:P23949,
CC ECO:0000250|UniProtKB:P47974}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24209.1; Type=Miscellaneous discrepancy; Note=Probable hybrid of the A and B paralogous sequences.; Evidence={ECO:0000305};
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DR EMBL; BC044086; AAH44086.1; -; mRNA.
DR EMBL; AF061982; AAD24209.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001080610.1; NM_001087141.1.
DR AlphaFoldDB; Q7ZXW9; -.
DR SMR; Q7ZXW9; -.
DR BioGRID; 98544; 1.
DR IntAct; Q7ZXW9; 1.
DR DNASU; 380302; -.
DR GeneID; 380302; -.
DR KEGG; xla:380302; -.
DR CTD; 380302; -.
DR Xenbase; XB-GENE-6256550; zfp36l2.S.
DR OMA; GYGQREV; -.
DR OrthoDB; 1541140at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 380302; Expressed in internal ear 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; IDA: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; IDA:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA: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 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..363
FT /note="mRNA decay activator protein ZFP36L2-A"
FT /id="PRO_0000397913"
FT ZN_FING 131..159
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 169..197
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 148..189
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT REGION 308..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 131..136
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT COMPBIAS 323..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 40078 MW; 7550798421C70F9C CRC64;
MSATLLSAFY DIDLLYKNEK ALNNLALSTM LDKKAVGSPV SSTNSNLFPG FLRRHSASNL
QALSGSTNPA KFCHNNNNNQ LNESAASSTA LLNRENKFRD RSFSENGERS QHLLHLQQQQ
QKAGAQVNST RYKTELCRPF EESGACKYGE KCQFAHGFHE LRSLTRHPKY KTELCRTFHT
IGFCPYGPRC HFIHNAEERR QAPGAGERPK LHHSLSFSGF PNHSLDSAPL LESPTSRTPP
PQSSGSLYCQ ELLQLNNNNP CANNAFTFSG QELGLITPLA IHTQNSSYFR QPSSSPPLSF
QPLRKVSESP VFDAPPSPPD SLSDRDSYLS GSLSSGSLSG SDSPTLDSNR RLPIFSRLSI
SDD
