TISDB_XENLA
ID TISDB_XENLA Reviewed; 364 AA.
AC Q805B4; Q5XH52; Q9W673;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=mRNA decay activator protein ZFP36L2-B {ECO:0000305};
DE AltName: Full=CCCH zinc finger protein 3-B {ECO:0000303|PubMed:12914788};
DE Short=XC3H-3b {ECO:0000303|PubMed:12914788};
DE AltName: Full=Zinc finger protein 36, C3H1 type-like 2-B;
GN Name=zfp36l2-B; Synonyms=zfp36l2 {ECO:0000312|Xenbase:XB-GENE-971016};
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:0000305, ECO:0000312|EMBL:BAC54909.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Neurula {ECO:0000269|PubMed:12914788};
RX PubMed=12914788; DOI=10.1016/s0006-291x(03)01419-0;
RA Kaneko T., Chan T., Satow R., Fujita T., Asashima M.;
RT "The isolation and characterization of XC3H-3b: a CCCH zinc-finger protein
RT required for pronephros development.";
RL Biochem. Biophys. Res. Commun. 308:566-572(2003).
RN [2] {ECO:0000312|EMBL:AAH84221.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud {ECO:0000312|EMBL:AAH84221.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAD24209.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF C-TERMINUS.
RC TISSUE=Kidney {ECO:0000312|EMBL:AAD24209.1};
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 [4]
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).
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
CC (PubMed:10751406). 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:12914788).
CC Induces also the degradation of ARE-containing mRNAs even in absence of
CC poly(A) tail (By similarity). Required for tubulogenesis during
CC pronephros development (PubMed:12914788).
CC {ECO:0000250|UniProtKB:P23949, ECO:0000250|UniProtKB:P47974,
CC ECO:0000250|UniProtKB:Q7ZXW9, ECO:0000269|PubMed:10751406,
CC ECO:0000269|PubMed:12914788}.
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: Remains unlocalized in the egg and early embryo.
CC From stage 21 (late neurula), expressed around the pronephros in the
CC anterior crests, pharyngeal arch, hindbrain, mesodermal tissues around
CC the pronephros and tail-bud. This expression pattern is maintained up
CC to the tadpole stage. {ECO:0000269|PubMed:12914788}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed in the unfertilized egg, with expression increasing from
CC embryonic stage 12 up to the tadpole stage.
CC {ECO:0000269|PubMed:12914788}.
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};
CC Sequence=AAH84221.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB097482; BAC54909.1; -; mRNA.
DR EMBL; BC084221; AAH84221.1; ALT_INIT; mRNA.
DR EMBL; AF061982; AAD24209.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001081886.1; NM_001088417.1.
DR AlphaFoldDB; Q805B4; -.
DR SMR; Q805B4; -.
DR GeneID; 398103; -.
DR KEGG; xla:398103; -.
DR CTD; 398103; -.
DR Xenbase; XB-GENE-971016; zfp36l2.L.
DR OMA; PNYYEDI; -.
DR OrthoDB; 1541140at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
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:0072080; P:nephron tubule development; IMP: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:0039020; P:pronephric nephron tubule development; IMP:UniProtKB.
DR GO; GO:0048793; P:pronephros development; IMP: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..364
FT /note="mRNA decay activator protein ZFP36L2-B"
FT /id="PRO_0000397914"
FT ZN_FING 133..161
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 171..199
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 102..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..191
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT REGION 308..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 133..138
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P47974"
FT COMPBIAS 109..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 364 AA; 40329 MW; A11C23B1834DD040 CRC64;
MSTTLLSAFY DIDLLYKNEK ALNNLALSTM LDKKAVGSPV SSTNSNLFPG FLRRHSATNL
QALSGSTNLA KFCPNNNNNP LKDPAVSSTA LLNRENKFRD RSFSENGERS QHLLHLQQQQ
QQQKAGAQVN STRYKTELCR PFEENGACKY GEKCQFAHGF HELRSLTRHP KYKTELCRTF
HTIGFCPYGP RCHFIHNAEE RRQAPGAGER PKLHHSLSFS GFPNHSLDSP LLESPTSRTP
PPQSSGSLYC QELLQLNNNN PCANNAFTFS GQELGLIAPL AIHTQNQSYC RQPCSSPPLS
FQPLRRVSES PVFDAPPSPP DSLSDRDSYL SGSLSSGSLS GSDSPTLDSN RRLPIFSRLS
ISDD
