ID   LN28B_XENLA             Reviewed;         252 AA.
AC   Q8AVK2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Protein lin-28 homolog B;
DE            Short=Lin-28B;
DE   Flags: Fragment;
GN   Name=lin28b;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Suppressor of specific microRNA (miRNA) biogenesis. Binds
CC       target primary miRNA transcripts and sequester them in the nucleolus,
CC       away from the microprocessor complex, hence preventing their processing
CC       into mature miRNA. The specific interaction with target pri-miRNAs
CC       occurs via an 5'-GGAG-3' motif in the pre-miRNA terminal loop.
CC       {ECO:0000250|UniProtKB:Q6ZN17}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q6ZN17}.
CC   -!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
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DR   EMBL; BC042225; AAH42225.1; -; mRNA.
DR   AlphaFoldDB; Q8AVK2; -.
DR   SMR; Q8AVK2; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010587; P:miRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
DR   GO; GO:0031123; P:RNA 3'-end processing; ISS:UniProtKB.
DR   CDD; cd04458; CSP_CDS; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR002059; CSP_DNA-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF00313; CSD; 1.
DR   Pfam; PF00098; zf-CCHC; 2.
DR   PRINTS; PR00050; COLDSHOCK.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   PROSITE; PS51857; CSD_2; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; RNA-binding;
KW   RNA-mediated gene silencing; Zinc; Zinc-finger.
FT   CHAIN           1..>252
FT                   /note="Protein lin-28 homolog B"
FT                   /id="PRO_0000253796"
FT   DOMAIN          32..105
FT                   /note="CSD"
FT   ZN_FING         130..147
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         152..169
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   NON_TER         252
SQ   SEQUENCE   252 AA;  27983 MW;  D4BBD00B45F1C47D CRC64;
     MAEGGAARGT REEQGKLPEQ EEEEEEDPQV LLGSGHCKWF NVRMGFGFIS MTSREGSPLE
     NPVDVFVHQS KLYMDGFRSL KEGEPVEFTF KKSSKGFESL RVTGPGGNPC LGSERRPKAK
     TVQKRKPKGD RCYNCGGLDH HAKECNLPPQ PKKCHYCQST MHMVANCPHK IVPQHPTTSQ
     GRYEAEPQPS TSSFQREGGG AFDYSSPSYS QEGRSELSER SSRSPQEASL SKISTSPEEQ
     SRKGPSVQKK KK