LN28B_CHICK
ID LN28B_CHICK Reviewed; 250 AA.
AC Q45KJ4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein lin-28 homolog B;
DE Short=Lin-28B;
GN Name=LIN28B;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Moss E.G., Kemper K.;
RT "Expression of Lin28A and Lin28B in post-implantation mouse embryos.";
RL Submitted (JUL-2005) 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; DQ127227; AAZ38896.1; -; mRNA.
DR RefSeq; NP_001029990.1; NM_001034818.1.
DR AlphaFoldDB; Q45KJ4; -.
DR SMR; Q45KJ4; -.
DR STRING; 9031.ENSGALP00000040862; -.
DR PaxDb; Q45KJ4; -.
DR Ensembl; ENSGALT00000044077; ENSGALP00000040862; ENSGALG00000026761.
DR GeneID; 421786; -.
DR KEGG; gga:421786; -.
DR CTD; 389421; -.
DR VEuPathDB; HostDB:geneid_421786; -.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00940000153295; -.
DR HOGENOM; CLU_089169_1_1_1; -.
DR InParanoid; Q45KJ4; -.
DR OMA; GPWGNMA; -.
DR OrthoDB; 1604809at2759; -.
DR PhylomeDB; Q45KJ4; -.
DR TreeFam; TF316240; -.
DR PRO; PR:Q45KJ4; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000026761; Expressed in testis and 3 other tissues.
DR ExpressionAtlas; Q45KJ4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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..250
FT /note="Protein lin-28 homolog B"
FT /id="PRO_0000253795"
FT DOMAIN 29..102
FT /note="CSD"
FT ZN_FING 127..144
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 149..166
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 250 AA; 27398 MW; ADEC99707ECC19B3 CRC64;
MAEAGASKGG EEPGRLPEHE EEEESPLWHG AGHCKWFNVR MGFGFISMSS REGSPLESPV
DVFVHQSKLY MEGFRSLKEG EPVEFTYKKS SKGLESIRVT GPGGSPCLGS ERRPKGKTVQ
KRKPKGDRCY NCGGLDHHAK ECSLPPQPKK CHYCQSIMHM VANCPHKTVS QQPTSSQGRH
EAEPQPSTSA FLREGGGTYG YSSPSYSQEG RSEISERSGR SPQEASSSKL SASPEEPSRK
GPSVQKRKKT
