LN28A_CHICK
ID LN28A_CHICK Reviewed; 202 AA.
AC Q45KJ5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protein lin-28 homolog A;
DE Short=Lin-28A;
GN Name=LIN28A; Synonyms=LIN28;
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 (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein that inhibits processing of pre-let-7
CC miRNAs and regulates translation of mRNAs that control developmental
CC timing, pluripotency and metabolism. Seems to recognize a common
CC structural G-quartet (G4) feature in its miRNA and mRNA targets (By
CC similarity). 'Translational enhancer' that drives specific mRNAs to
CC polysomes and increases the efficiency of protein synthesis. Its
CC association with the translational machinery and target mRNAs results
CC in an increased number of initiation events per molecule of mRNA and,
CC indirectly, in mRNA stabilization. Suppressor of microRNA (miRNA)
CC biogenesis, including that of let-7. Binds specific target miRNA
CC precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in their
CC terminal loop, and recruits uridylyltransferase. This results in the
CC terminal uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail
CC to be processed by Dicer and undergo degradation (By similarity).
CC Localized to the periendoplasmic reticulum area, binds to a large
CC number of spliced mRNAs and inhibits the translation of mRNAs destined
CC for the ER, reducing the synthesis of transmembrane proteins, ER or
CC Golgi lumen proteins, and secretory proteins. Binds to and enhances the
CC translation of mRNAs for several metabolic enzymes, increasing
CC glycolysis and oxidative phosphorylation. Which, with the let-7
CC repression may enhance tissue repair in adult tissue (By similarity).
CC {ECO:0000250|UniProtKB:Q8K3Y3, ECO:0000250|UniProtKB:Q9H9Z2}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8K3Y3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y3}. Rough
CC endoplasmic reticulum {ECO:0000250|UniProtKB:Q8K3Y3}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:Q9H9Z2}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q8K3Y3}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q8K3Y3}. Note=Predominantly cytoplasmic. In the
CC cytoplasm, localizes to peri-endoplasmic reticulum regions and may be
CC bound to the cytosolic surface of rough endoplasmic reticulum (ER) on
CC which ER-associated mRNAs are translated. Shuttle from the nucleus to
CC the cytoplasm requires RNA-binding. {ECO:0000250|UniProtKB:Q8K3Y3}.
CC -!- DOMAIN: The CCHC zinc fingers interact with the GGAG motif at the 3'
CC end of let-7 miRNAs precursors, more generally they bind the 5'-NGNNG-
CC 3' consensus motif with micromolar affinity. The CSD domain recognizes
CC the loop at the 5' end. The flexible linker allows accommodating
CC variable sequences and lengths among let-7 family members (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
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DR EMBL; DQ127226; AAZ38895.2; -; mRNA.
DR RefSeq; NP_001026944.2; NM_001031774.2.
DR AlphaFoldDB; Q45KJ5; -.
DR SMR; Q45KJ5; -.
DR STRING; 9031.ENSGALP00000000528; -.
DR PaxDb; Q45KJ5; -.
DR GeneID; 428206; -.
DR KEGG; gga:428206; -.
DR CTD; 79727; -.
DR VEuPathDB; HostDB:geneid_428206; -.
DR eggNOG; KOG3070; Eukaryota.
DR InParanoid; Q45KJ5; -.
DR OrthoDB; 1604809at2759; -.
DR PhylomeDB; Q45KJ5; -.
DR PRO; PR:Q45KJ5; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
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:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; 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; 1.
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 Cytoplasm; Endoplasmic reticulum; Metal-binding; Nucleus;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing; Zinc;
KW Zinc-finger.
FT CHAIN 1..202
FT /note="Protein lin-28 homolog A"
FT /id="PRO_0000253789"
FT DOMAIN 33..106
FT /note="CSD"
FT ZN_FING 131..148
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 153..170
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..130
FT /note="Flexible linker"
FT /evidence="ECO:0000250"
FT REGION 169..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 202 AA; 22089 MW; 83EBAAD70D152DC7 CRC64;
MGSVSNQQFA GAKPGEEPSG DSPKAENESQ PLHGSGICKW FNVRMGFGFL SMTAKGGAML
DSPVDVFVHQ SKLHMEGFRS LKEGEAVEFT FKKSSKGLES IRVTGPGGVF CIGSERRPKS
KSLQKRRSKG DRCYNCGGLD HHAKECKLPP QPKKCHFCQS ISHMVANCPA KAQQSPSSQG
KPAYFREKED MHSSALLPET RE
