LIN28_CAEBR
ID LIN28_CAEBR Reviewed; 237 AA.
AC Q61CX7; A8XGF0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein lin-28;
DE AltName: Full=Abnormal cell lineage protein 28;
GN Name=lin-28; ORFNames=CBG12720;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Heterochronic protein which controls the choice of stage
CC specific cell fates (By similarity). Regulates the timing of the second
CC larval stage events (L2 events) in the hypodermis (By similarity). May
CC negatively regulate the larval to adult transition via the suppression
CC of the microRNA (miRNA) let-7 during L3 (By similarity). Through this
CC regulatory role, controls the timing of the sexual maturation of the
CC nervous system (By similarity). Plays a role in governing the
CC developmental timing of male tail tip morphogenesis (By similarity).
CC Plays a role in the control of seam cell number and vulval development
CC (By similarity). {ECO:0000250|UniProtKB:P92186}.
CC -!- SUBUNIT: Component of a complex at least containing lep-2, lin-28 and
CC the long non-coding RNA lep-5, which mediates the degradation of lin-
CC 28. {ECO:0000250|UniProtKB:P92186}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P92186}.
CC -!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
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DR EMBL; HE600940; CAP31656.3; -; Genomic_DNA.
DR AlphaFoldDB; Q61CX7; -.
DR SMR; Q61CX7; -.
DR STRING; 6238.CBG12720; -.
DR EnsemblMetazoa; CBG12720b.1; CBG12720b.1; WBGene00033626.
DR WormBase; CBG12720a; CBP35906; WBGene00033626; Cbr-lin-28.
DR eggNOG; KOG3070; Eukaryota.
DR HOGENOM; CLU_089169_2_0_1; -.
DR InParanoid; Q61CX7; -.
DR OMA; EPPQSHC; -.
DR OrthoDB; 1604809at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IEA:EnsemblMetazoa.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:EnsemblMetazoa.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990715; F:mRNA CDS binding; IEA:EnsemblMetazoa.
DR GO; GO:0070883; F:pre-miRNA binding; IEA:EnsemblMetazoa.
DR GO; GO:0070878; F:primary miRNA binding; IEA:EnsemblMetazoa.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001708; P:cell fate specification; ISS:UniProtKB.
DR GO; GO:0007549; P:dosage compensation; IEA:EnsemblMetazoa.
DR GO; GO:2000635; P:negative regulation of primary miRNA processing; IEA:EnsemblMetazoa.
DR GO; GO:0031054; P:pre-miRNA processing; IBA:GO_Central.
DR GO; GO:0042659; P:regulation of cell fate specification; IEA:EnsemblMetazoa.
DR GO; GO:0040034; P:regulation of development, heterochronic; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
KW Cytoplasm; Developmental protein; Metal-binding; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..237
FT /note="Protein lin-28"
FT /id="PRO_0000253798"
FT DOMAIN 52..120
FT /note="CSD"
FT ZN_FING 143..160
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 166..183
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 237 AA; 26300 MW; 217A5D317FF3B509 CRC64;
MSTVVSEGRN GGNERYSPQD DVSKELPDIN GLSLEETMGI PSFDRLPSPT PRYFGSCKWF
NVSKGYGFVI DDNTGEDLFV HQSNLNMQGF RSLDEGERVS YYIQERSNGK GKEAYAVSGE
VEGQGLKGSR IHPLGRKKAV SLRCFRCGKF ATHKAKGCPN VKTDAKVCYT CGSEEHVSSV
CPERRRKHRP EQVAAEEAEA ARLAQEEADR SSPEENERKD GKLVEQKETE TADKAGK
