LIN28_CAERE
ID LIN28_CAERE Reviewed; 214 AA.
AC P91599; P91602;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein lin-28;
DE AltName: Full=Abnormal cell lineage protein 28;
GN Name=lin-28;
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9054503; DOI=10.1016/s0092-8674(00)81906-6;
RA Moss E.G., Lee R.C., Ambros V.;
RT "The cold shock domain protein LIN-28 controls developmental timing in C.
RT elegans and is regulated by the lin-4 RNA.";
RL Cell 88:637-646(1997).
CC -!- FUNCTION: Heterochronic protein which controls the choice of stage
CC specific cell fates. Regulates the timing of the second larval stage
CC events (L2 events) in the hypodermis (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
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DR EMBL; U75913; AAC47477.1; -; mRNA.
DR EMBL; U75914; AAC47478.1; -; mRNA.
DR AlphaFoldDB; P91599; -.
DR SMR; P91599; -.
DR STRING; 31234.CRE28214; -.
DR eggNOG; KOG3070; Eukaryota.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001708; P:cell fate specification; ISS:UniProtKB.
DR GO; GO:0010605; P:negative regulation of macromolecule metabolic process; IEA:UniProt.
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; Developmental protein; Metal-binding; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..214
FT /note="Protein lin-28"
FT /id="PRO_0000253800"
FT DOMAIN 48..116
FT /note="CSD"
FT ZN_FING 139..156
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 162..179
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 149
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="1"
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"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 21..33
FT /note="ELPDLENLKLTDD -> DVSELIPNLNNIQLNET (in Ref. 1;
FT AAC47478)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="D -> E (in Ref. 1; AAC47478)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="Y -> F (in Ref. 1; AAC47478)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="E -> D (in Ref. 1; AAC47478)"
FT /evidence="ECO:0000305"
FT CONFLICT 196..214
FT /note="AARLAAETAASSPRGDHDD -> EAARRAAEESSSTSDEGSSGIKEEHHEHQ
FT VKNETSDDSEQ (in Ref. 1; AAC47478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 23923 MW; 04D049A9B654B509 CRC64;
MSTVVSEGRN GGNERYSPQD ELPDLENLKL TDDMRVPSFD RLPSPTPRYY GSCKWFNVSK
GYGFVIDDIT REDLFVHQSN LNMQGFRSLD EGERVSYYIQ ERSNGKGREA YAVSGEVEGQ
GLKGSRIHPL GRKKAVSLRC FRCGKFATHK AKSCPNVKTD AKVCYTCGSE EHVSSICPER
RRKHRPEQVA AEEAEAARLA AETAASSPRG DHDD
