ID G1P807_MYOLU Unreviewed; 185 AA.
AC G1P807;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Lin-28 homolog B {ECO:0000313|Ensembl:ENSMLUP00000006277.2};
GN Name=LIN28B {ECO:0000313|Ensembl:ENSMLUP00000006277.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000006277.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000006277.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000006277.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the lin-28 family.
CC {ECO:0000256|ARBA:ARBA00008840}.
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DR EMBL; AAPE02042008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1P807; -.
DR STRING; 59463.ENSMLUP00000006277; -.
DR Ensembl; ENSMLUT00000006872.2; ENSMLUP00000006277.2; ENSMLUG00000006883.2.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00940000153295; -.
DR HOGENOM; CLU_089169_0_0_1; -.
DR InParanoid; G1P807; -.
DR OMA; WGNMAEG; -.
DR TreeFam; TF316240; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010587; P:miRNA catabolic process; IEA:Ensembl.
DR GO; GO:2000632; P:negative regulation of pre-miRNA processing; IEA:Ensembl.
DR GO; GO:2000635; P:negative regulation of primary miRNA processing; IEA:Ensembl.
DR GO; GO:2000627; P:positive regulation of miRNA catabolic process; IEA:Ensembl.
DR GO; GO:0031054; P:pre-miRNA processing; IEA:Ensembl.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:Ensembl.
DR GO; GO:0050779; P:RNA destabilization; IEA:Ensembl.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
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 PANTHER; PTHR46109; PROTEIN LIN-28; 1.
DR PANTHER; PTHR46109:SF3; PROTEIN LIN-28 HOMOLOG B; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS51857; CSD_2; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 1..36
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 63..77
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 33..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 185 AA; 20128 MW; BEDA1CEF3587FC65 CRC64;
QSKLFMEGFR SLKEGEPVEF TFKKSSKGLE SIRVTGPGGS PCLGSERRPK GKTLQKRRPK
GDRCYNCGGL DHHAKECSLP PQPKKCHYCQ SITHMVANCP HKTVVQPPVS SQGRQEADSQ
PCTAAFPREV GGGHGCTSPP FPQEARSEIA EWPGRSPQEA SSTKSSAAPE EQSKKGPSVQ
KRKKT
//
