ID G3TJ20_LOXAF Unreviewed; 205 AA.
AC G3TJ20;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Protein lin-28 homolog A {ECO:0000256|ARBA:ARBA00041056};
GN Name=LIN28A {ECO:0000313|Ensembl:ENSLAFP00000014696.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000014696.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000014696.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014696.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000014696.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014696.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}. Cytoplasm, Stress granule
CC {ECO:0000256|ARBA:ARBA00004210}. Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}. Rough endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004427}.
CC -!- SIMILARITY: Belongs to the lin-28 family.
CC {ECO:0000256|ARBA:ARBA00008840}.
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DR RefSeq; XP_003415460.1; XM_003415412.1.
DR AlphaFoldDB; G3TJ20; -.
DR STRING; 9785.ENSLAFP00000014696; -.
DR Ensembl; ENSLAFT00000017522.3; ENSLAFP00000014696.3; ENSLAFG00000017525.3.
DR GeneID; 100675495; -.
DR KEGG; lav:100675495; -.
DR CTD; 79727; -.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00940000153295; -.
DR HOGENOM; CLU_089169_4_0_1; -.
DR InParanoid; G3TJ20; -.
DR OMA; RCYNCAG; -.
DR OrthoDB; 5487692at2759; -.
DR TreeFam; TF316240; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IEA:Ensembl.
DR GO; GO:0035198; F:miRNA binding; IEA:Ensembl.
DR GO; GO:1905538; F:polysome binding; IEA:Ensembl.
DR GO; GO:0070883; F:pre-miRNA binding; IEA:Ensembl.
DR GO; GO:0140517; F:protein-RNA adaptor activity; IEA:Ensembl.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IEA:Ensembl.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0010587; P:miRNA catabolic process; IEA:Ensembl.
DR GO; GO:0045686; P:negative regulation of glial cell differentiation; IEA:Ensembl.
DR GO; GO:2000632; P:negative regulation of pre-miRNA processing; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR GO; GO:1901724; P:positive regulation of cell proliferation involved in kidney development; IEA:Ensembl.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IEA:Ensembl.
DR GO; GO:0031054; P:pre-miRNA processing; IEA:Ensembl.
DR GO; GO:0071076; P:RNA 3' uridylation; IEA:Ensembl.
DR GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 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 PANTHER; PTHR46109; PROTEIN LIN-28; 1.
DR PANTHER; PTHR46109:SF2; PROTEIN LIN-28 HOMOLOG A; 1.
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; Nucleic acid-binding proteins; 1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
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 35..107
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT DOMAIN 134..149
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 174..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 205 AA; 22324 MW; C7A789F441A4BFA6 CRC64;
MGSVSNQQFA GGCAKAAEEA PEDAARAVEE PQLLHGAGIC KWFNVRMGFG FLSMTARAGV
ALDPPVDVFV HQSKLHMEGF RSLKEGEAVE FTFKKSAKGL ESIRVTGPGG VFCIGSERRP
KGKNMQKRRS KGDRCYNCGG LDHHAKECKL PPQPKKCHFC QSISHMVASC PMKAQQASGS
QGKPAYFREE EEEIQSPALL PEAQN
//
