CNBP_RAT
ID CNBP_RAT Reviewed; 177 AA.
AC P62634; P20694; Q5QJQ8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=CCHC-type zinc finger nucleic acid binding protein {ECO:0000312|RGD:621807};
DE AltName: Full=Cellular nucleic acid-binding protein {ECO:0000305};
DE Short=CNBP {ECO:0000305};
DE AltName: Full=Zinc finger protein 9;
GN Name=Cnbp {ECO:0000312|RGD:621807}; Synonyms=Znf9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=7788528; DOI=10.1093/dnares/2.1.45;
RA Yasuda J., Mashiyama S., Makino R., Ohyama S., Sekiya T., Hayashi K.;
RT "Cloning and characterization of rat cellular nucleic acid binding protein
RT (CNBP) cDNA.";
RL DNA Res. 2:45-49(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RA Wang Z., Tenniswood M.;
RT "Identification and characterization of a distal repression region that
RT represses clusterin expression.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=14505273; DOI=10.1086/378720;
RA Liquori C.L., Ikeda Y., Weatherspoon M., Ricker K., Schoser B.G.,
RA Dalton J.C., Day J.W., Ranum L.P.;
RT "Myotonic dystrophy type 2: human founder haplotype and evolutionary
RT conservation of the repeat tract.";
RL Am. J. Hum. Genet. 73:849-862(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344/DuCrj, and LEC/Crj;
RX PubMed=15978772; DOI=10.1016/j.ygeno.2005.05.007;
RA Tsuji A.B., Sugyo A., Ogiu T., Sagara M., Kimura T., Ishikawa A., Sudo H.,
RA Ohtsuki M., Aburatani H., Imai T., Harada Y.N.;
RT "Fine mapping of radiation susceptibility and gene expression analysis of
RT LEC congenic rat lines.";
RL Genomics 86:271-279(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Single-stranded DNA-binding protein that preferentially binds
CC to the sterol regulatory element (SRE) sequence 5'-GTGCGGTG-3', and
CC thereby mediates transcriptional repression (By similarity). Has a role
CC as transactivator of the Myc promoter (By similarity). Binds single-
CC stranded RNA in a sequence-specific manner (PubMed:7788528). Binds G-
CC rich elements in target mRNA coding sequences (By similarity). Prevents
CC G-quadruplex structure formation in vitro, suggesting a role in
CC supporting translation by resolving stable structures on mRNAs (By
CC similarity). {ECO:0000250|UniProtKB:P53996,
CC ECO:0000250|UniProtKB:P62633, ECO:0000269|PubMed:7788528}.
CC -!- SUBUNIT: Associates with the 40S ribosomal subunit, the 80S ribosome
CC and with polysomes. {ECO:0000250|UniProtKB:P62633}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53996}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62633}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P53996}.
CC -!- PTM: Arginine methylation by PRMT1 in the Arg/Gly-rich region impedes
CC RNA binding. {ECO:0000250|UniProtKB:P62633}.
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DR EMBL; D45254; BAA08212.1; -; mRNA.
DR EMBL; AF242550; AAF78224.1; -; mRNA.
DR EMBL; AY329624; AAR89464.1; -; Genomic_DNA.
DR EMBL; AB158421; BAE16993.1; -; mRNA.
DR EMBL; AB158422; BAE16994.1; -; mRNA.
DR EMBL; BC062225; AAH62225.1; -; mRNA.
DR PIR; JC2512; JC2512.
DR RefSeq; NP_072120.1; NM_022598.1.
DR AlphaFoldDB; P62634; -.
DR BioGRID; 249114; 1.
DR STRING; 10116.ENSRNOP00000013884; -.
DR iPTMnet; P62634; -.
DR PhosphoSitePlus; P62634; -.
DR jPOST; P62634; -.
DR PaxDb; P62634; -.
DR PRIDE; P62634; -.
DR GeneID; 64530; -.
DR KEGG; rno:64530; -.
DR CTD; 7555; -.
DR RGD; 621807; Cnbp.
DR VEuPathDB; HostDB:ENSRNOG00000010239; -.
DR eggNOG; KOG4400; Eukaryota.
DR HOGENOM; CLU_058879_4_0_1; -.
DR InParanoid; P62634; -.
DR OMA; SHQARDC; -.
DR OrthoDB; 1535084at2759; -.
DR PhylomeDB; P62634; -.
DR PRO; PR:P62634; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000010239; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; P62634; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051880; F:G-quadruplex DNA binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:RGD.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:RGD.
DR GO; GO:0045182; F:translation regulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071919; P:G-quadruplex DNA formation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00098; zf-CCHC; 7.
DR SMART; SM00343; ZnF_C2HC; 7.
DR SUPFAM; SSF57756; SSF57756; 4.
DR PROSITE; PS50158; ZF_CCHC; 7.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; DNA-binding; Endoplasmic reticulum; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62633"
FT CHAIN 2..177
FT /note="CCHC-type zinc finger nucleic acid binding protein"
FT /id="PRO_0000089968"
FT ZN_FING 4..21
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 52..69
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 72..89
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 96..113
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 117..134
FT /note="CCHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 135..152
FT /note="CCHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 156..173
FT /note="CCHC-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 25..38
FT /note="RNA-binding Arg/Gly-rich region (RGG-box)"
FT /evidence="ECO:0000250|UniProtKB:P62633"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62633"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53996"
FT MOD_RES 25
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P62633"
FT MOD_RES 27
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:P62633"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53996"
FT MOD_RES 79
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P62633"
SQ SEQUENCE 177 AA; 19463 MW; 996F398285F52618 CRC64;
MSSNECFKCG RSGHWARECP TGGGRGRGMR SRGRGGFTSD RGFQFVSSSL PDICYRCGES
GHLAKDCDLQ EDACYNCGRG GHIAKDCKEP KREREQCCYN CGKPGHLARD CDHADEQKCY
SCGEFGHIQK DCTKVKCYRC GETGHVAINC SKTSEVNCYR CGESGHLARE CTIEATA
