CNBP_BOVIN
ID CNBP_BOVIN Reviewed; 170 AA.
AC Q3T0Q6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=CCHC-type zinc finger nucleic acid binding protein {ECO:0000305};
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; Synonyms=ZNF9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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:0000250|UniProtKB:P62634}.
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; BC102298; AAI02299.1; -; mRNA.
DR RefSeq; NP_001029396.1; NM_001034224.1.
DR AlphaFoldDB; Q3T0Q6; -.
DR STRING; 9913.ENSBTAP00000016130; -.
DR PaxDb; Q3T0Q6; -.
DR PRIDE; Q3T0Q6; -.
DR Ensembl; ENSBTAT00000016130; ENSBTAP00000016130; ENSBTAG00000012159.
DR GeneID; 504831; -.
DR KEGG; bta:504831; -.
DR CTD; 7555; -.
DR VEuPathDB; HostDB:ENSBTAG00000012159; -.
DR VGNC; VGNC:27492; CNBP.
DR eggNOG; KOG4400; Eukaryota.
DR GeneTree; ENSGT00950000183041; -.
DR HOGENOM; CLU_058879_4_0_1; -.
DR InParanoid; Q3T0Q6; -.
DR OMA; SHQARDC; -.
DR OrthoDB; 1535084at2759; -.
DR TreeFam; TF316974; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000012159; Expressed in semitendinosus and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0045182; F:translation regulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IBA:GO_Central.
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..170
FT /note="CCHC-type zinc finger nucleic acid binding protein"
FT /id="PRO_0000247013"
FT ZN_FING 4..21
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 45..62
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 65..82
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 89..106
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 110..127
FT /note="CCHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 128..145
FT /note="CCHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 149..166
FT /note="CCHC-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 25..33
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 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53996"
FT MOD_RES 72
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P62633"
SQ SEQUENCE 170 AA; 18742 MW; 152BEC42881358E8 CRC64;
MSSNECFKCG RSGHWARECP TGGGRGRGMR SRGRGFQFVS SSLPDICYRC GESGHLAKDC
DLQEDACYNC GRGGHIAKDC KEPKREREQC CYNCGKPGHL ARDCDHADEQ KCYSCGEFGH
IQKDCTKVKC YRCGETGHVA INCSKTSEVN CYRCGESGHL ARECTIEATA
