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CEBPD_SHEEP
ID   CEBPD_SHEEP             Reviewed;         255 AA.
AC   Q9N0J3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=CCAAT/enhancer-binding protein delta;
DE            Short=C/EBP delta;
GN   Name=CEBPD;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=10799300; DOI=10.1006/bbrc.2000.2630;
RA   Davies G.E., Sabatakos G., Cryer A., Ramji D.P.;
RT   "The ovine CCAAT-enhancer binding protein delta gene: cloning,
RT   characterization, and species-specific autoregulation.";
RL   Biochem. Biophys. Res. Commun. 271:346-352(2000).
CC   -!- FUNCTION: Transcription activator that recognizes two different DNA
CC       motifs: the CCAAT homology common to many promoters and the enhanced
CC       core homology common to many enhancers (PubMed:10799300). Important
CC       transcription factor regulating the expression of genes involved in
CC       immune and inflammatory responses. Transcriptional activator that
CC       enhances IL6 transcription alone and as heterodimer with CEBPB (By
CC       similarity). {ECO:0000250|UniProtKB:P49716,
CC       ECO:0000269|PubMed:10799300}.
CC   -!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Can form stable
CC       heterodimers with CEBPA, CEBPB and CEBPE. Interacts with SPI1/PU.1.
CC       Interacts with PRDM16. {ECO:0000250|UniProtKB:P49716,
CC       ECO:0000250|UniProtKB:Q00322}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC       ECO:0000305|PubMed:10799300}.
CC   -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR   EMBL; AJ276820; CAB92973.1; -; Genomic_DNA.
DR   PIR; JC7264; JC7264.
DR   AlphaFoldDB; Q9N0J3; -.
DR   SMR; Q9N0J3; -.
DR   eggNOG; KOG3119; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR016468; C/EBP_chordates.
DR   Pfam; PF07716; bZIP_2; 1.
DR   PIRSF; PIRSF005879; CCAAT/enhancer-binding; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..255
FT                   /note="CCAAT/enhancer-binding protein delta"
FT                   /id="PRO_0000310864"
FT   DOMAIN          177..240
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..208
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          212..240
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        141..162
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        107
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   255 AA;  27040 MW;  85227319B6DE4F13 CRC64;
     MTCALQPGRP SGGAPWTAEP AAFYEPGRAG KPGRGAEPAA PAMYDDESAI DFSAYIDSMA
     AVPTLELCHD ELFADLFNSN HKAGALELLP GGPARLGGPG PAPRPLKREP DWGDGDAPGS
     LLPAQVAACA QTVVSLAPAA QPTPPASPDP PRRSPAPPAP GPARDKAAGK RGPDRGSPEY
     RQRRERNNIA VRKSRDKAKR RNQEMQQKLV ELSAENEKLQ QRVEQLTRDL AGLRRFFKQL
     PGAPFLPGAG AADAR
 
 
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