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CEBP2_CAEEL
ID   CEBP2_CAEEL             Reviewed;         100 AA.
AC   Q8IG69;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=CCAAT/enhancer-binding protein homolog 2 {ECO:0000303|PubMed:26876169};
GN   Name=cebp-2 {ECO:0000312|WormBase:C48E7.11};
GN   ORFNames=C48E7.11 {ECO:0000312|WormBase:C48E7.11};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-39; MET-78; ALA-79
RP   AND GLY-85.
RX   PubMed=26505800; DOI=10.1016/j.bbrc.2015.10.106;
RA   Xu X.Y., Hu J.P., Wu M.M., Wang L.S., Fang N.Y.;
RT   "CCAAT/enhancer-binding protein CEBP-2 controls fat consumption and fatty
RT   acid desaturation in Caenorhabditis elegans.";
RL   Biochem. Biophys. Res. Commun. 468:312-318(2015).
RN   [3] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=26876169; DOI=10.1016/j.celrep.2016.01.055;
RA   Reddy K.C., Dunbar T.L., Nargund A.M., Haynes C.M., Troemel E.R.;
RT   "The C. elegans CCAAT-Enhancer-Binding Protein Gamma Is Required for
RT   Surveillance Immunity.";
RL   Cell Rep. 14:1581-1589(2016).
RN   [4] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28662060; DOI=10.1371/journal.pgen.1006876;
RA   Tjahjono E., Kirienko N.V.;
RT   "A conserved mitochondrial surveillance pathway is required for defense
RT   against Pseudomonas aeruginosa.";
RL   PLoS Genet. 13:e1006876-e1006876(2017).
RN   [5]
RP   FUNCTION, INTERACTION WITH ZIP-11, AND DISRUPTION PHENOTYPE.
RX   PubMed=34804026; DOI=10.3389/fimmu.2021.744454;
RA   Zheng Z., Aihemaiti Y., Liu J., Afridi M.I., Yang S., Zhang X., Xu Y.,
RA   Chen C., Tu H.;
RT   "The bZIP Transcription Factor ZIP-11 Is Required for the Innate Immune
RT   Regulation in Caenorhabditis elegans.";
RL   Front. Immunol. 12:744454-744454(2021).
CC   -!- FUNCTION: Transcription factor that binds to the promoter and the
CC       enhancer regions of target genes (By similarity). Regulates expression
CC       of genes involved in fat metabolism, including ech-1.1 and fat-5
CC       (PubMed:26505800). Has a protective role in response to infection by
CC       the Gram-negative bacterium P.aeruginosa (PubMed:26876169,
CC       PubMed:28662060, PubMed:34804026). Required for the activation of
CC       infection response gene irg-1 following P.aeruginosa infection
CC       (PubMed:26876169). Required to prevent P.aeruginosa ToxA-mediated
CC       lethality (PubMed:26876169). May also function in concert with
CC       transcription factor zip-11 to mediate immune responses, independently
CC       of the pmk-1/p38 MAPK pathway (PubMed:34804026). May act together with
CC       the bZIP transcription factor, zip-2 (PubMed:26876169).
CC       {ECO:0000250|UniProtKB:P53567, ECO:0000269|PubMed:26505800,
CC       ECO:0000269|PubMed:26876169, ECO:0000269|PubMed:28662060,
CC       ECO:0000269|PubMed:34804026}.
CC   -!- SUBUNIT: Interacts with transcription factor zip-11.
CC       {ECO:0000269|PubMed:34804026}.
CC   -!- INTERACTION:
CC       Q8IG69; Q21361: atf-2; NbExp=2; IntAct=EBI-2914231, EBI-317743;
CC       Q8IG69; Q22156: atf-4; NbExp=3; IntAct=EBI-2914231, EBI-6749607;
CC       Q8IG69; Q23272: atfs-1; NbExp=2; IntAct=EBI-2914231, EBI-6748337;
CC       Q8IG69; Q94126: ces-2; NbExp=3; IntAct=EBI-2914231, EBI-328155;
CC       Q8IG69; Q9N5A8: zip-11; NbExp=3; IntAct=EBI-2914231, EBI-6740132;
CC       Q8IG69; Q21148: zip-2; NbExp=3; IntAct=EBI-2914231, EBI-6731556;
CC       Q8IG69; Q9XUK2: zip-3; NbExp=3; IntAct=EBI-2914231, EBI-322774;
CC       Q8IG69; A0A1I6CMA8: zip-9; NbExp=2; IntAct=EBI-2914231, EBI-26597024;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26876169}.
CC   -!- TISSUE SPECIFICITY: Expressed broadly in somatic tissues including the
CC       intestine. {ECO:0000269|PubMed:26876169}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces overall fat
CC       content (PubMed:26505800). Decreases survival upon infection with
CC       P.aeruginosa (PubMed:26876169, PubMed:28662060). Reduces induction of
CC       expression of infection response gene, irg-1, in response to
CC       P.aeruginosa (PubMed:26876169). The decrease in survival upon
CC       P.aeruginosa infection on a zip-11 mutant background is abolished by
CC       RNAi-mediated knockdown of cebp-2. {ECO:0000269|PubMed:26505800,
CC       ECO:0000269|PubMed:26876169, ECO:0000269|PubMed:28662060,
CC       ECO:0000269|PubMed:34804026}.
CC   -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR   EMBL; BX284601; CCD64211.1; -; Genomic_DNA.
DR   RefSeq; NP_871835.1; NM_182035.3.
DR   AlphaFoldDB; Q8IG69; -.
DR   SMR; Q8IG69; -.
DR   IntAct; Q8IG69; 14.
DR   STRING; 6239.C48E7.11; -.
DR   EPD; Q8IG69; -.
DR   PaxDb; Q8IG69; -.
DR   PeptideAtlas; Q8IG69; -.
DR   EnsemblMetazoa; C48E7.11.1; C48E7.11.1; WBGene00016754.
DR   GeneID; 172319; -.
DR   KEGG; cel:CELE_C48E7.11; -.
DR   UCSC; C48E7.11; c. elegans.
DR   CTD; 172319; -.
DR   WormBase; C48E7.11; CE32167; WBGene00016754; cebp-2.
DR   eggNOG; KOG3119; Eukaryota.
DR   HOGENOM; CLU_2348671_0_0_1; -.
DR   InParanoid; Q8IG69; -.
DR   OMA; MAPKNKE; -.
DR   OrthoDB; 1532157at2759; -.
DR   PhylomeDB; Q8IG69; -.
DR   SignaLink; Q8IG69; -.
DR   PRO; PR:Q8IG69; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00016754; Expressed in embryo and 3 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; IMP:WormBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:WormBase.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   Pfam; PF07716; bZIP_2; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; DNA-binding; Immunity; Innate immunity; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..100
FT                   /note="CCAAT/enhancer-binding protein homolog 2"
FT                   /id="PRO_0000451177"
FT   DOMAIN          17..80
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          23..48
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          52..73
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          79..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          24..83
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        7..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..100
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         39
FT                   /note="R->C: In gk509377; low-fat phenotype. Increases
FT                   expression of ech-1.1 mRNA and decreases fat-5 mRNA."
FT                   /evidence="ECO:0000269|PubMed:26505800"
FT   MUTAGEN         78
FT                   /note="M->I: In gk112657; low-fat phenotype."
FT                   /evidence="ECO:0000269|PubMed:26505800"
FT   MUTAGEN         79
FT                   /note="A->T: In gk112658; low-fat phenotype."
FT                   /evidence="ECO:0000269|PubMed:26505800"
FT   MUTAGEN         85
FT                   /note="G->E: In gk112659; low-fat phenotype."
FT                   /evidence="ECO:0000269|PubMed:26505800"
SQ   SEQUENCE   100 AA;  11625 MW;  C4A65961F3C71BC6 CRC64;
     MSGNRKRNTS EPREDDEDDY STKRKRNNEA VNRTRQKKRQ EENDTAEKVD ELKKENETLE
     RKVEQLQKEL SFLKEMFMAY AKNDGNDGPP PPPPPSSSAV
 
 
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