CEBP1_CAEEL
ID CEBP1_CAEEL Reviewed; 319 AA.
AC Q18909;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=CCAAT/enhancer-binding protein homolog 1 {ECO:0000312|WormBase:D1005.3};
GN Name=cebp-1 {ECO:0000312|WormBase:D1005.3};
GN ORFNames=D1005.3 {ECO:0000312|WormBase:D1005.3};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP SER-250 AND ARG-251.
RX PubMed=19737525; DOI=10.1016/j.cell.2009.06.023;
RA Yan D., Wu Z., Chisholm A.D., Jin Y.;
RT "The DLK-1 kinase promotes mRNA stability and local translation in C.
RT elegans synapses and axon regeneration.";
RL Cell 138:1005-1018(2009).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ALA-285.
RX PubMed=21368137; DOI=10.1073/pnas.1101360108;
RA Bounoutas A., Kratz J., Emtage L., Ma C., Nguyen K.C., Chalfie M.;
RT "Microtubule depolymerization in Caenorhabditis elegans touch receptor
RT neurons reduces gene expression through a p38 MAPK pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3982-3987(2011).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH ETS-4.
RX PubMed=26484536; DOI=10.1371/journal.pgen.1005603;
RA Li C., Hisamoto N., Matsumoto K.;
RT "Axon regeneration is regulated by Ets-C/EBP transcription complexes
RT generated by activation of the cAMP/Ca2+ signaling pathways.";
RL PLoS Genet. 11:E1005603-E1005603(2015).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH NIPI-3, AND DEVELOPMENTAL STAGE.
RX PubMed=27927209; DOI=10.1186/s12915-016-0320-z;
RA Kim K.W., Thakur N., Piggott C.A., Omi S., Polanowska J., Jin Y., Pujol N.;
RT "Coordinated inhibition of C/EBP by Tribbles in multiple tissues is
RT essential for Caenorhabditis elegans development.";
RL BMC Biol. 14:104-104(2016).
RN [6] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ALA-246.
RX PubMed=27927200; DOI=10.1186/s12915-016-0334-6;
RA McEwan D.L., Feinbaum R.L., Stroustrup N., Haas W., Conery A.L.,
RA Anselmo A., Sadreyev R., Ausubel F.M.;
RT "Tribbles ortholog NIPI-3 and bZIP transcription factor CEBP-1 regulate a
RT Caenorhabditis elegans intestinal immune surveillance pathway.";
RL BMC Biol. 14:105-105(2016).
RN [7] {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 [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH IMA-3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP SER-53; LEU-54; GLN-62; ARG-63; ASP-64 AND 162-LYS--ARG-169.
RX PubMed=31417366; DOI=10.3389/fncel.2019.00348;
RA Malinow R.A., Ying P., Koorman T., Boxem M., Jin Y., Kim K.W.;
RT "Functional Dissection of C. elegans bZip-Protein CEBP-1 Reveals Novel
RT Structural Motifs Required for Axon Regeneration and Nuclear Import.";
RL Front. Cell. Neurosci. 13:348-348(2019).
RN [9] {ECO:0000305}
RP FUNCTION, AND INDUCTION.
RX PubMed=31851340; DOI=10.1093/toxsci/kfz244;
RA Caito S.W., Newell-Caito J., Martell M., Crawford N., Aschner M.;
RT "Methylmercury Induces Metabolic Alterations in Caenorhabditis elegans:
RT Role for C/EBP Transcription Factor.";
RL Toxicol. Sci. 174:112-123(2020).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=34407394; DOI=10.1016/j.celrep.2021.109529;
RA Wu C., Karakuzu O., Garsin D.A.;
RT "Tribbles pseudokinase NIPI-3 regulates intestinal immunity in
RT Caenorhabditis elegans by controlling SKN-1/Nrf activity.";
RL Cell Rep. 36:109529-109529(2021).
CC -!- FUNCTION: Transcription factor (By similarity). Binds to promoter
CC regions of target genes, perhaps at the motif 5'-
CC [AGCT]TT[AGT][TC]GAAA[ACT]-3' (PubMed:27927209). Modulates expression
CC of genes involved in development and in stress responses, including
CC those regulating the p38/MAPK signaling pathways such as MAPKK sek-1
CC and phosphatase vhp-1 (PubMed:27927209, PubMed:34407394). Involved in
CC innate immunity (PubMed:27927200, PubMed:28662060, PubMed:34407394).
CC Plays a role in repressing the response to infection by the Gram-
CC negative bacterium P.aeruginosa, perhaps acting independently of the
CC pmk-1 or pmk-3 p38/MAPK pathways (PubMed:27927200). However, also plays
CC a protective role in the response to infection by P.aeruginosa
CC (PubMed:28662060). Required in axonal regrowth following injury and
CC synaptogenesis (PubMed:19737525, PubMed:31417366, PubMed:26484536).
CC Following axon injury, in concert with transcription factor ets-4,
CC activates expression of receptor tyrosine kinase svh-2
CC (PubMed:26484536). May function downstream of the Ca2+-activated
CC p38/MAPK pathway to promote axon regeneration (PubMed:26484536). Plays
CC a role in modulating polymerization of neuronal microtubules
CC (PubMed:21368137). Involved in modulating lipid homeostasis
CC (PubMed:31851340). {ECO:0000250|UniProtKB:P49716,
CC ECO:0000269|PubMed:19737525, ECO:0000269|PubMed:21368137,
CC ECO:0000269|PubMed:26484536, ECO:0000269|PubMed:27927200,
CC ECO:0000269|PubMed:27927209, ECO:0000269|PubMed:28662060,
CC ECO:0000269|PubMed:31417366, ECO:0000269|PubMed:31851340,
CC ECO:0000269|PubMed:34407394}.
CC -!- SUBUNIT: May interact with transcription factor ets-4
CC (PubMed:26484536). May interact (via N-terminus) with nipi-3
CC (PubMed:27927209). May interact (via N-terminus) with importin subunit
CC alpha ima-3 (PubMed:31417366). {ECO:0000269|PubMed:26484536,
CC ECO:0000269|PubMed:27927209, ECO:0000269|PubMed:31417366}.
CC -!- INTERACTION:
CC Q18909; H2L0N3: zip-4; NbExp=2; IntAct=EBI-326791, EBI-6777775;
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:19737525}. Cytoplasm
CC {ECO:0000269|PubMed:19737525}. Nucleus {ECO:0000269|PubMed:19737525,
CC ECO:0000269|PubMed:31417366}. Cell projection, axon
CC {ECO:0000269|PubMed:19737525}. Note=Localization to nucleus dependent
CC partially upon importin ima-3. {ECO:0000269|PubMed:31417366}.
CC -!- TISSUE SPECIFICITY: Expressed in touch and motor neurons.
CC {ECO:0000269|PubMed:19737525}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in most postembryonic tissues,
CC including epidermis, muscles, pharynx, intestine and neurons.
CC {ECO:0000269|PubMed:27927209}.
CC -!- INDUCTION: In response to methylmercury. {ECO:0000269|PubMed:31851340}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown suppresses lifespan
CC reduction caused by infection by the Gram-negative bacterium
CC P.aeruginosa when combined with simultaneous knockdown of nipi-3
CC (PubMed:27927200). Knockdown reduces survival due to infection by the
CC Gram-negative bacterium P.aeruginosa in a valine--tRNA ligase glp-4
CC mutant background (PubMed:28662060). {ECO:0000269|PubMed:27927200,
CC ECO:0000269|PubMed:28662060}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
CC -!- CAUTION: Plays a role in repressing the response to infection by the
CC Gram-negative bacterium P.aeruginosa (PubMed:27927200). However, is
CC also reported to play a protective role in the response to infection by
CC P.aeruginosa (PubMed:28662060). These differences may be due to
CC conditions of infection or perhaps genetic background.
CC {ECO:0000269|PubMed:27927200, ECO:0000269|PubMed:28662060,
CC ECO:0000305|PubMed:27927200, ECO:0000305|PubMed:28662060}.
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DR EMBL; BX284606; CCD68278.2; -; Genomic_DNA.
DR RefSeq; NP_508276.2; NM_075875.3.
DR SMR; Q18909; -.
DR DIP; DIP-25681N; -.
DR IntAct; Q18909; 3.
DR STRING; 6239.D1005.3; -.
DR EPD; Q18909; -.
DR PaxDb; Q18909; -.
DR PeptideAtlas; Q18909; -.
DR EnsemblMetazoa; D1005.3.1; D1005.3.1; WBGene00016997.
DR GeneID; 180481; -.
DR KEGG; cel:CELE_D1005.3; -.
DR UCSC; D1005.3; c. elegans.
DR CTD; 180481; -.
DR WormBase; D1005.3; CE47425; WBGene00016997; cebp-1.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000171291; -.
DR HOGENOM; CLU_075902_0_0_1; -.
DR InParanoid; Q18909; -.
DR OMA; YKMNCEV; -.
DR OrthoDB; 1436278at2759; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00016997; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0045202; C:synapse; 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:0031103; P:axon regeneration; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IMP:UniProtKB.
DR GO; GO:1905944; P:positive regulation of formation of growth cone in injured axon; IMP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IGI:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; IGI:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR046347; bZIP_sf.
DR SUPFAM; SSF57959; SSF57959; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Developmental protein; DNA-binding; Nucleus;
KW Reference proteome; Synapse; Transcription; Transcription regulation.
FT CHAIN 1..319
FT /note="CCAAT/enhancer-binding protein homolog 1"
FT /id="PRO_0000455762"
FT DOMAIN 233..308
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 53..67
FT /note="N' domain; required for axon regeneration"
FT /evidence="ECO:0000269|PubMed:31417366"
FT REGION 237..271
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 275..308
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MUTAGEN 53
FT /note="S->F: In ju1518; Suppresses developmental arrest in
FT a nipi-3 mutant background."
FT /evidence="ECO:0000269|PubMed:31417366"
FT MUTAGEN 54
FT /note="L->F: In ju1519; Suppresses developmental arrest in
FT a nipi-3 mutant background."
FT /evidence="ECO:0000269|PubMed:31417366"
FT MUTAGEN 62
FT /note="Missing: In ju1590; Blocks injury-induced axon
FT regrowth."
FT /evidence="ECO:0000269|PubMed:31417366"
FT MUTAGEN 63
FT /note="R->P: In ju634; Blocks injury-induced axon regrowth.
FT Suppresses developmental arrest in a nipi-3 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:31417366"
FT MUTAGEN 64
FT /note="D->N: In ju1521; Blocks injury-induced axon
FT regrowth. Suppresses developmental arrest in a nipi-3
FT mutant background."
FT /evidence="ECO:0000269|PubMed:31417366"
FT MUTAGEN 162..169
FT /note="KTRRAVKR->ATARAVAA: Abolishes interaction with ima-3
FT in vitro."
FT /evidence="ECO:0000269|PubMed:31417366"
FT MUTAGEN 246
FT /note="A->V: In ag33; Resistant to effects of toxin ToxA
FT from Gram-positive bacterium P.aeruginosa. Suppresses
FT lifespan reduction caused by P.aeruginosa in a nipi-3
FT mutant background."
FT /evidence="ECO:0000269|PubMed:27927200"
FT MUTAGEN 250
FT /note="S->L: In ju640; Suppresses neuronal defects in a E3
FT ubiquitin-protein ligase rpm-1 mutant background."
FT /evidence="ECO:0000269|PubMed:19737525"
FT MUTAGEN 251
FT /note="R->C: In ju659; Suppresses neuronal defects in a E3
FT ubiquitin-protein ligase rpm-1 mutant background."
FT /evidence="ECO:0000269|PubMed:19737525"
FT MUTAGEN 285
FT /note="A->V: In u819; Suppresses microtubule disruption in
FT touch receptor neurons caused by colchicine."
FT /evidence="ECO:0000269|PubMed:21368137"
SQ SEQUENCE 319 AA; 37076 MW; F0B03E47D4A912F5 CRC64;
MYSKLNYSHQ KGDQALKHPH LVRLQQSEVR GFTDMPNNGA STSSAGSFAR QDSLTIAASL
QQRDRERHPV DFMETELDLG DYLQVLHDLD VPTDNVDFDD AELQKCNILY DGEHPYEQPE
LNGYERHVAY GTGYRVPGDY DQDGYKMNCE VKAETPDFGA TKTRRAVKRP VPYDDYQKEY
SEESSDMTDN DGSVDDSYFE PKSKKTKSAG LENFKPQTRA RKYKLKADEE KAEPTYKLKR
ARNNDAVRKS RKKAKELQDK KEAEHDKMKR RIAELEGLLQ SERDARRRDQ DTLEQLLRNK
GPMKEQRMPQ RHILENFNK
