NFIL3_CAEEL
ID NFIL3_CAEEL Reviewed; 401 AA.
AC Q21361;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Transcription factor atf-2 {ECO:0000305};
DE AltName: Full=cAMP-dependent transcription factor atf-2 {ECO:0000312|WormBase:K08F8.2};
GN Name=atf-2 {ECO:0000312|WormBase:K08F8.2};
GN ORFNames=K08F8.2 {ECO:0000312|WormBase:K08F8.2};
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 PHOSPHORYLATION.
RX PubMed=11703092; DOI=10.1006/mcbr.2001.0300;
RA Berman K., McKay J., Avery L., Cobb M.;
RT "Isolation and characterization of pmk-(1-3): three p38 homologs in
RT Caenorhabditis elegans.";
RL Mol. Cell Biol. Res. Commun. 4:337-344(2001).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CES-2, AND DEVELOPMENTAL STAGE.
RX PubMed=16310763; DOI=10.1016/j.ydbio.2005.10.029;
RA Wang X., Jia H., Chamberlin H.M.;
RT "The bZip proteins CES-2 and ATF-2 alter the timing of transcription for a
RT cell-specific target gene in C. elegans.";
RL Dev. Biol. 289:456-465(2006).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=19686386; DOI=10.1111/j.1471-4159.2009.06323.x;
RA Janssen T., Husson S.J., Meelkop E., Temmerman L., Lindemans M.,
RA Verstraelen K., Rademakers S., Mertens I., Nitabach M., Jansen G.,
RA Schoofs L.;
RT "Discovery and characterization of a conserved pigment dispersing factor-
RT like neuropeptide pathway in Caenorhabditis elegans.";
RL J. Neurochem. 111:228-241(2009).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=21502138; DOI=10.1242/jcs.080192;
RA Erdelyi P., Borsos E., Takacs-Vellai K., Kovacs T., Kovacs A.L.,
RA Sigmond T., Hargitai B., Pasztor L., Sengupta T., Dengg M., Pecsi I.,
RA Toth J., Nilsen H., Vertessy B.G., Vellai T.;
RT "Shared developmental roles and transcriptional control of autophagy and
RT apoptosis in Caenorhabditis elegans.";
RL J. Cell Sci. 124:1510-1518(2011).
CC -!- FUNCTION: Acts as a transcription factor that recognizes and binds to
CC the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many
CC promoters (PubMed:16310763, PubMed:21502138). Involved in the
CC development of the excretory duct cell, by positively modulating
CC embryonic transcription of putative transcription factor lin-48, acting
CC in concert with cell death specification protein ces-2
CC (PubMed:16310763). Negatively modulates expression of key autophagy-
CC related genes, bec-1/ATG6 and lgg-1/ATG8, and may link together
CC autophagy and apoptosis during development (PubMed:21502138).
CC Positively modulates expression of neuropeptide pigment dispersing
CC factor homologs pdf-1 and pdf-2 (PubMed:19686386).
CC {ECO:0000269|PubMed:16310763, ECO:0000269|PubMed:19686386,
CC ECO:0000269|PubMed:21502138}.
CC -!- SUBUNIT: Interacts with cell death specification protein ces-2.
CC {ECO:0000269|PubMed:16310763}.
CC -!- INTERACTION:
CC Q21361; O16213: atf-8; NbExp=2; IntAct=EBI-317743, EBI-6735245;
CC Q21361; Q8IG69: cebp-2; NbExp=2; IntAct=EBI-317743, EBI-2914231;
CC Q21361; Q94126: ces-2; NbExp=4; IntAct=EBI-317743, EBI-328155;
CC Q21361; P92004: tag-260; NbExp=3; IntAct=EBI-317743, EBI-316398;
CC Q21361; Q21148: zip-2; NbExp=2; IntAct=EBI-317743, EBI-6731556;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expression begins in the embryo and persists into
CC larval and adult stages (PubMed:16310763). Expressed in the excretory
CC duct cell, as well as other cells, at larval L3 stage
CC (PubMed:16310763). {ECO:0000269|PubMed:16310763}.
CC -!- PTM: Phosphorylated by mitogen-activated protein kinases pmk-2 and pmk-
CC 3 (PubMed:11703092). May be responsive to osmotic stress
CC (PubMed:11703092). {ECO:0000269|PubMed:11703092}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284602; CAA91284.1; -; Genomic_DNA.
DR PIR; T23490; T23490.
DR RefSeq; NP_495861.1; NM_063460.3.
DR AlphaFoldDB; Q21361; -.
DR SMR; Q21361; -.
DR DIP; DIP-25386N; -.
DR IntAct; Q21361; 21.
DR STRING; 6239.K08F8.2; -.
DR EPD; Q21361; -.
DR PaxDb; Q21361; -.
DR EnsemblMetazoa; K08F8.2.1; K08F8.2.1; WBGene00000220.
DR GeneID; 174399; -.
DR KEGG; cel:CELE_K08F8.2; -.
DR UCSC; K08F8.2; c. elegans.
DR CTD; 37978; -.
DR WormBase; K08F8.2; CE03468; WBGene00000220; atf-2.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000169039; -.
DR HOGENOM; CLU_687426_0_0_1; -.
DR InParanoid; Q21361; -.
DR OMA; MIMEQKL; -.
DR OrthoDB; 1215059at2759; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000220; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 2.
DR SMART; SM00338; BRLZ; 2.
DR SUPFAM; SSF57959; SSF57959; 2.
DR PROSITE; PS50217; BZIP; 2.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..401
FT /note="Transcription factor atf-2"
FT /id="PRO_0000454187"
FT DOMAIN 54..100
FT /note="bZIP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT DOMAIN 329..392
FT /note="bZIP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 19..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..85
FT /note="Basic motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 89..96
FT /note="Leucine-zipper 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 181..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..360
FT /note="Basic motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 364..378
FT /note="Leucine-zipper 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COILED 361..388
FT /evidence="ECO:0000255"
FT COMPBIAS 19..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43836 MW; 74FCFBA375FBE7B3 CRC64;
MDVDSASLSP SSRLSVVCSA SAEFSSSSSD SSNFSEGSPP ESRRNSVNES VIKDEHYWER
RRRNNDASRR SREKRRQNDL AMEEKIMLLS AENERLKSQL GTTPIPQPSV TEPPTSLIIP
QVAKNLFPAG PIASLQASSM LTVPLLQAAS HIPSMLQLCQ LQPTTIQSPV YASTQQPAST
SASSLFSSSS SSAFHPFRPS ESAQQSFPSS SVIVKIERRS PDSSTDVNMP QPQLQPGSSV
IQQIGQPAPS GTPQPVIQAV QQGPSLLSAL LSQRRPSPTV PQSRTEHISG LNSPPRHTGN
KSDCESVSSS ASFSPSHSSE DHSNYSNKSP QYVDRRRRNN EAAKRCRANR RAVFEYRSRR
VQLLEGENED LRTQIETLKA EIAHFKSVLA QRASVVTALH P
