DAF12_CAEEL
ID DAF12_CAEEL Reviewed; 753 AA.
AC G5EFF5; G5EBZ6; G5EG55; Q2XN07;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Nuclear hormone receptor family member daf-12 {ECO:0000305};
DE AltName: Full=Abnormal dauer formation protein 12 {ECO:0000312|WormBase:F11A1.3a};
GN Name=daf-12 {ECO:0000312|WormBase:F11A1.3a};
GN Synonyms=daf-20 {ECO:0000312|WormBase:F11A1.3a},
GN mig-7 {ECO:0000312|WormBase:F11A1.3a},
GN XL285 {ECO:0000312|WormBase:F11A1.3a};
GN ORFNames=F11A1.3 {ECO:0000312|WormBase:F11A1.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAD34462.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF ARG-143.
RX PubMed=11072073; DOI=10.1016/s0167-4781(00)00224-4;
RA Snow M.I., Larsen P.L.;
RT "Structure and expression of daf-12: a nuclear hormone receptor with three
RT isoforms that are involved in development and aging in Caenorhabditis
RT elegans.";
RL Biochim. Biophys. Acta 1494:104-116(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF CYS-121; ALA-125; SER-137; ARG-143; ARG-197; CYS-461;
RP MET-562; ARG-564; GLY-582 AND PRO-746.
RX PubMed=10859169;
RA Antebi A., Yeh W.H., Tait D., Hedgecock E.M., Riddle D.L.;
RT "daf-12 encodes a nuclear receptor that regulates the dauer diapause and
RT developmental age in C. elegans.";
RL Genes Dev. 14:1512-1527(2000).
RN [3] {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 [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9477318; DOI=10.1242/dev.125.7.1191;
RA Antebi A., Culotti J.G., Hedgecock E.M.;
RT "daf-12 regulates developmental age and the dauer alternative in
RT Caenorhabditis elegans.";
RL Development 125:1191-1205(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH DIN-1.
RX PubMed=15314028; DOI=10.1101/gad.312604;
RA Ludewig A.H., Kober-Eisermann C., Weitzel C., Bethke A., Neubert K.,
RA Gerisch B., Hutter H., Antebi A.;
RT "A novel nuclear receptor/coregulator complex controls C. elegans lipid
RT metabolism, larval development, and aging.";
RL Genes Dev. 18:2120-2133(2004).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=15489294; DOI=10.1101/gad.1218504;
RA Shostak Y., Van Gilst M.R., Antebi A., Yamamoto K.R.;
RT "Identification of C. elegans DAF-12-binding sites, response elements, and
RT target genes.";
RL Genes Dev. 18:2529-2544(2004).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15383841; DOI=10.1371/journal.pbio.0020280;
RA Matyash V., Entchev E.V., Mende F., Wilsch-Brauninger M., Thiele C.,
RA Schmidt A.W., Knolker H.J., Ward S., Kurzchalia T.V.;
RT "Sterol-derived hormone(s) controls entry into diapause in Caenorhabditis
RT elegans by consecutive activation of DAF-12 and DAF-16.";
RL PLoS Biol. 2:E280-E280(2004).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND
RP MUTAGENESIS OF CYS-121; ALA-125; SER-137; ARG-143; ARG-196 AND ARG-197.
RX PubMed=15611047; DOI=10.1074/jbc.m412928200;
RA Shostak Y., Yamamoto K.R.;
RT "Overlapping but separable determinants of DNA binding and nuclear
RT localization map to the C-terminal end of the Caenorhabditis elegans DAF-12
RT DNA binding domain.";
RL J. Biol. Chem. 280:6554-6560(2005).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16626392; DOI=10.1111/j.1474-9726.2006.00203.x;
RA Fisher A.L., Lithgow G.J.;
RT "The nuclear hormone receptor DAF-12 has opposing effects on Caenorhabditis
RT elegans lifespan and regulates genes repressed in multiple long-lived
RT worms.";
RL Aging Cell 5:127-138(2006).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=16529801; DOI=10.1016/j.cell.2006.01.037;
RA Motola D.L., Cummins C.L., Rottiers V., Sharma K.K., Li T., Li Y.,
RA Suino-Powell K., Xu H.E., Auchus R.J., Antebi A., Mangelsdorf D.J.;
RT "Identification of ligands for DAF-12 that govern dauer formation and
RT reproduction in C. elegans.";
RL Cell 124:1209-1223(2006).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=18436204; DOI=10.1016/j.ydbio.2008.03.019;
RA Dixon S.J., Alexander M., Chan K.K., Roy P.J.;
RT "Insulin-like signaling negatively regulates muscle arm extension through
RT DAF-12 in Caenorhabditis elegans.";
RL Dev. Biol. 318:153-161(2008).
RN [12]
RP FUNCTION.
RX PubMed=19828440; DOI=10.1073/pnas.0908131106;
RA Hammell C.M., Karp X., Ambros V.;
RT "A feedback circuit involving let-7-family miRNAs and DAF-12 integrates
RT environmental signals and developmental timing in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18668-18673(2009).
RN [13]
RP FUNCTION.
RX PubMed=21471153; DOI=10.1242/dev.057109;
RA Huang X., Zhang H., Zhang H.;
RT "The zinc-finger protein SEA-2 regulates larval developmental timing and
RT adult lifespan in C. elegans.";
RL Development 138:2059-2068(2011).
RN [14]
RP FUNCTION.
RX PubMed=21814518; DOI=10.1371/journal.pgen.1002179;
RA Hochbaum D., Zhang Y., Stuckenholz C., Labhart P., Alexiadis V., Martin R.,
RA Knolker H.J., Fisher A.L.;
RT "DAF-12 regulates a connected network of genes to ensure robust
RT developmental decisions.";
RL PLoS Genet. 7:E1002179-E1002179(2011).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23990780; DOI=10.1371/journal.ppat.1003545;
RA Liu F., He C.X., Luo L.J., Zou Q.L., Zhao Y.X., Saini R., Han S.F.,
RA Knolker H.J., Wang L.S., Ge B.X.;
RT "Nuclear hormone receptor regulation of microRNAs controls innate immune
RT responses in C. elegans.";
RL PLoS Pathog. 9:E1003545-E1003545(2013).
RN [16]
RP FUNCTION.
RX PubMed=24957743; DOI=10.1007/s12263-014-0414-6;
RA Fischer M., Fitzenberger E., Kull R., Boll M., Wenzel U.;
RT "The zinc matrix metalloproteinase ZMP-2 increases survival of
RT Caenorhabditis elegans through interference with lipoprotein absorption.";
RL Genes Nutr. 9:414-414(2014).
RN [17]
RP FUNCTION.
RX PubMed=25774872; DOI=10.1371/journal.pgen.1005027;
RA Wang Z., Stoltzfus J., You Y.J., Ranjit N., Tang H., Xie Y., Lok J.B.,
RA Mangelsdorf D.J., Kliewer S.A.;
RT "The nuclear receptor DAF-12 regulates nutrient metabolism and reproductive
RT growth in nematodes.";
RL PLoS Genet. 11:E1005027-E1005027(2015).
CC -!- FUNCTION: Nuclear receptor which binds directly to response elements in
CC target gene promoters (PubMed:9477318, PubMed:10859169,
CC PubMed:15314028, PubMed:15489294, PubMed:15383841, PubMed:15611047,
CC PubMed:16626392, PubMed:19828440, PubMed:21814518). Activity is
CC modulated by binding of steroid hormone ligands that include
CC dafachronic acids (PubMed:16529801). Regulates expression of genes
CC involved in postembryonic development and the dauer diapause, in
CC response to environmental cues (PubMed:9477318, PubMed:10859169,
CC PubMed:15489294, PubMed:15383841, PubMed:16626392, PubMed:19828440,
CC PubMed:21814518). Inhibits the expression of let-7 family members when
CC bound to corepressor din-1s which is an isoform of din-1
CC (PubMed:19828440). Plays a role in controlling the timing of seam cell
CC development during the larval stages (PubMed:21471153). Has a role in
CC the immune response to bacterial infection, via regulation of let-7
CC miRNAs (PubMed:23990780). Controls expression of genes that promote the
CC aerobic catabolism of fatty acids for reproductive growth
CC (PubMed:25774872). May be involved in thermotolerance
CC (PubMed:24957743). {ECO:0000269|PubMed:10859169,
CC ECO:0000269|PubMed:15314028, ECO:0000269|PubMed:15383841,
CC ECO:0000269|PubMed:15489294, ECO:0000269|PubMed:15611047,
CC ECO:0000269|PubMed:16529801, ECO:0000269|PubMed:16626392,
CC ECO:0000269|PubMed:19828440, ECO:0000269|PubMed:21471153,
CC ECO:0000269|PubMed:21814518, ECO:0000269|PubMed:23990780,
CC ECO:0000269|PubMed:24957743, ECO:0000269|PubMed:25774872,
CC ECO:0000269|PubMed:9477318}.
CC -!- SUBUNIT: Interacts with din-1 isoform d. {ECO:0000269|PubMed:15314028}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:10859169, ECO:0000269|PubMed:15611047,
CC ECO:0000269|PubMed:23990780}. Note=Diffuse expression during mitosis
CC (PubMed:10859169). Increased nuclear accumulation upon infection by
CC E.coli (PubMed:23990780). {ECO:0000269|PubMed:10859169,
CC ECO:0000269|PubMed:23990780}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=a {ECO:0000312|WormBase:F11A1.3a}; Synonyms=A1
CC {ECO:0000303|PubMed:11072073};
CC IsoId=G5EFF5-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F11A1.3b}; Synonyms=A2
CC {ECO:0000303|PubMed:11072073};
CC IsoId=G5EFF5-2; Sequence=VSP_057859;
CC Name=c {ECO:0000312|WormBase:F11A1.3c}; Synonyms=B
CC {ECO:0000303|PubMed:11072073};
CC IsoId=G5EFF5-3; Sequence=VSP_057858;
CC Name=d {ECO:0000312|WormBase:F11A1.3d};
CC IsoId=G5EFF5-4; Sequence=VSP_057860;
CC -!- TISSUE SPECIFICITY: Expressed throughout muscles of the pharynx
CC (PubMed:11072073). Expressed in epidermal seam cells, the vulva, head
CC neurons, mature spermatheca, uterus and intestine (PubMed:10859169,
CC PubMed:23990780). {ECO:0000269|PubMed:10859169,
CC ECO:0000269|PubMed:11072073, ECO:0000269|PubMed:23990780}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed from embryo through to adult
CC stages; peak expression levels seem to occur during larval stage L2.
CC {ECO:0000269|PubMed:10859169}.
CC -!- DISRUPTION PHENOTYPE: Reduced lifespan associated with accelerated
CC aging and increased tissue deterioration (PubMed:16626392). Defective
CC dauer formation (PubMed:9477318, PubMed:10859169). In the absence of
CC cholesterol, arrest with abnormal cuticle formation (PubMed:15383841).
CC Increased resistance to P.aeruginosa infection possibly due to elevated
CC expression of antimicrobial genes (PubMed:23990780). Prevents increase
CC in the number of muscle arm extension in a daf-2 (e1375) background
CC (PubMed:18436204). RNAi-mediated knockdown results in reduced lifespan,
CC but increased resistance to bacterial infection (PubMed:23990780).
CC {ECO:0000269|PubMed:10859169, ECO:0000269|PubMed:15383841,
CC ECO:0000269|PubMed:16626392, ECO:0000269|PubMed:18436204,
CC ECO:0000269|PubMed:23990780, ECO:0000269|PubMed:9477318}.
CC -!- MISCELLANEOUS: [Isoform b]: Produced by alternative initiation at Met-
CC 60 of isoform a. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform c]: Produced by alternative initiation at Met-
CC 487 of isoform a. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform d]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
CC {ECO:0000255|RuleBase:RU000377}.
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DR EMBL; AF136238; AAD34462.1; -; mRNA.
DR EMBL; AF136239; AAD34463.1; -; mRNA.
DR EMBL; AF136240; AAD34464.1; -; mRNA.
DR EMBL; BX284606; CAC42283.1; -; Genomic_DNA.
DR EMBL; BX284606; CAC42284.1; -; Genomic_DNA.
DR EMBL; BX284606; CAC42285.1; -; Genomic_DNA.
DR EMBL; BX284606; CAJ43436.1; -; Genomic_DNA.
DR RefSeq; NP_001024547.1; NM_001029376.4. [G5EFF5-1]
DR RefSeq; NP_001024548.1; NM_001029377.3.
DR RefSeq; NP_001024549.1; NM_001029378.1.
DR RefSeq; NP_001041239.1; NM_001047774.2. [G5EFF5-4]
DR AlphaFoldDB; G5EFF5; -.
DR SMR; G5EFF5; -.
DR IntAct; G5EFF5; 2.
DR STRING; 6239.F11A1.3a; -.
DR BindingDB; G5EFF5; -.
DR PaxDb; G5EFF5; -.
DR PeptideAtlas; G5EFF5; -.
DR PRIDE; G5EFF5; -.
DR EnsemblMetazoa; F11A1.3a.1; F11A1.3a.1; WBGene00000908. [G5EFF5-1]
DR EnsemblMetazoa; F11A1.3b.1; F11A1.3b.1; WBGene00000908. [G5EFF5-2]
DR EnsemblMetazoa; F11A1.3c.1; F11A1.3c.1; WBGene00000908. [G5EFF5-3]
DR EnsemblMetazoa; F11A1.3d.1; F11A1.3d.1; WBGene00000908. [G5EFF5-4]
DR GeneID; 181263; -.
DR KEGG; cel:CELE_F11A1.3; -.
DR UCSC; F11A1.3a; c. elegans.
DR CTD; 181263; -.
DR WormBase; F11A1.3a; CE27584; WBGene00000908; daf-12. [G5EFF5-1]
DR WormBase; F11A1.3b; CE27585; WBGene00000908; daf-12. [G5EFF5-2]
DR WormBase; F11A1.3c; CE27586; WBGene00000908; daf-12. [G5EFF5-3]
DR WormBase; F11A1.3d; CE39240; WBGene00000908; daf-12. [G5EFF5-4]
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; G5EFF5; -.
DR OMA; LMNEEEP; -.
DR OrthoDB; 297114at2759; -.
DR PhylomeDB; G5EFF5; -.
DR Reactome; R-CEL-159418; Recycling of bile acids and salts.
DR Reactome; R-CEL-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-CEL-4090294; SUMOylation of intracellular receptors.
DR SignaLink; G5EFF5; -.
DR PRO; PR:G5EFF5; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000908; Expressed in larva and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:1902051; F:(25S)-Delta(4)-dafachronate binding; IDA:WormBase.
DR GO; GO:1902052; F:(25S)-Delta(7)-dafachronate binding; IDA:WormBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:WormBase.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:WormBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007568; P:aging; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IGI:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR GO; GO:0010286; P:heat acclimation; IGI:UniProtKB.
DR GO; GO:0060179; P:male mating behavior; IMP:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061066; P:positive regulation of dauer larval development; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0061065; P:regulation of dauer larval development; IGI:UniProtKB.
DR GO; GO:0040034; P:regulation of development, heterochronic; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; Developmental protein;
KW DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..753
FT /note="Nuclear hormone receptor family member daf-12"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433989"
FT DOMAIN 516..753
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 115..190
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 118..138
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 154..173
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 191..206
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:15611047"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..486
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057858"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057859"
FT VAR_SEQ 1..57
FT /note="MGTNGGVIAEQSMEIETNENPDKVEEPVVRRKRVTRRRHRRIHSKNNCLTPP
FT NSDDD -> MADNLLSSQNYINWTMLNKFYGK (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_057860"
FT MUTAGEN 121
FT /note="C->Y: In sa156; no transcriptional activity in
FT vitro. Defective dauer formation."
FT /evidence="ECO:0000269|PubMed:10859169,
FT ECO:0000269|PubMed:15611047"
FT MUTAGEN 125
FT /note="A->V: In m420; no transcriptional activity in vitro.
FT Defective dauer formation."
FT /evidence="ECO:0000269|PubMed:10859169,
FT ECO:0000269|PubMed:15611047"
FT MUTAGEN 137
FT /note="S->F: In m421; no transcriptional activity in vitro.
FT Defective dauer formation."
FT /evidence="ECO:0000269|PubMed:10859169,
FT ECO:0000269|PubMed:15611047"
FT MUTAGEN 143
FT /note="R->K: In m116 and m423; no transcriptional activity
FT in vitro. Defective dauer formation."
FT /evidence="ECO:0000269|PubMed:10859169,
FT ECO:0000269|PubMed:11072073, ECO:0000269|PubMed:15611047"
FT MUTAGEN 195
FT /note="R->A: Defective nuclear localization; when
FT associated with A-198."
FT /evidence="ECO:0000269|PubMed:15611047"
FT MUTAGEN 196
FT /note="R->A: Defective nuclear localization; when
FT associated with A-198."
FT /evidence="ECO:0000269|PubMed:15611047"
FT MUTAGEN 196
FT /note="R->K: Small reduction in DNA binding in vitro."
FT /evidence="ECO:0000269|PubMed:15611047"
FT MUTAGEN 197
FT /note="R->A: Severely reduced DNA binding and reduced
FT transcriptional activity in vitro."
FT /evidence="ECO:0000269|PubMed:15611047"
FT MUTAGEN 197
FT /note="R->K: In m424; reduced DNA binding affinity and
FT transcriptional activity in vitro. Defective dauer
FT formation."
FT /evidence="ECO:0000269|PubMed:10859169,
FT ECO:0000269|PubMed:15611047"
FT MUTAGEN 198
FT /note="K->A: Defective nuclear localization; when
FT associated with A-195 or A-196."
FT /evidence="ECO:0000269|PubMed:15611047"
FT MUTAGEN 461
FT /note="C->Y: In rh286; mild gonadal heterochrony."
FT /evidence="ECO:0000269|PubMed:10859169"
FT MUTAGEN 562
FT /note="M->I: In m25; defective dauer formation."
FT /evidence="ECO:0000269|PubMed:10859169"
FT MUTAGEN 564
FT /note="R->C: In rh62 and rh274; dauer-constitutive
FT phenotype with gonadal heterochrony."
FT /evidence="ECO:0000269|PubMed:10859169"
FT MUTAGEN 564
FT /note="R->H: In rh273; dauer-constitutive phenotype with
FT gonadal heterochrony."
FT /evidence="ECO:0000269|PubMed:10859169"
FT MUTAGEN 582
FT /note="G->K: In rh193; temperature sensitive mutant."
FT /evidence="ECO:0000269|PubMed:10859169"
FT MUTAGEN 746
FT /note="P->S: In rh284; temperature sensitive mutation that
FT prevents transcriptional activity and with gonadal
FT heterochrony."
FT /evidence="ECO:0000269|PubMed:10859169,
FT ECO:0000269|PubMed:21814518"
SQ SEQUENCE 753 AA; 84199 MW; BD166E3A0ED95D08 CRC64;
MGTNGGVIAE QSMEIETNEN PDKVEEPVVR RKRVTRRRHR RIHSKNNCLT PPNSDDDPQM
STPDDPVIHS PPSIGAAPGM NGYHGSGVKL EESSGACGSP DDGLLDSSEE SRRRQKTCRV
CGDHATGYNF NVITCESCKA FFRRNALRPK EFKCPYSEDC EINSVSRRFC QKCRLRKCFT
VGMKKEWILN EEQLRRRKNS RLNNTGTCNK RSQPGNQQSP QGPNQQPHLS PHHPGVAIYP
PQPQRPLTIN PMDNQMMHHM QANRPNAMPQ LISPPGAQPY PLTSPVGSSA SDSPPNRSLT
MMHNGEKSPD GYDPNIMAHR APPPSFNNRP KMDSGQVVLS TEEYKQLLSR IPGAQVPGLM
NEEEPINKRA AYNCNGHPMP AETTPPYSAP MSDMSLSRHN STSSGTEKNH MTHSTVSAIP
GNSAQNHFDI ASFGMGIVTA TGGGDAAEEM YKRMNMFYEN CIQSALDSPE NQEPKPQEAM
IPKEEYMTPT HGFQYQSDPY QVPPAERNIN YQLNAAELKA LDAVREAFYG MDDPMEQGRQ
MQSFLKANKT PADIMNIMDV TMRRFVKVAK GVPAFREVSQ EGKFSLLKGG MIEMLTVRGV
TRYDASTNSF KTPTIKGQNV SVNVDDMFAK LNANAQAQKA KCLEFFGFFD EEIKKNELAV
YLVMLAVLFS VRSDPPMNEN DVRIVTERHN HFMSLLNRYL ESLFGEQARR IFERIPKALG
LLNEIARNAG MLFMGTVRSG EAEELPGEFF KIK
