NH114_CAEEL
ID NH114_CAEEL Reviewed; 418 AA.
AC G5EEM0; A0A168HAV7; Q86PI7;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Nuclear hormone receptor 114 {ECO:0000312|WormBase:Y45G5AM.1a};
GN Name=nhr-114 {ECO:0000312|WormBase:Y45G5AM.1a};
GN ORFNames=Y45G5AM.1 {ECO:0000312|WormBase:Y45G5AM.1a};
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|EMBL:AAO27833.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18629017; DOI=10.1002/cfg.318;
RA Cuppen E., van der Linden A.M., Jansen G., Plasterk R.H.;
RT "Proteins interacting with Caenorhabditis elegans Galpha subunits.";
RL Comp. Funct. Genomics 4:479-491(2003).
RN [2] {ECO:0000312|EMBL:AAO39202.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15983867; DOI=10.1007/s00239-004-0175-8;
RA Robinson-Rechavi M., Maina C.V., Gissendanner C.R., Laudet V., Sluder A.;
RT "Explosive lineage-specific expansion of the orphan nuclear receptor HNF4
RT in nematodes.";
RL J. Mol. Evol. 60:577-586(2005).
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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23499532; DOI=10.1016/j.cub.2013.02.034;
RA Gracida X., Eckmann C.R.;
RT "Fertility and germline stem cell maintenance under different diets
RT requires nhr-114/HNF4 in C. elegans.";
RL Curr. Biol. 23:607-613(2013).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=33016879; DOI=10.7554/elife.60259;
RA Giese G.E., Walker M.D., Ponomarova O., Zhang H., Li X., Minevich G.,
RA Walhout A.J.;
RT "C. elegans methionine/S-adenosylmethionine cycle activity is sensed and
RT adjusted by a nuclear hormone receptor.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Probable transcription factor which may have a role in
CC detoxifying dietary metabolites arising from bacterial tryptophan
CC metabolism (PubMed:23499532). Required for fertility and involved in
CC proper postembryonic germline development, especially germline stem
CC cell (GSC) proliferation (PubMed:23499532). Required for activation of
CC the methionine/S-adenosylmethionine (Met/SAM) cycle in response to low
CC levels of SAM (PubMed:33016879). {ECO:0000269|PubMed:23499532,
CC ECO:0000269|PubMed:33016879}.
CC -!- INTERACTION:
CC G5EEM0; Q9XTB2: gpa-13; NbExp=3; IntAct=EBI-315855, EBI-6094254;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU004334,
CC ECO:0000269|PubMed:18629017, ECO:0000269|PubMed:23499532}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y45G5AM.1a};
CC IsoId=G5EEM0-1; Sequence=Displayed;
CC Name=d {ECO:0000312|WormBase:Y45G5AM.1d};
CC IsoId=G5EEM0-2; Sequence=VSP_060919;
CC -!- TISSUE SPECIFICITY: Expressed in germ and intestinal cells and at low
CC levels in the hypodermis. {ECO:0000269|PubMed:18629017,
CC ECO:0000269|PubMed:23499532}.
CC -!- DEVELOPMENTAL STAGE: First expressed in the embryo and subsequently in
CC larvae and adults. {ECO:0000269|PubMed:23499532}.
CC -!- DISRUPTION PHENOTYPE: No obvious somatic morphological defects in
CC adults (PubMed:23499532). However, shows diet-sensitive sterility
CC arising from germ-cell proliferation defects (PubMed:23499532). Sterile
CC when fed the standard bacterial strain, E.coli B (OP50) as food source,
CC and fertile when maintained on E.coli K-12 strains or bacterial soil
CC isolates (PubMed:23499532). Dietary supplementation of L-tryptophan,
CC but not the D isomer, to E.coli B strains suppresses sterility; this
CC effect requires live bacteria (PubMed:23499532). Sterility when fed
CC E.coli B strain OP50 can be rescued by dietary supplementation of
CC either vitamin B12, methionine or choline (PubMed:33016879). RNAi-
CC mediated knockdown targeted to the intestine, but not the germline,
CC restored almost normal fertility on an E.coli OP50 diet
CC (PubMed:23499532). RNAi-mediated knockdown on a rrf-1 mutant
CC background, in which knockdown occurs mainly in the germline but occurs
CC only weakly in somatic tissues, allowed recovery of a majority (64%) of
CC fertile animals (PubMed:23499532). RNAi-mediated knockdown on an nhr-10
CC mutant background suppresses expression of acdh-1 (PubMed:33016879).
CC {ECO:0000269|PubMed:23499532, ECO:0000269|PubMed:33016879}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
CC {ECO:0000255|RuleBase:RU004334}.
CC -!- CAUTION: It has been reported that mutant phenotypes can be rescued by
CC tryptophan dietary supplementation, but not by methionine
CC (PubMed:23499532). However, a later report describes successful
CC phenotype rescue by methionine supplementation; this may be due to
CC methodological differences (PubMed:33016879).
CC {ECO:0000269|PubMed:23499532, ECO:0000269|PubMed:33016879}.
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DR EMBL; AF408754; AAO27833.1; -; mRNA.
DR EMBL; AY204201; AAO39202.1; -; mRNA.
DR EMBL; BX284605; CCD74319.1; -; Genomic_DNA.
DR EMBL; BX284605; SAP35607.1; -; Genomic_DNA.
DR RefSeq; NP_001024242.1; NM_001029071.2. [G5EEM0-1]
DR RefSeq; NP_001317845.1; NM_001330839.1. [G5EEM0-2]
DR AlphaFoldDB; G5EEM0; -.
DR SMR; G5EEM0; -.
DR IntAct; G5EEM0; 78.
DR STRING; 6239.Y45G5AM.1a.2; -.
DR PaxDb; G5EEM0; -.
DR EnsemblMetazoa; Y45G5AM.1a.1; Y45G5AM.1a.1; WBGene00003704. [G5EEM0-1]
DR EnsemblMetazoa; Y45G5AM.1d.1; Y45G5AM.1d.1; WBGene00003704. [G5EEM0-2]
DR GeneID; 178821; -.
DR KEGG; cel:CELE_Y45G5AM.1; -.
DR CTD; 178821; -.
DR WormBase; Y45G5AM.1a; CE33735; WBGene00003704; nhr-114.
DR WormBase; Y45G5AM.1d; CE51628; WBGene00003704; nhr-114.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00970000196356; -.
DR InParanoid; G5EEM0; -.
DR OMA; SRDHVCL; -.
DR OrthoDB; 622732at2759; -.
DR PhylomeDB; G5EEM0; -.
DR SignaLink; G5EEM0; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003704; Expressed in larva and 7 other tissues.
DR ExpressionAtlas; G5EEM0; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IMP:UniProtKB.
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; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
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 splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..418
FT /note="Nuclear hormone receptor 114"
FT /id="PRO_0000452183"
FT DOMAIN 170..409
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 12..87
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 15..35
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 51..70
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 89..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..409
FT /note="AF-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT COMPBIAS 93..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..286
FT /note="MTPQSSPSSSRDHVCLVCQDFASGYHYGVPSCVGCKTFFRRTIMKKQKYICQ
FT FEGNCPVDKTIRCACRYCRFEKCLSVGMDRNALQQNRDPIGYTKRTRRPKKELKTTSDC
FT SSDEGASTPPSVSPLQLSPPPISPLLFQAAPLKPRRCILQTLAEREKCANDLRLSEYLP
FT IRSLHEALCSKALLNDTAFLEKWGQPSERHQIFDLRFVNHDDYHYWHERDWFLLTEYAK
FT TFDVFEALDYQDKAELVRHAAITVPVLVQVWNSPDYGPDTIVFPDGAYFDRTPEPTR
FT -> MVPTSIVLQSQ (in isoform d)"
FT /id="VSP_060919"
FT CONFLICT 1..9
FT /note="Missing (in Ref. 2; AAO39202)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="Q -> R (in Ref. 2; AAO39202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 47859 MW; 94400687A542EFD6 CRC64;
MTPQSSPSSS RDHVCLVCQD FASGYHYGVP SCVGCKTFFR RTIMKKQKYI CQFEGNCPVD
KTIRCACRYC RFEKCLSVGM DRNALQQNRD PIGYTKRTRR PKKELKTTSD CSSDEGASTP
PSVSPLQLSP PPISPLLFQA APLKPRRCIL QTLAEREKCA NDLRLSEYLP IRSLHEALCS
KALLNDTAFL EKWGQPSERH QIFDLRFVNH DDYHYWHERD WFLLTEYAKT FDVFEALDYQ
DKAELVRHAA ITVPVLVQVW NSPDYGPDTI VFPDGAYFDR TPEPTRPAGL NRKKYQMLDL
VLKPFRDLQL DATEFAAFKA VTFLNPDADI SLPARKLVNN ERVRITKQLY GYMAMKDDVD
TAIERFARLV LMGTSMSKMA CESKEAVWIA DFFENIGFSA FARQLFFGDT TSVVAHKL
