NHR40_CAEEL
ID NHR40_CAEEL Reviewed; 450 AA.
AC Q22127; Q8MPY4; Q9GTH6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Nuclear hormone receptor family member nhr-40;
GN Name=nhr-40 {ECO:0000312|WormBase:T03G6.2c};
GN ORFNames=T03G6.2 {ECO:0000312|WormBase:T03G6.2c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16920335; DOI=10.1016/j.mod.2006.06.006;
RA Brozova E., Simeckova K., Kostrouch Z., Rall J.E., Kostrouchova M.;
RT "NHR-40, a Caenorhabditis elegans supplementary nuclear receptor, regulates
RT embryonic and early larval development.";
RL Mech. Dev. 123:689-701(2006).
RN [4]
RP FUNCTION.
RX PubMed=18616929; DOI=10.1016/j.bbrc.2008.06.115;
RA Pohludka M., Simeckova K., Vohanka J., Yilma P., Novak P., Krause M.W.,
RA Kostrouchova M., Kostrouch Z.;
RT "Proteomic analysis uncovers a metabolic phenotype in C. elegans after nhr-
RT 40 reduction of function.";
RL Biochem. Biophys. Res. Commun. 374:49-54(2008).
CC -!- FUNCTION: Orphan nuclear receptor (Probable). Plays a role in
CC morphogenesis and elongation during embryonic and larval development
CC (PubMed:16920335). Plays a role in muscle formation and motility
CC (PubMed:16920335, PubMed:18616929). {ECO:0000269|PubMed:16920335,
CC ECO:0000269|PubMed:18616929, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=c {ECO:0000312|WormBase:T03G6.2c}; Synonyms=d
CC {ECO:0000303|PubMed:16920335};
CC IsoId=Q22127-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T03G6.2b};
CC IsoId=Q22127-3; Sequence=VSP_003726;
CC -!- TISSUE SPECIFICITY: Isoform b: Expressed in body wall muscle cells,
CC pharyngeal muscles, rectal gland cells, vulval and uterine muscles and
CC neurons in the head and ventral nerve cord (PubMed:16920335). Isoform
CC c: Expressed in body wall muscle cells, neurons in the head, nerve
CC ring, ventral and dorsal nerve cords and epidermal cells in the tail
CC (PubMed:16920335). {ECO:0000269|PubMed:16920335}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development
CC (PubMed:16920335). First expressed in embryos from the 1.5-fold stage
CC (PubMed:16920335). Highly expressed during the L2 stage of larval
CC development (PubMed:16920335). {ECO:0000269|PubMed:16920335}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in arrest due to
CC elongation and morphogenesis defects at the embryonic or larval stages
CC in 30% of offspring (PubMed:16920335). Furthermore, embryos have highly
CC disorganized epithelial cells (PubMed:16920335). RNAi-mediated
CC knockdown in adults results in mis-localized or missing body wall
CC muscle cells (PubMed:16920335). {ECO:0000269|PubMed:16920335}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
CC {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; AF273782; AAG15131.1; -; mRNA.
DR EMBL; BX284606; CCD71834.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD71835.1; -; Genomic_DNA.
DR RefSeq; NP_001024873.1; NM_001029702.4. [Q22127-3]
DR RefSeq; NP_001024874.1; NM_001029703.3.
DR RefSeq; NP_741729.1; NM_171636.5.
DR AlphaFoldDB; Q22127; -.
DR SMR; Q22127; -.
DR STRING; 6239.T03G6.2c; -.
DR PaxDb; Q22127; -.
DR PeptideAtlas; Q22127; -.
DR PRIDE; Q22127; -.
DR EnsemblMetazoa; T03G6.2b.1; T03G6.2b.1; WBGene00003630. [Q22127-3]
DR EnsemblMetazoa; T03G6.2c.1; T03G6.2c.1; WBGene00003630. [Q22127-1]
DR GeneID; 180560; -.
DR KEGG; cel:CELE_T03G6.2; -.
DR UCSC; T03G6.2b; c. elegans. [Q22127-1]
DR CTD; 180560; -.
DR WormBase; T03G6.2b; CE31228; WBGene00003630; nhr-40. [Q22127-3]
DR WormBase; T03G6.2c; CE53506; WBGene00003630; nhr-40. [Q22127-1]
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; Q22127; -.
DR OrthoDB; 920203at2759; -.
DR PhylomeDB; Q22127; -.
DR PRO; PR:Q22127; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003630; Expressed in larva and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; PF00104; Hormone_recep; 1.
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 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..450
FT /note="Nuclear hormone receptor family member nhr-40"
FT /id="PRO_0000053779"
FT DOMAIN 173..450
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 28..103
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 31..51
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 67..91
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT VAR_SEQ 1..20
FT /note="MLVPPVSMIMYHELPSIKNK -> MPNN (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_003726"
FT CONFLICT 209
FT /note="S -> SSFLFF (in Ref. 1; AAG15131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 51807 MW; 83DFA1EF524374BA CRC64;
MLVPPVSMIM YHELPSIKNK KREKIPEGTL CVVCSDFASG IHYSVASCNG CKTFFRRALV
NKQTFTCQFS GDCVVGKSVR CVCRSCRLKK CFDMGMDPKA IQHDRDKIRY TKALKKKREE
EKRLKEMVIK EDIGSPQSIA SDTYINTSTP SSSTMINILE NDHHSYDPEA QNDVKAVIED
LLRLESRVKS LRNSYRFESQ VSATSCMYSS CLLDDITYMA ENTHENEGTI EPFECSVEKL
REWFVRDLSL MLEWGKCLPI MERLLLNDKL ALMKAFAPIF PLIQLAFYTR NEFECDIVIK
LEPDCTPKPI PERLNYPDGS FIEKGNKPAN TWEEMHTMLI DGCYKMMRQL KIKESTFVLY
KMLLFHNPDA DGLSSLGKKT IENERMRLLT QLFSYLSTER GKEAQTIFSN LLMMSATLSK
TASFIKRVFD FNHIFNRTND LIDQLIIVGL
