HIZR1_CAEEL
ID HIZR1_CAEEL Reviewed; 413 AA.
AC G5ED47;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=High zinc activated nuclear receptor protein {ECO:0000303|PubMed:28095401};
DE AltName: Full=Nuclear hormone receptor family member nhr-33 {ECO:0000305|PubMed:28095401};
GN Name=hizr-1 {ECO:0000303|PubMed:28095401, ECO:0000312|WormBase:ZK455.6};
GN Synonyms=nhr-33 {ECO:0000312|WormBase:ZK455.6};
GN ORFNames=ZK455.6 {ECO:0000312|WormBase:ZK455.6};
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, INDUCTION BY ZINC,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-23; SER-30; ARG-63 AND
RP ASP-270.
RX PubMed=28095401; DOI=10.1371/journal.pbio.2000094;
RA Warnhoff K., Roh H.C., Kocsisova Z., Tan C.H., Morrison A., Croswell D.,
RA Schneider D.L., Kornfeld K.;
RT "The nuclear receptor HIZR-1 uses zinc as a ligand to mediate homeostasis
RT in response to high zinc.";
RL PLoS Biol. 15:E2000094-E2000094(2017).
CC -!- FUNCTION: Nuclear receptor transcription factor that binds to DNA
CC enhancer elements to promote the transcription of genes required to
CC maintain micronutrient homeostasis. Direct binding to its ligand zinc
CC allows for nuclear accumulation and activation, which thereby induces
CC the transcription of genes required to promote the storage and
CC detoxification of excess dietary zinc. This in turn, allows for
CC internal zinc levels to be detected and regulated.
CC {ECO:0000269|PubMed:28095401}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:28095401}. Cytoplasm {ECO:0000269|PubMed:28095401}.
CC Note=Localizes to the cytoplasm in the absence of excess zinc, but
CC accumulates in the nucleus when zinc is in excess.
CC {ECO:0000269|PubMed:28095401}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in intestinal cells in the absence
CC of zinc supplementation. Upon zinc supplementation, accumulates in
CC alimentary tract cells, and it is mainly expressed in the intestine.
CC {ECO:0000269|PubMed:28095401}.
CC -!- INDUCTION: Induced by high levels of zinc.
CC {ECO:0000269|PubMed:28095401}.
CC -!- DISRUPTION PHENOTYPE: In the presence of excess dietary zinc, reduced
CC transcription of genes such as cdf-2, ttm-1b and mtl-1, which are
CC required for zinc homeostasis, and retarded growth as compared to wild-
CC type. {ECO:0000269|PubMed:28095401}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
CC {ECO:0000255|RuleBase:RU004334}.
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DR EMBL; BX284606; CAA91494.3; -; Genomic_DNA.
DR RefSeq; NP_509893.3; NM_077492.3.
DR AlphaFoldDB; G5ED47; -.
DR SMR; G5ED47; -.
DR STRING; 6239.ZK455.6; -.
DR PaxDb; G5ED47; -.
DR EnsemblMetazoa; ZK455.6.1; ZK455.6.1; WBGene00013976.
DR GeneID; 191322; -.
DR KEGG; cel:CELE_ZK455.6; -.
DR CTD; 191322; -.
DR WormBase; ZK455.6; CE43818; WBGene00013976; hizr-1.
DR eggNOG; KOG3575; Eukaryota.
DR HOGENOM; CLU_007368_1_1_1; -.
DR InParanoid; G5ED47; -.
DR OMA; EADVCCK; -.
DR OrthoDB; 1020893at2759; -.
DR PhylomeDB; G5ED47; -.
DR PRO; PR:G5ED47; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00013976; Expressed in adult organism and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..413
FT /note="High zinc activated nuclear receptor protein"
FT /evidence="ECO:0000305"
FT /id="PRO_0000440165"
FT DOMAIN 135..396
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 11..86
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 14..34
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 50..69
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 101..412
FT /note="Required for zinc-binding"
FT /evidence="ECO:0000269|PubMed:28095401"
FT SITE 23
FT /note="Required for DNA binding"
FT /evidence="ECO:0000269|PubMed:28095401"
FT SITE 30
FT /note="Required for DNA binding"
FT /evidence="ECO:0000269|PubMed:28095401"
FT SITE 63
FT /note="Required for DNA binding"
FT /evidence="ECO:0000269|PubMed:28095401"
FT MUTAGEN 23
FT /note="G->E: Does not bind DNA enhancer elements."
FT /evidence="ECO:0000269|PubMed:28095401"
FT MUTAGEN 30
FT /note="S->L: Does not bind DNA enhancer elements."
FT /evidence="ECO:0000269|PubMed:28095401"
FT MUTAGEN 63
FT /note="R->C: Does not bind DNA enhancer elements."
FT /evidence="ECO:0000269|PubMed:28095401"
FT MUTAGEN 270
FT /note="D->N: In am285; gain of function. The mutant protein
FT accumulates in nucleus and increases transcription of zinc-
FT activated genes in the absence of excess dietary zinc."
FT /evidence="ECO:0000269|PubMed:28095401"
SQ SEQUENCE 413 AA; 46736 MW; 4DD11A8D099C8806 CRC64;
MQKVMNDPED LGNCKICLQR ADGIHFAVSS CRACAAFFRR TVILKLNYTC KEKGNCTVEK
SLRNLCRSCR YTRCINEGMK IELVQLQRDS IGRKKSGASI SIDPLFTPNV ASSLSAIFKN
EKEDVLSTSC TILSQMTSGY AMFLNIRRST NTLVQSSVIT PTFKMPKIEL HASRFDSAKQ
VCKAEAHLVT DIVNSYFSPF NSLKFEDKVA LFKNFFCYFS HTDRAYQSFK QFESDNLNDK
ILMPDGGFIK RTELGRFYEN AEGVHTSAED AAKIFQPALN YILDVIVDYM RRIHIIETEY
LALLGFCLWD DAVPGLSKEA KSLAVQTQSK LLAELQNFYS SQNKDAVEIT QRVGVLLLLV
PKLTKCVIML RENSVLAELF NYYEADVCCK NFKEDASVDL DCTSQCIVHT KND
