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NHR67_CAEEL
ID   NHR67_CAEEL             Reviewed;         416 AA.
AC   Q9XVV3;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Nuclear hormone receptor family member nhr-67;
GN   Name=nhr-67; ORFNames=C08F8.8;
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 [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   [2]
RP   FUNCTION.
RX   PubMed=18179707; DOI=10.1186/1471-2199-9-2;
RA   DeMeo S.D., Lombel R.M., Cronin M., Smith E.L., Snowflack D.R., Reinert K.,
RA   Clever S., Wightman B.;
RT   "Specificity of DNA-binding by the FAX-1 and NHR-67 nuclear receptors of
RT   Caenorhabditis elegans is partially mediated via a subclass-specific P-box
RT   residue.";
RL   BMC Mol. Biol. 9:2-2(2008).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=19906858; DOI=10.1242/dev.035477;
RA   Kato M., Sternberg P.W.;
RT   "The C. elegans tailless/Tlx homolog nhr-67 regulates a stage-specific
RT   program of linker cell migration in male gonadogenesis.";
RL   Development 136:3907-3915(2009).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22363008; DOI=10.1126/science.1215156;
RA   Blum E.S., Abraham M.C., Yoshimura S., Lu Y., Shaham S.;
RT   "Control of nonapoptotic developmental cell death in Caenorhabditis elegans
RT   by a polyglutamine-repeat protein.";
RL   Science 335:970-973(2012).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=27472063; DOI=10.1038/cdd.2016.77;
RA   Malin J.A., Kinet M.J., Abraham M.C., Blum E.S., Shaham S.;
RT   "Transcriptional control of non-apoptotic developmental cell death in C.
RT   elegans.";
RL   Cell Death Differ. 23:1985-1994(2016).
CC   -!- FUNCTION: Orphan nuclear receptor that binds DNA containing an extended
CC       core motif half-site sequence 5'-AAGTCA-3' (PubMed:18179707,
CC       PubMed:19906858). In males, plays an essential role in the migration of
CC       the linker cell which guides gonad elongation during the L3 and L4
CC       stages of larval development by negatively regulating the expression of
CC       netrin receptor unc-5 at the mid-L3 stage (PubMed:22363008,
CC       PubMed:19906858). Involved in the regulation of non-apoptotic cell
CC       death in the linker cell, acting upstream of or in parallel to
CC       transcription factor hsf-1 (PubMed:27472063).
CC       {ECO:0000269|PubMed:18179707, ECO:0000269|PubMed:19906858,
CC       ECO:0000269|PubMed:22363008, ECO:0000269|PubMed:27472063}.
CC   -!- INTERACTION:
CC       Q9XVV3; O02482: unc-37; NbExp=3; IntAct=EBI-314697, EBI-314716;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -!- TISSUE SPECIFICITY: Expressed in linker cell.
CC       {ECO:0000269|PubMed:19906858}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in males prevents
CC       migration of the linker cell (LC) during larval development resulting
CC       in abnormal gonad migration (PubMed:9851916, PubMed:19906858). At the
CC       L3-to-L4 molt stage, the LC fails to reach the P7.p hypodermal cell and
CC       fails to perform the turn from the dorsal to the ventral side of the
CC       body. During the late L4 stage, the LC turns ventrally but stays
CC       farther behind its normal position (PubMed:9851916, PubMed:19906858).
CC       In addition, LC polarization, which normally occurs during the L3-L4
CC       stages, is severely delayed and mig-2 polarization to the adherent side
CC       of thr LC is impaired (PubMed:19906858). In the LC, expression of unc-5
CC       at the L3 and L4 larval stages is increased and expression of zmp-1 is
CC       absent at L4 stage (PubMed:19906858). Prevents non-apoptotic cell death
CC       in the LC (PubMed:27472063). Knockdown enhances LC survival on egl-20,
CC       eor-1, or lin-29 mutant backgrounds (PubMed:27472063). Causes
CC       precocious expression of let-70 in the LC during larval stage L3
CC       (PubMed:27472063). RNAi-mediated knockdown in hermaphrodites causes no
CC       defect in distal tip cell migration (PubMed:19906858).
CC       {ECO:0000269|PubMed:19906858, ECO:0000269|PubMed:27472063,
CC       ECO:0000269|PubMed:9851916}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
CC       {ECO:0000305}.
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DR   EMBL; Z73103; CAA97428.1; -; Genomic_DNA.
DR   PIR; T19102; T19102.
DR   RefSeq; NP_502094.1; NM_069693.3.
DR   AlphaFoldDB; Q9XVV3; -.
DR   SMR; Q9XVV3; -.
DR   BioGRID; 43123; 34.
DR   DIP; DIP-25535N; -.
DR   IntAct; Q9XVV3; 33.
DR   STRING; 6239.C08F8.8; -.
DR   EPD; Q9XVV3; -.
DR   PaxDb; Q9XVV3; -.
DR   EnsemblMetazoa; C08F8.8.1; C08F8.8.1; WBGene00003657.
DR   GeneID; 178024; -.
DR   KEGG; cel:CELE_C08F8.8; -.
DR   UCSC; C08F8.8; c. elegans.
DR   CTD; 178024; -.
DR   WormBase; C08F8.8; CE18491; WBGene00003657; nhr-67.
DR   eggNOG; KOG3575; Eukaryota.
DR   HOGENOM; CLU_055512_0_0_1; -.
DR   InParanoid; Q9XVV3; -.
DR   OMA; RYISCMV; -.
DR   OrthoDB; 870262at2759; -.
DR   PhylomeDB; Q9XVV3; -.
DR   SignaLink; Q9XVV3; -.
DR   PRO; PR:Q9XVV3; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00003657; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:WormBase.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:WormBase.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
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; IMP:WormBase.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0035262; P:gonad morphogenesis; IMP:WormBase.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:WormBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR   GO; GO:0012501; P:programmed cell death; IMP:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
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; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF48508; SSF48508; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..416
FT                   /note="Nuclear hormone receptor family member nhr-67"
FT                   /id="PRO_0000053794"
FT   DNA_BIND        18..98
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         21..41
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         57..86
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          331..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..349
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  46771 MW;  4BC549E9C26BEA28 CRC64;
     MMTAVSQMSV PSSRILLDVD CRVCEDHSSG KHYSIFSCDG CAGFFKRSIR RHRQYVCKNK
     GSPSEGQCKV DKTHRNQCRA CRLRKCLEIG MNKDAVQHER GPRNSSLRRQ QMMFDHGSSP
     NSPEMGSESD AIILPTSSMN RDTVAGTAAR IFFALVGFCQ NPLNGVPKER QMTMFQQNWA
     ALLVLHATET RAITSKQIRT ETISGSSEQR NAVANAFEII ERLQLDNREY MMLKHFTMWR
     DTPSAIQIVF QLASIQNFTH RTEPTRYIQC INAIAAIPTT SIIDVLFRPS IGSASMPRLI
     QDMFKPPQQP TPTSLFPMAN FNLNFLLKQE KTETEEGEDI EEEDDATSSN QFDENSSTDD
     RSVGELDPVQ LFLALNSSTQ PSSASSPSSS RPRHSIRSIT ELLSIQEEES VNVEEV
 
 
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