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PQM1_CAEEL
ID   PQM1_CAEEL              Reviewed;         295 AA.
AC   G5EFY7;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Zinc finger transcription factor pqm-1 {ECO:0000305};
DE   AltName: Full=CePqM132 {ECO:0000312|EMBL:AAB63299.1};
DE   AltName: Full=Paraquat responsive protein {ECO:0000303|PubMed:9512531};
GN   Name=pqm-1 {ECO:0000312|WormBase:F40F8.7};
GN   ORFNames=F40F8.7 {ECO:0000312|WormBase:F40F8.7};
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:AAB63299.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:AAB63299.1};
RX   PubMed=9512531; DOI=10.1093/nar/26.7.1621;
RA   Tawe W.N., Eschbach M.-L., Walter R.D., Henkle-Duehrsen K.;
RT   "Identification of stress-responsive genes in Caenorhabditis elegans using
RT   RT-PCR differential display.";
RL   Nucleic Acids Res. 26:1621-1627(1998).
RN   [2] {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   [3] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=23911329; DOI=10.1016/j.cell.2013.07.006;
RA   Tepper R.G., Ashraf J., Kaletsky R., Kleemann G., Murphy C.T.,
RA   Bussemaker H.J.;
RT   "PQM-1 complements DAF-16 as a key transcriptional regulator of DAF-2-
RT   mediated development and longevity.";
RL   Cell 154:676-690(2013).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   CYS-163.
RX   PubMed=27401555; DOI=10.1101/gad.283895.116;
RA   Dowen R.H., Breen P.C., Tullius T., Conery A.L., Ruvkun G.;
RT   "A microRNA program in the C. elegans hypodermis couples to intestinal
RT   mTORC2/PQM-1 signaling to modulate fat transport.";
RL   Genes Dev. 30:1515-1528(2016).
RN   [5] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=29949773; DOI=10.1016/j.celrep.2018.05.093;
RA   O'Brien D., Jones L.M., Good S., Miles J., Vijayabaskar M.S., Aston R.,
RA   Smith C.E., Westhead D.R., van Oosten-Hawle P.;
RT   "A PQM-1-Mediated Response Triggers Transcellular Chaperone Signaling and
RT   Regulates Organismal Proteostasis.";
RL   Cell Rep. 23:3905-3919(2018).
RN   [6] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH CEH-60, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   266-THR--THR-268.
RX   PubMed=30956009; DOI=10.1016/j.devcel.2019.03.002;
RA   Dowen R.H.;
RT   "CEH-60/PBX and UNC-62/MEIS Coordinate a Metabolic Switch that Supports
RT   Reproduction in C. elegans.";
RL   Dev. Cell 49:235-250.e7(2019).
RN   [7] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=31532389; DOI=10.7554/elife.44674;
RA   Rajan M., Anderson C.P., Rindler P.M., Romney S.J.,
RA   Ferreira Dos Santos M.C., Gertz J., Leibold E.A.;
RT   "NHR-14 loss of function couples intestinal iron uptake with innate
RT   immunity in C. elegans through PQM-1 signaling.";
RL   Elife 8:0-0(2019).
RN   [8] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=33009389; DOI=10.1038/s41467-020-18369-w;
RA   Heimbucher T., Hog J., Gupta P., Murphy C.T.;
RT   "PQM-1 controls hypoxic survival via regulation of lipid metabolism.";
RL   Nat. Commun. 11:4627-4627(2020).
RN   [9] {ECO:0000305}
RP   ERRATUM OF PUBMED:33009389.
RX   PubMed=33219230; DOI=10.1038/s41467-020-19868-6;
RA   Heimbucher T., Hog J., Gupta P., Murphy C.T.;
RT   "Author Correction: PQM-1 controls hypoxic survival via regulation of lipid
RT   metabolism.";
RL   Nat. Commun. 11:6018-6018(2020).
CC   -!- FUNCTION: Zinc finger transcription factor which acts as both a
CC       transcriptional activator and repressor (PubMed:23911329,
CC       PubMed:30956009). Binds to the promoters of genes that contain the 5'-
CC       CTTATCA-3' DNA consensus sequence in their regulatory region
CC       (PubMed:23911329, PubMed:31532389). Functions downstream of the
CC       Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:23911329,
CC       PubMed:27401555). Involved in normal development, lifespan, stress
CC       response, lipid metabolism, innate immunity and exit from the
CC       developmentally arrested larval state known as dauer (PubMed:23911329,
CC       PubMed:27401555, PubMed:29949773, PubMed:31532389, PubMed:33009389).
CC       Required for stress-induced expression of hsp-90 and resistance to heat
CC       stress, perhaps as part of a systemic stress signaling pathway
CC       (PubMed:29949773). Involved in maintenance of proteostasis
CC       (PubMed:29949773). Under hypoxic stress increases lipid levels by
CC       positively regulating fatty acid synthesis via fat-7 expression
CC       (PubMed:33009389). Associates with homeobox protein ceh-60 at the
CC       promoters of some stress-responsive genes to regulate expression; may
CC       require phosphorylation for transcriptional repression activity
CC       (PubMed:30956009). Acts downstream of nhr-14 to activate transcription
CC       of intestinal metal transporter smf-3, modulating innate immunity and
CC       iron uptake (PubMed:31532389). May act downstream of the mTORC2
CC       signaling mediated pathway (PubMed:27401555). May act in a mutually
CC       exclusive manner with the FOXO transcription factor daf-16
CC       (PubMed:23911329, PubMed:27401555). {ECO:0000269|PubMed:23911329,
CC       ECO:0000269|PubMed:27401555, ECO:0000269|PubMed:29949773,
CC       ECO:0000269|PubMed:30956009, ECO:0000269|PubMed:31532389,
CC       ECO:0000269|PubMed:33009389}.
CC   -!- SUBUNIT: Interacts with ceh-60. {ECO:0000269|PubMed:30956009}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:30956009}. Nucleus
CC       {ECO:0000269|PubMed:23911329, ECO:0000269|PubMed:29949773,
CC       ECO:0000269|PubMed:31532389}. Cytoplasm {ECO:0000269|PubMed:23911329,
CC       ECO:0000269|PubMed:31532389}. Note=Nuclear localization under normal
CC       conditions, cytoplasmic as a result of heat-stress (PubMed:23911329).
CC       Nuclear localization declines over normal lifespan (PubMed:23911329).
CC       Exposure to Gram-negative bacterium P.aeruginosa enhances nuclear
CC       localization (PubMed:31532389). Hypoxic stress enhances nuclear
CC       localization (PubMed:33009389). {ECO:0000269|PubMed:23911329,
CC       ECO:0000269|PubMed:31532389, ECO:0000269|PubMed:33009389}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in intestinal cells from larval through
CC       to adult stages (PubMed:23911329). Expressed in neurons during L1
CC       larval stage (PubMed:29949773). {ECO:0000269|PubMed:23911329,
CC       ECO:0000269|PubMed:29949773}.
CC   -!- INDUCTION: Induced by paraquat, a chemical causing production of
CC       reactive oxygen species (ROS). {ECO:0000269|PubMed:9512531}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown on a daf-2 mutant
CC       background shortens lifespan substantially, by up to 45%, but does not
CC       alter lifespan on a daf-16 mutant or wild-type background
CC       (PubMed:23911329). Knockdown activates vitellogenesis on either lin-29,
CC       rict-1 or sgk-1 mutant backgrounds, but not on daf-2 mutants
CC       (PubMed:27401555). Reduced expression of metal transporter smf-3 on an
CC       nhr-14 mutant background (PubMed:27401555). Enhanced sensitivity to
CC       P.aeruginosa infection on an nhr-14 mutant background
CC       (PubMed:31532389). {ECO:0000269|PubMed:23911329,
CC       ECO:0000269|PubMed:27401555, ECO:0000269|PubMed:31532389}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF008590; AAB63299.1; -; mRNA.
DR   EMBL; BX284602; CAA93267.1; -; Genomic_DNA.
DR   PIR; T22039; T22039.
DR   RefSeq; NP_496391.1; NM_063990.4.
DR   AlphaFoldDB; G5EFY7; -.
DR   IntAct; G5EFY7; 2.
DR   STRING; 6239.F40F8.7.2; -.
DR   EPD; G5EFY7; -.
DR   PaxDb; G5EFY7; -.
DR   EnsemblMetazoa; F40F8.7.1; F40F8.7.1; WBGene00004096.
DR   GeneID; 174705; -.
DR   KEGG; cel:CELE_F40F8.7; -.
DR   CTD; 174705; -.
DR   WormBase; F40F8.7; CE05846; WBGene00004096; pqm-1.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00970000196485; -.
DR   HOGENOM; CLU_937626_0_0_1; -.
DR   InParanoid; G5EFY7; -.
DR   OMA; RTSTICD; -.
DR   OrthoDB; 1114064at2759; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004096; Expressed in larva and 3 other tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IMP:UniProtKB.
DR   GO; GO:0034605; P:cellular response to heat; IMP:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR   GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR   GO; GO:0005977; P:glycogen metabolic process; IMP:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IMP:WormBase.
DR   GO; GO:1903187; P:negative regulation of vitellogenesis; IMP:UniProtKB.
DR   GO; GO:0032364; P:oxygen homeostasis; IMP:UniProtKB.
DR   GO; GO:1905911; P:positive regulation of dauer entry; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:1903188; P:positive regulation of vitellogenesis; IMP:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
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:0001666; P:response to hypoxia; IMP:UniProtKB.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   1: Evidence at protein level;
KW   Activator; Chromosome; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..295
FT                   /note="Zinc finger transcription factor pqm-1"
FT                   /id="PRO_0000452746"
FT   ZN_FING         161..183
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         227..249
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         163
FT                   /note="C->Y: In mg477; suppresses defect in vitellogenesis
FT                   on sgk-1 mutant background."
FT                   /evidence="ECO:0000269|PubMed:27401555"
FT   MUTAGEN         266..268
FT                   /note="TST->AAA: Up-regulates expression of stress-response
FT                   genes which may also be ceh-60 targets."
FT                   /evidence="ECO:0000269|PubMed:30956009"
SQ   SEQUENCE   295 AA;  33346 MW;  D504D4DB0687DB15 CRC64;
     MSFLNNDFGS PPATSSPPTT MPKLPTIQDM LNNIGASTVN LMQPNPYLMQ NQIPLPVPNL
     PLNPFLHLNP AISQEIIQQF IAMSFNTPNV LASIANMGDD EGPSCNPKMR RGDLLKSVSM
     DSTEDPPSIT LDNNGDMIVP NNDKEGWCRN KKYIEQTENG YMCTVCRKVY GRYNSVSYHV
     TIYHRNPPIK CNVPNCQFTT REARYIHFHK NYRHGIPLPE SIDQGSRKCP HCRHVSKSPA
     MLEKHIRRHQ IKDGLSNINE AIRERTSTIC DEAMEIEPAE TEVDPIETKP RSCTL
 
 
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