KLF1_CAEEL
ID KLF1_CAEEL Reviewed; 497 AA.
AC Q9TZ64;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Kruppel-like factor 1 {ECO:0000305};
GN Name=klf-1 {ECO:0000312|WormBase:F56F11.3};
GN ORFNames=F56F11.3 {ECO:0000312|WormBase:F56F11.3};
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, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND UBIQUITINATION.
RX PubMed=18680432; DOI=10.1089/dna.2008.0739;
RA Hashmi S., Ji Q., Zhang J., Parhar R.S., Huang C.H., Brey C., Gaugler R.;
RT "A Krueppel-like factor in Caenorhabditis elegans with essential roles in
RT fat regulation, cell death, and phagocytosis.";
RL DNA Cell Biol. 27:545-551(2008).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH WWP-1, AND DISRUPTION PHENOTYPE.
RX PubMed=24805825; DOI=10.1038/ncomms4772;
RA Carrano A.C., Dillin A., Hunter T.;
RT "A Krueppel-like factor downstream of the E3 ligase WWP-1 mediates dietary-
RT restriction-induced longevity in Caenorhabditis elegans.";
RL Nat. Commun. 5:3772-3772(2014).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31346165; DOI=10.1038/s41467-019-11275-w;
RA Herholz M., Cepeda E., Baumann L., Kukat A., Hermeling J., Maciej S.,
RA Szczepanowska K., Pavlenko V., Frommolt P., Trifunovic A.;
RT "KLF-1 orchestrates a xenobiotic detoxification program essential for
RT longevity of mitochondrial mutants.";
RL Nat. Commun. 10:3323-3323(2019).
CC -!- FUNCTION: Transcription factor which modulates genes involved in lipid
CC metabolism and the phase I detoxification pathway, including cytochrome
CC P450 oxidases (PubMed:18680432, PubMed:24805825, PubMed:31346165).
CC Required for diet restriction- and mitochondrial dysfunction-mediated
CC lifespan extension, perhaps acting in a ubiquitination-dependent manner
CC (PubMed:24805825, PubMed:31346165). Involved in the response to
CC oxidative stress (PubMed:31346165). Plays a role in cell death
CC (PubMed:18680432). {ECO:0000269|PubMed:18680432,
CC ECO:0000269|PubMed:24805825, ECO:0000269|PubMed:31346165}.
CC -!- SUBUNIT: Interacts with E3 ubiquitin-protein ligase wwp-1 (via WW
CC domains). {ECO:0000269|PubMed:24805825}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31346165}. Cytoplasm
CC {ECO:0000269|PubMed:31346165}. Note=Localized to nucleus at the larval
CC L4 stage, becoming cytoplasmic during early adulthood. Translocation to
CC the nucleus dependent, in some circumstances, on oxidative stress.
CC {ECO:0000269|PubMed:31346165}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, hypodermis and a few
CC neurons. {ECO:0000269|PubMed:31346165}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all developmental stages, increasing
CC gradually from embryo to larval L4 stage, decreasing and stabilizing in
CC adult stage (PubMed:18680432). Expressed in intestine in all larval and
CC adult stages, and in a few neuronal and hypodermal cells
CC (PubMed:18680432). {ECO:0000269|PubMed:18680432}.
CC -!- INDUCTION: Induced by treatment with high levels of paraquat, a
CC chemical causing production of reactive oxygen species (ROS), but not
CC by other exogenous stressors, such as heat shock or osmotic stress.
CC {ECO:0000269|PubMed:31346165}.
CC -!- PTM: Ubiquitinated; probably preferentially monoubiquitinated by wwp-1.
CC {ECO:0000269|PubMed:24805825}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockown leads to increased cell
CC death, perhaps by apoptosis, in the germline and uterus of
CC hermaphrodites (PubMed:18680432). Lipid contents in the intestine
CC increase (PubMed:18680432). RNAi-mediated knockdown causes reduced
CC ability of dietary restriction to extend lifespan (PubMed:24805825).
CC Abolishes lifespan extension completely on an eat-2 mutant background,
CC independent of whether knockdown is ubiquitous, or targeted only to the
CC intestine (PubMed:24805825). Abolishes lifespan extension on either
CC isp-1;ctb-1 double mutant, or isp-1, gas-1 or mev-1 single mutant
CC backgrounds; knockdown is most effective when applied in early
CC adulthood, rather than during early development (PubMed:31346165).
CC Further decreases the lower movement rates of isp-1;ctb-1 double
CC mutants (PubMed:31346165). {ECO:0000269|PubMed:18680432,
CC ECO:0000269|PubMed:24805825, ECO:0000269|PubMed:31346165}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BX284603; CCD72011.1; -; Genomic_DNA.
DR PIR; T33634; T33634.
DR RefSeq; NP_497632.1; NM_065231.3.
DR AlphaFoldDB; Q9TZ64; -.
DR SMR; Q9TZ64; -.
DR IntAct; Q9TZ64; 21.
DR STRING; 6239.F56F11.3.1; -.
DR EPD; Q9TZ64; -.
DR PaxDb; Q9TZ64; -.
DR PeptideAtlas; Q9TZ64; -.
DR EnsemblMetazoa; F56F11.3.1; F56F11.3.1; WBGene00018990.
DR GeneID; 175404; -.
DR KEGG; cel:CELE_F56F11.3; -.
DR UCSC; F56F11.3.1; c. elegans.
DR CTD; 175404; -.
DR WormBase; F56F11.3; CE11280; WBGene00018990; klf-1.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164016; -.
DR HOGENOM; CLU_035852_0_0_1; -.
DR InParanoid; Q9TZ64; -.
DR OMA; HCTHPNC; -.
DR OrthoDB; 1067503at2759; -.
DR SignaLink; Q9TZ64; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00018990; Expressed in larva and 3 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0043277; P:apoptotic cell clearance; IMP:WormBase.
DR GO; GO:0006915; P:apoptotic process; IMP:WormBase.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IMP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..497
FT /note="Kruppel-like factor 1"
FT /id="PRO_0000452643"
FT ZN_FING 414..438
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 444..468
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 474..496
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 371..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 55494 MW; 101FD094C9F5FEC7 CRC64;
MTSSSINATS SREPLIHIPN KPSLSIDPLA RADRSVHLSP SFFQPGLSSI SSENDDAEQR
IHEATRSFNQ FGHQFYESIR ELSESTSAYE RLKANALRRK LENTFGNDSG AATSSSSSSV
FERQSDFSAF APYKNSHFDS TQSLFQPTTS FNDRLEQIKS DFIAEHQKSM SSFSGFNTPT
TALGAAFQGM QVKKSAFAPV LLRENLDTRR PGGHLISDIL NRDPLPQSRN LNLNMARNVP
IRLIHSTSNF DIASSSSGDS GHQDHESIVV EDADMDSPTS PCVKRSAMNF DLRDEPLTVN
VESVSSTSDL PSSVSSSVNS FVYQNFDPLE FKRKIDELTA SACLAVMPDA NGQVDPMAIK
TQLDAIKKQM EEHQTHMAEA SQRLHVDSSL EDSNCEPSPS SSYDASEPSV KRLHHCTHPN
CGKVYTKSSH LKAHFRTHTG EKPYECSWDG CDWRFARSDE LTRHYRKHTG DRPFKCSQCS
RAFSRSDHLS LHMKRHF
