KLF3_CAEEL
ID KLF3_CAEEL Reviewed; 315 AA.
AC Q65ZG6; P91329;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Kruppel-like factor 3 {ECO:0000305};
GN Name=klf-3 {ECO:0000312|WormBase:F54H5.4b};
GN ORFNames=F54H5.4 {ECO:0000312|WormBase:F54H5.4b};
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, AND DEVELOPMENTAL STAGE.
RX PubMed=19427851; DOI=10.1016/j.yexcr.2009.04.025;
RA Zhang J., Yang C., Brey C., Rodriguez M., Oksov Y., Gaugler R.,
RA Dickstein E., Huang C.H., Hashmi S.;
RT "Mutation in Caenorhabditis elegans Krueppel-like factor, KLF-3 results in
RT fat accumulation and alters fatty acid composition.";
RL Exp. Cell Res. 315:2568-2580(2009).
RN [3] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=23639358; DOI=10.1016/j.jmb.2013.04.020;
RA Zhang J., Hashmi S., Cheema F., Al-Nasser N., Bakheet R., Parhar R.S.,
RA Al-Mohanna F., Gaugler R., Hussain M.M., Hashmi S.;
RT "Regulation of lipoprotein assembly, secretion and fatty acid beta-
RT oxidation by Krueppel-like transcription factor, klf-3.";
RL J. Mol. Biol. 425:2641-2655(2013).
RN [4] {ECO:0000305}
RP INDUCTION.
RX PubMed=28261316; DOI=10.1186/s12986-017-0172-8;
RA Ling J., Brey C., Schilling M., Lateef F., Lopez-Dee Z.P., Fernandes K.,
RA Thiruchelvam K., Wang Y., Chandel K., Rau K., Parhar R., Al-Mohanna F.,
RA Gaugler R., Hashmi S.;
RT "Defective lipid metabolism associated with mutation in klf-2 and klf-3:
RT important roles of essential dietary salts in fat storage.";
RL Nutr. Metab. 14:22-22(2017).
CC -!- FUNCTION: Probable transcription factor which regulates lipid
CC catabolism, storage, and secretion, probably by modulating genes
CC involved in fatty acid desaturation and beta-oxidation, and lipoprotein
CC assembly and secretion (PubMed:19427851, PubMed:23639358). Involved in
CC reproduction, perhaps indirectly (PubMed:19427851, PubMed:23639358).
CC {ECO:0000269|PubMed:19427851, ECO:0000269|PubMed:23639358}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:F54H5.4b};
CC IsoId=Q65ZG6-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F54H5.4a};
CC IsoId=Q65ZG6-2; Sequence=VSP_061014;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, including in the
CC germline and especially in intestine in larval and adult stages (at
CC protein level). {ECO:0000269|PubMed:19427851,
CC ECO:0000269|PubMed:23639358}.
CC -!- INDUCTION: Expression is repressed in response to high levels of
CC dietary calcium. {ECO:0000269|PubMed:28261316}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BX284602; CCD68189.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD68190.1; -; Genomic_DNA.
DR PIR; T25800; T25800.
DR RefSeq; NP_001022204.1; NM_001027033.1. [Q65ZG6-2]
DR RefSeq; NP_001022205.1; NM_001027034.3. [Q65ZG6-1]
DR AlphaFoldDB; Q65ZG6; -.
DR SMR; Q65ZG6; -.
DR DIP; DIP-26046N; -.
DR IntAct; Q65ZG6; 6.
DR STRING; 6239.F54H5.4b; -.
DR SwissLipids; SLP:000000843; -.
DR PaxDb; Q65ZG6; -.
DR EnsemblMetazoa; F54H5.4a.1; F54H5.4a.1; WBGene00003480. [Q65ZG6-2]
DR EnsemblMetazoa; F54H5.4b.1; F54H5.4b.1; WBGene00003480. [Q65ZG6-1]
DR EnsemblMetazoa; F54H5.4b.2; F54H5.4b.2; WBGene00003480. [Q65ZG6-1]
DR GeneID; 191713; -.
DR KEGG; cel:CELE_F54H5.4; -.
DR UCSC; F54H5.4b; c. elegans.
DR CTD; 191713; -.
DR WormBase; F54H5.4a; CE01967; WBGene00003480; klf-3.
DR WormBase; F54H5.4b; CE37379; WBGene00003480; klf-3.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_883476_0_0_1; -.
DR InParanoid; Q65ZG6; -.
DR OMA; PNPSAYW; -.
DR OrthoDB; 1201386at2759; -.
DR PhylomeDB; Q65ZG6; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003480; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q65ZG6; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; HEP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..315
FT /note="Kruppel-like factor 3"
FT /id="PRO_0000452532"
FT ZN_FING 230..254
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 260..284
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 290..312
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 149..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..14
FT /note="MLKMEQSAPPRYEE -> MTSPNIFQ (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_061014"
SQ SEQUENCE 315 AA; 35903 MW; 3B9D0006D1A8D7D3 CRC64;
MLKMEQSAPP RYEEDWADVY EFIERDSSRK NVPAIEAIER RLAFSPLITP NPGAKQFAPI
HVPGREPPRM LLPPTPHFQA PFSPHPPPVQ QVPSYSPPHA PPSYETYPEV YYPPHIICNP
YDVPTTSDRN PPYYTEVTTV SAVTLHSMTP PTHKIETPPS SPENSFGPLA SQLPAIKMEI
PMHPLPHNGE LDSTRSSPSS TTSSERSPLQ RKSRIESNKR NPTDKKFVVH ACTYPGCFKK
YSKSSHLKAH ERTHSGEKPF VCKWQNCSWK FARSDELTRH MRKHTGDKPF RCSLCDRNFA
RSDHLSLHMK RHSTI
