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 23-FEB-2022, entry version 137. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 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; MAPDDGM; -. DR OrthoDB; 1201386at2759; -. DR PhylomeDB; Q65ZG6; -. DR Proteomes; UP000001940; Chromosome II. DR Bgee; WBGene00003480; Expressed in multi-cellular organism and 4 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 //