DRE1_CAEEL
ID DRE1_CAEEL Reviewed; 936 AA.
AC Q94251;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=F-box protein dre-1 {ECO:0000305};
DE AltName: Full=Daf-12 redundant function protein {ECO:0000312|WormBase:K04A8.6a};
GN Name=dre-1 {ECO:0000312|WormBase:K04A8.6a};
GN ORFNames=K04A8.6 {ECO:0000312|WormBase:K04A8.6a};
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, INTERACTION WITH SKR-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-514;
RP GLY-629; GLY-744 AND ALA-902.
RX PubMed=17336909; DOI=10.1016/j.devcel.2007.01.018;
RA Fielenbach N., Guardavaccaro D., Neubert K., Chan T., Li D., Feng Q.,
RA Hutter H., Pagano M., Antebi A.;
RT "DRE-1: an evolutionarily conserved F box protein that regulates C. elegans
RT developmental age.";
RL Dev. Cell 12:443-455(2007).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CED-9 AND SKR-1, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF SER-275.
RX PubMed=23431138; DOI=10.1073/pnas.1217271110;
RA Chiorazzi M., Rui L., Yang Y., Ceribelli M., Tishbi N., Maurer C.W.,
RA Ranuncolo S.M., Zhao H., Xu W., Chan W.C., Jaffe E.S., Gascoyne R.D.,
RA Campo E., Rosenwald A., Ott G., Delabie J., Rimsza L.M., Shaham S.,
RA Staudt L.M.;
RT "Related F-box proteins control cell death in Caenorhabditis elegans and
RT human lymphoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3943-3948(2013).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BLMP-1, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLY-514.
RX PubMed=24613396; DOI=10.1016/j.devcel.2014.01.028;
RA Horn M., Geisen C., Cermak L., Becker B., Nakamura S., Klein C., Pagano M.,
RA Antebi A.;
RT "DRE-1/FBXO11-dependent degradation of BLMP-1/BLIMP-1 governs C. elegans
RT developmental timing and maturation.";
RL Dev. Cell 28:697-710(2014).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH BLMP-1.
RX PubMed=24968003; DOI=10.1371/journal.pgen.1004428;
RA Huang T.F., Cho C.Y., Cheng Y.T., Huang J.W., Wu Y.Z., Yeh A.Y.,
RA Nishiwaki K., Chang S.C., Wu Y.C.;
RT "BLMP-1/Blimp-1 regulates the spatiotemporal cell migration pattern in C.
RT elegans.";
RL PLoS Genet. 10:E1004428-E1004428(2014).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins including blmp-1 (PubMed:17336909, PubMed:23431138,
CC PubMed:24613396, PubMed:24968003). Heterochronic protein which is
CC required for the timing of gonad development and epidermal seam cell
CC differentiation (PubMed:17336909). Regulates tail-spike cell death
CC through inhibition of the apoptosis regulator ced-9 (PubMed:23431138).
CC {ECO:0000269|PubMed:17336909, ECO:0000269|PubMed:23431138,
CC ECO:0000269|PubMed:24613396, ECO:0000269|PubMed:24968003}.
CC -!- SUBUNIT: Component of a SCF ubiquitin ligase complex (PubMed:17336909,
CC PubMed:23431138, PubMed:24613396, PubMed:24968003). Interacts (via F-
CC box) with skr-1 (PubMed:17336909, PubMed:23431138). Interacts with
CC blmp-1; the interaction targets blmp-1 for proteasomal degradation
CC (PubMed:24613396). Interacts with ced-9; the interaction inhibits ced-9
CC activity, either directly or indirectly (PubMed:23431138).
CC {ECO:0000269|PubMed:17336909, ECO:0000269|PubMed:23431138,
CC ECO:0000269|PubMed:24613396, ECO:0000269|PubMed:24968003}.
CC -!- INTERACTION:
CC Q94251; G5ECU1: skr-1; NbExp=3; IntAct=EBI-314286, EBI-323117;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17336909}. Cytoplasm
CC {ECO:0000269|PubMed:17336909}.
CC -!- TISSUE SPECIFICITY: In mid-embryogenesis, expression is most prominent
CC in epidermal and intestinal cells (PubMed:17336909). By the 1.5-fold
CC stage of embryogenesis, expression is additionally detected in neurons
CC and other cells (PubMed:17336909). During larval and adult stages,
CC highest expression is seen in epidermal seam cells and hypodermis
CC (PubMed:17336909). In larvae, strongly expressed in the P epidermal
CC blast cells and descendents that give rise to the vulva and weakly
CC expressed in the somatic gonad, including the gonadoblasts, the anchor
CC cell and the distal tip cells (PubMed:17336909). Some weak expression
CC also seen in adult spermatheca and uterus (PubMed:17336909). In the
CC musculature, expressed in the pharynx, anal depressor, sex muscles, and
CC body wall muscles. Detected in neurons of the head, tail, ventral cord
CC and periphery (PubMed:17336909). Also expressed in the embryonic tail
CC spike cell (PubMed:23431138). {ECO:0000269|PubMed:17336909,
CC ECO:0000269|PubMed:23431138}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected during mid-
CC embryogenesis with high levels in larvae and low levels in adults.
CC {ECO:0000269|PubMed:17336909}.
CC -!- DISRUPTION PHENOTYPE: Most mutants arrest as three-fold embryos that
CC fail to hatch and those that hatch arrest in L1 with many animals
CC appearing uncoordinated and misshapen (PubMed:17336909). 7- to 8-fold
CC increase in blmp-1 levels in seam and hypodermal cells
CC (PubMed:24613396). {ECO:0000269|PubMed:17336909,
CC ECO:0000269|PubMed:24613396}.
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DR EMBL; FO081056; CCD68857.1; -; Genomic_DNA.
DR RefSeq; NP_504661.1; NM_072260.5.
DR AlphaFoldDB; Q94251; -.
DR SMR; Q94251; -.
DR BioGRID; 44090; 5.
DR DIP; DIP-27041N; -.
DR IntAct; Q94251; 2.
DR STRING; 6239.K04A8.6; -.
DR EPD; Q94251; -.
DR PaxDb; Q94251; -.
DR PeptideAtlas; Q94251; -.
DR EnsemblMetazoa; K04A8.6a.1; K04A8.6a.1; WBGene00001089.
DR EnsemblMetazoa; K04A8.6a.2; K04A8.6a.2; WBGene00001089.
DR UCSC; K04A8.6; c. elegans.
DR WormBase; K04A8.6a; CE27388; WBGene00001089; dre-1.
DR eggNOG; KOG1777; Eukaryota.
DR GeneTree; ENSGT00530000063425; -.
DR HOGENOM; CLU_005078_1_0_1; -.
DR InParanoid; Q94251; -.
DR PhylomeDB; Q94251; -.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q94251; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001089; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q94251; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0008406; P:gonad development; IGI:WormBase.
DR GO; GO:0008078; P:mesodermal cell migration; IGI:WormBase.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:WormBase.
DR GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IMP:WormBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0040034; P:regulation of development, heterochronic; IMP:WormBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.160.20.10; -; 3.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR029799; FBX11/DRE-1.
DR InterPro; IPR022441; Para_beta_helix_rpt-2.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR22990:SF20; PTHR22990:SF20; 1.
DR Pfam; PF13229; Beta_helix; 2.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00722; CASH; 3.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00710; PbH1; 18.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF51126; SSF51126; 3.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR03804; para_beta_helix; 2.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Developmental protein; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..936
FT /note="F-box protein dre-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000430929"
FT DOMAIN 159..205
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 405..427
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 428..450
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 451..473
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 474..496
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 497..519
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REPEAT 520..542
FT /note="PbH1 6"
FT /evidence="ECO:0000255"
FT REPEAT 543..565
FT /note="PbH1 7"
FT /evidence="ECO:0000255"
FT REPEAT 566..588
FT /note="PbH1 8"
FT /evidence="ECO:0000255"
FT REPEAT 589..611
FT /note="PbH1 9"
FT /evidence="ECO:0000255"
FT REPEAT 612..634
FT /note="PbH1 10"
FT /evidence="ECO:0000255"
FT REPEAT 635..657
FT /note="PbH1 11"
FT /evidence="ECO:0000255"
FT REPEAT 658..680
FT /note="PbH1 12"
FT /evidence="ECO:0000255"
FT REPEAT 681..703
FT /note="PbH1 13"
FT /evidence="ECO:0000255"
FT REPEAT 704..726
FT /note="PbH1 14"
FT /evidence="ECO:0000255"
FT REPEAT 727..749
FT /note="PbH1 15"
FT /evidence="ECO:0000255"
FT REPEAT 750..772
FT /note="PbH1 16"
FT /evidence="ECO:0000255"
FT REPEAT 773..795
FT /note="PbH1 17"
FT /evidence="ECO:0000255"
FT REPEAT 796..818
FT /note="PbH1 18"
FT /evidence="ECO:0000255"
FT ZN_FING 843..914
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 275
FT /note="S->A: In ns39; strong tail spike cell survival
FT defect with 79% of animals possessing an inappropriately
FT surviving cell."
FT /evidence="ECO:0000269|PubMed:23431138"
FT MUTAGEN 514
FT /note="G->S: In dh99; failure of distal tip cells to
FT migrate completely back to the midbody, precocious fusion
FT of epidermal seam cells, molting defects, constitutive
FT dauer formation and increased blmp-1 levels."
FT /evidence="ECO:0000269|PubMed:17336909,
FT ECO:0000269|PubMed:24613396"
FT MUTAGEN 629
FT /note="G->R: In dh190/dh292; enhances gonadal heterochrony
FT phenotype in daf-12 null mutants."
FT /evidence="ECO:0000269|PubMed:17336909"
FT MUTAGEN 744
FT /note="G->R: In dh278/dh284; enhances gonadal heterochrony
FT phenotype in daf-12 null mutants."
FT /evidence="ECO:0000269|PubMed:17336909"
FT MUTAGEN 902
FT /note="A->V: In dh280; enhances gonadal heterochrony
FT phenotype in daf-12 null mutants."
FT /evidence="ECO:0000269|PubMed:17336909"
SQ SEQUENCE 936 AA; 105071 MW; 91E9907CDAC66587 CRC64;
MSSSSSPFFH PPPQQVMDDT TQQSPSYSQN SNSPSQHTFE SMEPAAGGST SMRYSPSGSS
EADNPTLGLF SAQASYPYSL RKRRPCLTKD EDLCFPITAA TADETPQPTM KKFKLECLSP
GEARDFSIED ESGTNLEAKM ETTECEPEEE EAVEEEDQQD HINRLPEELL LKVFSFLPDK
SLLACSSVSY RFNQISNSHE VWKELYCNLY DYRIPLFHPS HAKFEFREQS RWRDGNPWKE
SHRQLHHGVH VMKEPRVNLR SVNYRCFDQI EKAQSFLEED EYREKLIFLH TGVHEPIDTI
LINTDVQIIG ASDSRDITSS VVLEGSKNTA LTFTDGSANA YFGFITVRFR ADPVCRQQPQ
IAQQAQQMNH FYSILVTDKD AMPYIERCDI TSKVGNGAAV CVKKSAAPKF KYCTVLDCEN
VGIYITDNAT GHYEHCEIAR NTLAGVWVKN HANPYFRKCT IHSGKDVGVF TFEHGQGYFE
KCNIHSNRIS GIEVKNSANP VVIRCEVHHG YTGGIYVHER GRGQFMENRI YANAYAGIWI
TSHSDPTIRK NEIFTGQQGG VYIFGEGRGL IEQNNIYGNA LAGIQIRSQS DPIVRLNKIH
DGLHGGIYVH EKGRGLIEEN EVYGNTLAGI WVTTGSSPIL RKNRIHSGKQ VGVYFYDQGH
GLLEENDIFN HLYSGVQIRT GSNPKITRNK IWGGQNGGVL VYNGGKGCLE DNEIFDNAMA
GVWIKTDSEP TLRRNKIYDG RDGGVCIFNR GKGLLEDNEI FRNAQAGVLI STESNPTLRR
NRVFDGKSAG IEITNGATAT LEENQLFRNK YGGLCVATGV TPVQRGNRIY DNHDTISRAI
KTGLCLFKVS SNNSFPMHNF YRCTTCNTTE RNAICTNCIR TCHRGHSVEL VRFDRFFCDC
GAGTLERHCH LQNVPRDNDT VYDSATPIST ETGTEI
