SEL10_CAEEL
ID SEL10_CAEEL Reviewed; 587 AA.
AC Q93794; O44083; Q95ZT0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=F-box/WD repeat-containing protein sel-10;
DE AltName: Full=Egg laying defective protein 41 {ECO:0000303|PubMed:15306688};
DE AltName: Full=Suppressor/enhancer of lin-12 protein 10;
GN Name=sel-10 {ECO:0000312|WormBase:F55B12.3a};
GN Synonyms=egl-41 {ECO:0000312|WormBase:F55B12.3a};
GN ORFNames=F55B12.3 {ECO:0000312|WormBase:F55B12.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND INTERACTION WITH
RP LIN-12.
RX PubMed=9389650; DOI=10.1101/gad.11.23.3182;
RA Hubbard E.J.A., Wu G., Kitajewski J., Greenwald I.;
RT "sel-10, a negative regulator of lin-12 activity in Caenorhabditis elegans,
RT encodes a member of the CDC4 family of proteins.";
RL Genes Dev. 11:3182-3193(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
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]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8293978; DOI=10.1093/genetics/135.3.765;
RA Sundaram M., Greenwald I.;
RT "Suppressors of a lin-12 hypomorph define genes that interact with both
RT lin-12 and glp-1 in Caenorhabditis elegans.";
RL Genetics 135:765-783(1993).
RN [4]
RP FUNCTION, AND INTERACTION WITH GLP-1 AND SEL-12.
RX PubMed=9861048; DOI=10.1073/pnas.95.26.15787;
RA Wu G., Hubbard E.J.A., Kitajewski J.K., Greenwald I.;
RT "Evidence for functional and physical association between Caenorhabditis
RT elegans SEL-10, a Cdc4p-related protein, and SEL-12 presenilin.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15787-15791(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH FEM-1; FEM-2 AND FEM-3.
RX PubMed=15306688; DOI=10.1073/pnas.0405087101;
RA Jaeger S., Schwartz H.T., Horvitz H.R., Conradt B.;
RT "The Caenorhabditis elegans F-box protein SEL-10 promotes female
RT development and may target FEM-1 and FEM-3 for degradation by the
RT proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12549-12554(2004).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=17626846; DOI=10.1126/science.1145727;
RA Ding M., Chao D., Wang G., Shen K.;
RT "Spatial regulation of an E3 ubiquitin ligase directs selective synapse
RT elimination.";
RL Science 317:947-951(2007).
RN [7]
RP FUNCTION, INTERACTION WITH SKR-1, AND MUTAGENESIS OF GLY-567.
RX PubMed=18718460; DOI=10.1016/j.ydbio.2008.07.035;
RA Killian D.J., Harvey E., Johnson P., Otori M., Mitani S., Xue D.;
RT "SKR-1, a homolog of Skp1 and a member of the SCF(SEL-10) complex,
RT regulates sex-determination and LIN-12/Notch signaling in C. elegans.";
RL Dev. Biol. 322:322-331(2008).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19528325; DOI=10.1534/genetics.109.104885;
RA Dorfman M., Gomes J.E., O'Rourke S., Bowerman B.;
RT "Using RNA interference to identify specific modifiers of a temperature-
RT sensitive, embryonic-lethal mutation in the Caenorhabditis elegans
RT ubiquitin-like Nedd8 protein modification pathway E1-activating gene rfl-
RT 1.";
RL Genetics 182:1035-1049(2009).
RN [9]
RP FUNCTION, INTERACTION WITH ZYG-1, AND DISRUPTION PHENOTYPE.
RX PubMed=22623721; DOI=10.1242/jcs.097105;
RA Peel N., Dougherty M., Goeres J., Liu Y., O'Connell K.F.;
RT "The C. elegans F-box proteins LIN-23 and SEL-10 antagonize centrosome
RT duplication by regulating ZYG-1 levels.";
RL J. Cell Sci. 125:3535-3544(2012).
RN [10]
RP FUNCTION.
RX PubMed=23154983; DOI=10.1101/gad.203703.112;
RA de la Cova C., Greenwald I.;
RT "SEL-10/Fbw7-dependent negative feedback regulation of LIN-45/Braf
RT signaling in C. elegans via a conserved phosphodegron.";
RL Genes Dev. 26:2524-2535(2012).
CC -!- FUNCTION: Probable substrate recognition component of SCF (SKP1-CUL-F-
CC box protein) E3 ubiquitin-protein ligase complex, which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (PubMed:17626846). Regulates synapse elimination in early
CC development in the motor neuron HSNL (PubMed:17626846). Cell autonomous
CC negative regulator of lin-12/Notch-mediated signaling, with respect to
CC lin-12 activity in cell fate decisions and tumorigenesis
CC (PubMed:9389650). May target the intracellular domains of lin-12/Notch
CC proteins for ubiquitin-dependent degradation (PubMed:9389650). Involved
CC in sex determination by promoting female development (PubMed:15306688,
CC PubMed:18718460). Potential regulator of presenilin (PubMed:9861048).
CC May have a role in egg laying (PubMed:8293978, PubMed:15306688).
CC Regulates zyg-1 levels (possibly redundantly with lin-23) to control
CC centrosome duplication during mitosis (PubMed:22623721). Negatively
CC regulates lin-45 activity and protein stability, probably by targeting
CC it for ubiquitination and proteasomal degradation (PubMed:23154983).
CC {ECO:0000269|PubMed:15306688, ECO:0000269|PubMed:17626846,
CC ECO:0000269|PubMed:18718460, ECO:0000269|PubMed:22623721,
CC ECO:0000269|PubMed:23154983, ECO:0000269|PubMed:8293978,
CC ECO:0000269|PubMed:9389650, ECO:0000269|PubMed:9861048}.
CC -!- SUBUNIT: Probable component of the SCF(sel-10) E3 ubiquitin-protein
CC ligase complex which includes skr-1 and F-box domain-containing protein
CC sel-10 as a substrate recognition component (PubMed:17626846).
CC Interacts with fem-1, fem-2, and fem-3 (PubMed:15306688). Interacts
CC with the intracellular domain of glp-1 and sel-12 (PubMed:9861048).
CC Interacts with lin-12 (PubMed:9389650). Interacts with skr-1
CC (PubMed:18718460). Interacts with zyg-1 (PubMed:22623721).
CC {ECO:0000269|PubMed:15306688, ECO:0000269|PubMed:17626846,
CC ECO:0000269|PubMed:18718460, ECO:0000269|PubMed:22623721,
CC ECO:0000269|PubMed:9389650, ECO:0000269|PubMed:9861048}.
CC -!- INTERACTION:
CC Q93794; P17221: fem-1; NbExp=2; IntAct=EBI-323098, EBI-1998155;
CC Q93794; P49594: fem-2; NbExp=2; IntAct=EBI-323098, EBI-1998402;
CC Q93794; P34691: fem-3; NbExp=2; IntAct=EBI-323098, EBI-445465;
CC Q93794; P14585: lin-12; NbExp=3; IntAct=EBI-323098, EBI-326049;
CC Q93794; G5ECU1: skr-1; NbExp=5; IntAct=EBI-323098, EBI-323117;
CC Q93794; P31695: Notch4; Xeno; NbExp=2; IntAct=EBI-323098, EBI-643670;
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:17626846}. Cytoplasm {ECO:0000269|PubMed:19528325}.
CC Note=Expressed throughout the axon throughout development.
CC {ECO:0000269|PubMed:17626846}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q93794-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q93794-2; Sequence=VSP_009813;
CC -!- TISSUE SPECIFICITY: Expressed in tail and head neurons.
CC {ECO:0000269|PubMed:19528325}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at the 50-cell embryonic stage
CC and continues throughout development (PubMed:19528325). Expressed in
CC the HSNL motor neuron from early larval stage L4 to the young adult
CC stage (PubMed:17626846). {ECO:0000269|PubMed:17626846,
CC ECO:0000269|PubMed:19528325}.
CC -!- DISRUPTION PHENOTYPE: Worms show a weak masculinization phenotype
CC (PubMed:8293978). Moreover sel-10 mutants suppress the egg laying
CC defective (egl) phenotype of the sel-12 mutants (PubMed:8293978). RNAi-
CC mediated knockdown results in increased zyg-1 expression at centrosomes
CC (PubMed:22623721). {ECO:0000269|PubMed:22623721,
CC ECO:0000269|PubMed:8293978}.
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DR EMBL; AF020788; AAC47809.1; -; mRNA.
DR EMBL; Z79757; CAB02129.2; -; Genomic_DNA.
DR EMBL; Z79757; CAC42307.1; -; Genomic_DNA.
DR PIR; T22703; T22703.
DR RefSeq; NP_001023975.1; NM_001028804.2. [Q93794-2]
DR RefSeq; NP_506421.1; NM_074020.5. [Q93794-1]
DR AlphaFoldDB; Q93794; -.
DR SMR; Q93794; -.
DR BioGRID; 44892; 18.
DR IntAct; Q93794; 11.
DR MINT; Q93794; -.
DR STRING; 6239.F55B12.3a; -.
DR iPTMnet; Q93794; -.
DR EPD; Q93794; -.
DR PaxDb; Q93794; -.
DR PeptideAtlas; Q93794; -.
DR EnsemblMetazoa; F55B12.3a.1; F55B12.3a.1; WBGene00004767. [Q93794-1]
DR EnsemblMetazoa; F55B12.3b.1; F55B12.3b.1; WBGene00004767. [Q93794-2]
DR GeneID; 179878; -.
DR KEGG; cel:CELE_F55B12.3; -.
DR UCSC; F55B12.3b.1; c. elegans. [Q93794-1]
DR CTD; 179878; -.
DR WormBase; F55B12.3a; CE25007; WBGene00004767; sel-10. [Q93794-1]
DR WormBase; F55B12.3b; CE27762; WBGene00004767; sel-10. [Q93794-2]
DR eggNOG; KOG0274; Eukaryota.
DR GeneTree; ENSGT00940000174696; -.
DR InParanoid; Q93794; -.
DR OMA; HTGGVWT; -.
DR OrthoDB; 927943at2759; -.
DR PhylomeDB; Q93794; -.
DR SignaLink; Q93794; -.
DR PRO; PR:Q93794; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004767; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0046660; P:female sex differentiation; IMP:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:UniProtKB.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IGI:WormBase.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0040028; P:regulation of vulval development; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Developmental protein;
KW Differentiation; Reference proteome; Repeat; Sexual differentiation;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..587
FT /note="F-box/WD repeat-containing protein sel-10"
FT /id="PRO_0000051212"
FT DOMAIN 121..167
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 253..291
FT /note="WD 1"
FT REPEAT 294..333
FT /note="WD 2"
FT REPEAT 336..373
FT /note="WD 3"
FT REPEAT 376..415
FT /note="WD 4"
FT REPEAT 416..455
FT /note="WD 5"
FT REPEAT 461..498
FT /note="WD 6"
FT REPEAT 501..539
FT /note="WD 7"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 54..55
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_009813"
FT MUTAGEN 567
FT /note="G->E: In n1074; masculinizing phenotype. Does not
FT self-interact in vitro or bind to skr-1 protein."
FT /evidence="ECO:0000269|PubMed:18718460"
SQ SEQUENCE 587 AA; 65312 MW; 2D3970B4EFAA1B8C CRC64;
MWPRNDVHMD DGSMTPEDQE PVTDNDMEYN DNGEESSYSN GSSSSYNADK LSSSRPLQHK
LDLSASPSRN NDLNPRVEHL IALFKDLSSA EQMDAFTRLL QESNMTNIRQ LRAIIEPHFQ
RDFLSCLPVE LGMKILHNLT GYDLLKVAQV SKNWKLISEI DKIWKSLGVE EFKHHPDPTD
RVTGAWQGTA IAAGVTIPDH IQPCDLNVHR FLKLQKFGDI FERAADKSRY LRADKIEKNW
NANPIMGSAV LRGHEDHVIT CMQIHDDVLV TGSDDNTLKV WCIDKGEVMY TLVGHTGGVW
TSQISQCGRY IVSGSTDRTV KVWSTVDGSL LHTLQGHTST VRCMAMAGSI LVTGSRDTTL
RVWDVESGRH LATLHGHHAA VRCVQFDGTT VVSGGYDFTV KIWNAHTGRC IRTLTGHNNR
VYSLLFESER SIVCSGSLDT SIRVWDFTRP EGQECVALLQ GHTSLTSGMQ LRGNILVSCN
ADSHVRVWDI HEGTCVHMLS GHRSAITSLQ WFGRNMVATS SDDGTVKLWD IERGALIRDL
VTLDSGGNGG CIWRLCSTST MLACAVGSRN NTEETKVILL DFDAVYP
