SEL10_CAEBR
ID SEL10_CAEBR Reviewed; 589 AA.
AC Q61FW2; A8XCX4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=F-box/WD repeat-containing protein sel-10;
DE AltName: Full=Suppressor/enhancer of lin-12 protein 10;
GN Name=sel-10 {ECO:0000250|UniProtKB:Q93794}; ORFNames=CBG11475;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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. Regulates synapse elimination in early development in the
CC motor neuron HSNL. Cell autonomous negative regulator of lin-12/Notch-
CC mediated signaling, with respect to lin-12 activity in cell fate
CC decisions and tumorigenesis. May target the intracellular domains of
CC lin-12/Notch proteins for ubiquitin-dependent degradation. Involved in
CC sex determination by promoting female development. Potential regulator
CC of presenilin. May have a role in egg laying. Regulates zyg-1 levels
CC (possibly redundantly with lin-23) to control centrosome duplication
CC during mitosis. Negatively regulates lin-45 activity and protein
CC stability, probably by targeting it for ubiquitination and proteasomal
CC degradation. {ECO:0000250|UniProtKB:Q93794}.
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. Interacts with fem-1, fem-
CC 2, and fem-3. Interacts with the intracellular domain of glp-1 and sel-
CC 12. Interacts with lin-12. Interacts with skr-1. Interacts with zyg-1.
CC {ECO:0000250|UniProtKB:Q93794}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000250|UniProtKB:Q93794}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q93794}. Note=Expressed throughout the axon
CC throughout development. {ECO:0000250|UniProtKB:Q93794}.
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DR EMBL; HE600908; CAP30492.3; -; Genomic_DNA.
DR RefSeq; XP_002635232.1; XM_002635186.1.
DR AlphaFoldDB; Q61FW2; -.
DR SMR; Q61FW2; -.
DR STRING; 6238.CBG11475; -.
DR PRIDE; Q61FW2; -.
DR GeneID; 8577228; -.
DR KEGG; cbr:CBG_11475; -.
DR CTD; 8577228; -.
DR WormBase; CBG11475a; CBP46595; WBGene00032586; Cbr-sel-10.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_7_1; -.
DR InParanoid; Q61FW2; -.
DR OMA; HTGGVWT; -.
DR OrthoDB; 927943at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Cell projection; Cytoplasm; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..589
FT /note="F-box/WD repeat-containing protein sel-10"
FT /id="PRO_0000302093"
FT DOMAIN 123..169
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 255..295
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 297..335
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 338..375
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 378..415
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 418..457
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 463..502
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 503..541
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 65816 MW; 90E99E806CE081E6 CRC64;
MWPRNDVQMD EGSMTPEDQE PEPAIDQDME FDVNLEENSY SNGSGSSYNA DKLSSSSPLQ
HKLDLSASPT QNNEANPRVE HLVALFKDLT VAEQMEAFAR LVQESNMSNI RQMRAIIEPH
FQKDFLSCLP VEIGIKILQN LNSTDLMKVA QVSKNWKMLS EVEKVWKSLE DRGFKNLLEP
SDRTRGAWEA TAVIPGVNIP DHVNQCEINI HRLVKLLKYG PIYERSADKS RYLRGEKIEK
NWHSRPIMGS AILRGHEEHV ITCMQIHNDL LVTGSDDNTL KVWSIDDGEV KHTLNGHSGG
VWTSQISQCG RYIVSGSTDR TVKVWRAEDG FLLHTLQGHT STVRCMAMAN TTLVTGSRDC
TLRVWDIETG LHVRTLQGHQ AAVRCVQFDG NIVVSGGYDF TVKIWDAFSG KCLRTLIGHS
NRVYSLLYES ERSIVCSGSL DTSIRVWDFS RPEGQELIAF LSGHTSLTSG MQLRGNILVS
CNADSHVRVW DIYEGTCIHI LSGHRSAITS LQWFGRGLVA TSSDDGSVKL WDIERGVLIR
DLVSLNSGGN GGCIWRLCST QTMLACAIGS RNNTEETKVI LLDFDANHP
