LIN23_CAEEL
ID LIN23_CAEEL Reviewed; 665 AA.
AC Q09990; Q9GNN6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=F-box/WD repeat-containing protein lin-23;
DE AltName: Full=Abnormal cell lineage protein 23;
GN Name=lin-23; ORFNames=K10B2.1;
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], FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS
RP OF GLY-441.
RX PubMed=11060233; DOI=10.1242/dev.127.23.5071;
RA Kipreos E.T., Gohel S.P., Hedgecock E.M.;
RT "The Caenorhabditis elegans F-box/WD-repeat protein lin-23 functions to
RT limit cell division during development.";
RL Development 127:5071-5082(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
CC -!- FUNCTION: Functions cell autonomously to negatively regulate cell cycle
CC progression. Required to restrain cell proliferation in response to
CC developmental cues. Probably recognizes and binds to some proteins and
CC promotes their ubiquitination and degradation (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:11060233}.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highest levels in embryos and adults, lowest
CC levels in larvae. Maternal expression results in high zygotic levels.
CC {ECO:0000269|PubMed:11060233}.
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DR EMBL; AF275253; AAG28037.1; -; mRNA.
DR EMBL; FO080748; CCD66391.1; -; Genomic_DNA.
DR PIR; T16607; T16607.
DR RefSeq; NP_495285.1; NM_062884.5.
DR AlphaFoldDB; Q09990; -.
DR SMR; Q09990; -.
DR BioGRID; 39398; 10.
DR STRING; 6239.K10B2.1; -.
DR EPD; Q09990; -.
DR PaxDb; Q09990; -.
DR PeptideAtlas; Q09990; -.
DR EnsemblMetazoa; K10B2.1a.1; K10B2.1a.1; WBGene00003009.
DR GeneID; 174058; -.
DR UCSC; K10B2.1; c. elegans.
DR CTD; 174058; -.
DR WormBase; K10B2.1a; CE28600; WBGene00003009; lin-23.
DR eggNOG; KOG0281; Eukaryota.
DR GeneTree; ENSGT00940000155898; -.
DR HOGENOM; CLU_000288_103_6_1; -.
DR InParanoid; Q09990; -.
DR PhylomeDB; Q09990; -.
DR SignaLink; Q09990; -.
DR PRO; PR:Q09990; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003009; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q09990; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IPI:WormBase.
DR GO; GO:0019902; F:phosphatase binding; IPI:WormBase.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0034511; F:U3 snoRNA binding; IEA:InterPro.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:WormBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:WormBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR021977; Beta-TrCP_D.
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; IPR039241; Rrp9-like.
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 PANTHER; PTHR19865; PTHR19865; 1.
DR Pfam; PF12125; Beta-TrCP_D; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM01028; Beta-TrCP_D; 1.
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 Cell cycle; Cell division; Cytoplasm; Developmental protein;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..665
FT /note="F-box/WD repeat-containing protein lin-23"
FT /id="PRO_0000051058"
FT DOMAIN 81..127
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 220..257
FT /note="WD 1"
FT REPEAT 260..299
FT /note="WD 2"
FT REPEAT 301..337
FT /note="WD 3"
FT REPEAT 343..380
FT /note="WD 4"
FT REPEAT 383..420
FT /note="WD 5"
FT REPEAT 423..460
FT /note="WD 6"
FT REPEAT 472..509
FT /note="WD 7"
FT REGION 574..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 441
FT /note="G->R: In Lin-32(RH293)."
FT /evidence="ECO:0000269|PubMed:11060233"
SQ SEQUENCE 665 AA; 75917 MW; BF3E9AF51F12ECCC CRC64;
MSSPHRASTT QQLADLSLTE GEHDEGKPLS IDYLQGHEGL IEEVLKWSEH EQLDFMDKIV
HRLSHYQLGK VDNFIRPMLQ RDFISNLPAH LVELILFNVN SDSLKSCEEV STSWRCALAR
GQHWKKLIEK NVRSDSLWWG LSEKRQWDKF LNISRDMSVR RICEKFNYDV NIKRDKLDQL
ILMHVFYSKL YPKIIRDIHN IDNNWKRGNY KMTRINCQSE NSKGVYCLQY DDDKIVSGLR
DNTIKIWDRK DYSCSRILSG HTGSVLCLQY DNRVIISGSS DATVRVWDVE TGECIKTLIH
HCEAVLHLRF ANGIMVTCSK DRSIAVWDMV SPRDITIRRV LVGHRAAVNV VDFDDRYIVS
ASGDRTIKVW SMDTLEFVRT LAGHRRGIAC LQYRGRLVVS GSSDNTIRLW DIHSGVCLRV
LEGHEELVRC IRFDEKRIVS GAYDGKIKVW DLQAALDPRA LSSEICLCSL VQHTGRVFRL
QFDDFQIVSS SHDDTILIWD FLDAPPSGLP SSTNRATLPE LPNQAAVARA QMLFEMAARR
EIERRDREVV EEPALRPRAN AARRHNADIA AAAAAAEAAR GAGDNDESSS EEDLDRVDQV
NNPNVAGPAP PQPHNQNHRR RQPRPELPVR LMQEMAAFDN MRRQQNNMDH LGGGDVDEEM
PDGGP
