ID LAG3_CAEEL Reviewed; 490 AA. AC Q09260; Q9NGS2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 02-JUN-2021, entry version 130. DE RecName: Full=Protein lag-3; DE AltName: Full=Abnormal cell lineage protein 3; DE AltName: Full=Abnormal germline proliferation protein 3; GN Name=sel-8; Synonyms=lag-3; ORFNames=C32A3.1; 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] (ISOFORMS A AND B), AND FUNCTION. RX PubMed=10830967; DOI=10.1038/35012645; RA Petcherski A.G., Kimble J.; RT "LAG-3 is a putative transcriptional activator in the C. elegans Notch RT pathway."; RL Nature 405:364-368(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). RN [3] RP FUNCTION. RX PubMed=16319922; DOI=10.1038/sj.emboj.7600901; RA Lee M.H., Hook B., Lamont L.B., Wickens M., Kimble J.; RT "LIP-1 phosphatase controls the extent of germline proliferation in RT Caenorhabditis elegans."; RL EMBO J. 25:88-96(2006). RN [4] {ECO:0007744|PDB:2FO1} RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 52-114 IN COMPLEX WITH LIN-12; RP LAG-1 AND DNA. RX PubMed=16530045; DOI=10.1016/j.cell.2006.01.035; RA Wilson J.J., Kovall R.A.; RT "Crystal structure of the CSL-Notch-Mastermind ternary complex bound to RT DNA."; RL Cell 124:985-996(2006). CC -!- FUNCTION: glp-1 and lin-12 Notch proteins promote signaling by CC recruiting lag-3 to target promoters, where it functions as a CC transcriptional activator, probably as part of a complex with a Notch CC intracellular domain (NICD) and the transcription regulator lag-1 CC (PubMed:10830967, PubMed:16530045). May regulate phosphatase lip-1 mRNA CC transcription downstream of glp-1 (PubMed:16319922). CC {ECO:0000269|PubMed:10830967, ECO:0000269|PubMed:16319922, CC ECO:0000269|PubMed:16530045}. CC -!- SUBUNIT: Component of a complex consisting of at least lag-1, lin- CC 12/Notch and lag-3 (PubMed:16530045, PubMed:10830967). Interacts with a CC Notch intracellular domain (NICD) of lin-12/Notch or glp-1/Notch; the CC interactions are direct (PubMed:16530045, PubMed:10830967). CC {ECO:0000269|PubMed:10830967, ECO:0000269|PubMed:16530045}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; CC IsoId=Q09260-1; Sequence=Displayed; CC Name=b; CC IsoId=Q09260-2; Sequence=VSP_003908; 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; AF241847; AAF71523.1; -; mRNA. DR EMBL; AF241846; AAF71522.1; -; mRNA. DR EMBL; Z48241; CAA88284.1; -; Genomic_DNA. DR EMBL; Z48241; CAC42265.1; -; Genomic_DNA. DR PIR; T19628; T19628. DR RefSeq; NP_001021194.1; NM_001026023.2. DR RefSeq; NP_001021195.1; NM_001026024.2. [Q09260-2] DR PDB; 2FO1; X-ray; 3.12 A; D=52-114. DR PDBsum; 2FO1; -. DR SMR; Q09260; -. DR BioGRID; 40704; 16. DR ComplexPortal; CPX-3152; CSL-Notch-Mastermind transcription factor complex. DR IntAct; Q09260; 3. DR STRING; 6239.C32A3.1a; -. DR PaxDb; Q09260; -. DR EnsemblMetazoa; C32A3.1a.1; C32A3.1a.1; WBGene00004765. [Q09260-1] DR EnsemblMetazoa; C32A3.1b.1; C32A3.1b.1; WBGene00004765. [Q09260-2] DR GeneID; 175464; -. DR UCSC; C32A3.1b.2; c. elegans. [Q09260-1] DR CTD; 175464; -. DR WormBase; C32A3.1a; CE27810; WBGene00004765; sel-8. [Q09260-1] DR WormBase; C32A3.1b; CE01505; WBGene00004765; sel-8. [Q09260-2] DR eggNOG; ENOG502QRT9; Eukaryota. DR HOGENOM; CLU_696827_0_0_1; -. DR InParanoid; Q09260; -. DR OMA; HTPFANI; -. DR OrthoDB; 1557766at2759; -. DR SignaLink; Q09260; -. DR EvolutionaryTrace; Q09260; -. DR PRO; PR:Q09260; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00004765; Expressed in multi-cellular organism and 4 other tissues. DR GO; GO:0005634; C:nucleus; IDA:WormBase. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:WormBase. DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:WormBase. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0007219; P:Notch signaling pathway; IDA:WormBase. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:WormBase. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase. DR DisProt; DP02378; -. DR IDEAL; IID50087; -. DR InterPro; IPR021587; Transcription_activator_LAG-3. DR Pfam; PF11498; Activator_LAG-3; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Nucleus; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..490 FT /note="Protein lag-3" FT /id="PRO_0000084353" FT REGION 18..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 105..155 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 213..235 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 307..362 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 391..490 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 118..136 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 213..233 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 307..322 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 334..362 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 391..456 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..22 FT /note="Missing (in isoform b)" FT /evidence="ECO:0000303|PubMed:10830967" FT /id="VSP_003908" FT HELIX 60..83 FT /evidence="ECO:0007829|PDB:2FO1" FT HELIX 85..98 FT /evidence="ECO:0007829|PDB:2FO1" FT HELIX 100..112 FT /evidence="ECO:0007829|PDB:2FO1" SQ SEQUENCE 490 AA; 56482 MW; 396A6C194C382A07 CRC64; MDDLSEFFVI EEMFISEPSV AGMKPSTSKT THSPPPEEPT APFVNDNLPN PEDEPTIGDL NAFHSGEELH RQRSELARAN YEKARPEMIA NQRAVTAHLF NRYTEDEERK RVEQQKNKEA MNASTSAPTS SRNGGQSVEN RKRRNDVVVA PPTSEEEWKR AQQQHWMGQQ QPQMQFQMQQ QYHSQQQQYI MMQQQHHHMT GMQQIHHQMP STSSADSIRS VPTPASSMHQ PSPAEMRNGC GMSRNATMDM TCSPMSGGQP IVDENNLAVP EGEWFDKLAL AVAEQYNVDT ILGPDTYDTF LAELDFSSSE SPTKQSPMEM NGDRMPSTAP PPAQNPQHIA QLQQQQNKMR LMQQQQQEMQ RIEQQRRQQI MQQQQQQQQQ EHQRQQMLLQ QQQQQQQMQQ HHQMNGGGQF ATQAHQQAAY MQQMQRMEQI RHQQQQAQQH QQAQQQHQQQ AQHHQMGYGI PNGYPQQMHM HPPAYGAHHM PQPTAFANIN //