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 17-JUN-2020, entry version 125. 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). CC -!- FUNCTION: glp-1 and lin-12 promote signaling by recruiting lag-3 to CC target promoters, where it functions as a transcriptional activator CC (PubMed:10830967). May regulate phosphatase lip-1 mRNA transcription CC downstream of glp-1 (PubMed:16319922). {ECO:0000269|PubMed:10830967, CC ECO:0000269|PubMed:16319922}. CC -!- SUBUNIT: Associates with lag-1. 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. [Q09260-1] DR RefSeq; NP_001021195.1; NM_001026024.2. [Q09260-2] DR PDB; 2FO1; X-ray; 3.12 A; D=49-132. DR PDBsum; 2FO1; -. DR SMR; Q09260; -. DR BioGRID; 40704; 11. 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 KEGG; cel:CELE_C32A3.1; -. 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; KOG1290; Eukaryota. DR eggNOG; ENOG410XRBH; LUCA. 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 3 other tissues. DR GO; GO:0005634; C:nucleus; IDA:WormBase. DR GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:WormBase. DR GO; GO:0003713; F:transcription coactivator activity; IDA:WormBase. 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 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 COMPBIAS 162..467 FT /note="Gln-rich" FT COMPBIAS 185..188 FT /note="Poly-Gln" FT COMPBIAS 341..346 FT /note="Poly-Gln" FT COMPBIAS 353..357 FT /note="Poly-Gln" FT COMPBIAS 372..380 FT /note="Poly-Gln" FT COMPBIAS 390..400 FT /note="Poly-Gln" FT COMPBIAS 433..442 FT /note="Poly-Gln" 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:0000244|PDB:2FO1" FT HELIX 85..98 FT /evidence="ECO:0000244|PDB:2FO1" FT HELIX 100..112 FT /evidence="ECO:0000244|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 //