ID LAC1_MOUSE Reviewed; 105 AA. AC P01843; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 02-SEP-2026, entry version 165. DE RecName: Full=Ig lambda-1 chain C region; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6812053; DOI=10.1073/pnas.79.15.4681; RA Selsing E., Miller J., Wilson R., Storb U.; RT "Evolution of mouse immunoglobulin lambda genes."; RL Proc. Natl. Acad. Sci. U.S.A. 79:4681-4685(1982). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (MOPC 315). RX PubMed=6259534; DOI=10.1038/290065a0; RA Bothwell A.L.M., Paskind M., Schwartz R.C., Sonenshein G.E., Gefter M.L., RA Baltimore D.; RT "Dual expression of lambda genes in the MOPC-315 plasmacytoma."; RL Nature 290:65-67(1981). RN [3] RP NUCLEOTIDE SEQUENCE (S43). RX PubMed=6283385; DOI=10.1038/298380a0; RA Bothwell A.L.M., Paskind M., Reth M., Imanishi-Kari T., Rajewsky K., RA Baltimore D.; RT "Somatic variants of murine immunoglobulin lambda light chains."; RL Nature 298:380-382(1982). RN [4] RP PROTEIN SEQUENCE (MYELOMA PROTEIN MOPC 104E). RX PubMed=5276767; DOI=10.1073/pnas.68.3.590; RA Appella E.; RT "Amino acid sequences of two mouse immunoglobulin lambda chains."; RL Proc. Natl. Acad. Sci. U.S.A. 68:590-594(1971). CC -!- MISCELLANEOUS: The MOPC-315 cell line produces 2 light chains, 1 normal CC lambda-2 chain and 1 abnormal lambda-1 chain that is missing a large CC part of the V region. The C region sequence (shown here) appears CC completely normal. 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; J00582; AAA51636.1; -; mRNA. DR EMBL; J00587; AAB59672.1; -; Genomic_DNA. DR PIR; A93922; L1MS. DR PDB; 1JN6; X-ray; 2.70 A; A=1-100. DR PDB; 1JNH; X-ray; 2.85 A; A/C/E/G=1-102. DR AlphaFoldDB; P01843; -. DR SMR; P01843; -. DR FunCoup; P01843; 379. DR MINT; P01843; -. DR GlyGen; P01843; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P01843; -. DR jPOST; P01843; -. DR PeptideAtlas; P01843; -. DR ABCD; P01843; 1 sequenced antibody. DR InParanoid; P01843; -. DR OMA; LWWVFGG; -. DR EvolutionaryTrace; P01843; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P01843; protein. DR GO; GO:0071735; C:IgG immunoglobulin complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0003823; F:antigen binding; IBA:GO_Central. DR GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central. DR CDD; cd07699; IgC1_L; 1. DR FunFam; 2.60.40.10:FF:000283; Immunoglobulin kappa constant; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR050160; MHC/Immunoglobulin. DR PANTHER; PTHR19944:SF98; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR19944; MHC CLASS II-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. DR PDBsum; 1JN6; -. DR PDBsum; 1JNH; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; KW Immunoglobulin domain; Reference proteome. FT CHAIN <1..105 FT /note="Ig lambda-1 chain C region" FT /id="PRO_0000153608" FT DOMAIN 6..100 FT /note="Ig-like" FT DISULFID 27..86 FT DISULFID 104 FT /note="Interchain (with heavy chain)" FT CONFLICT 19..20 FT /note="ET -> TE (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 56 FT /note="Q -> E (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 75 FT /note="Missing (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 81..82 FT /note="HS -> SH (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 85 FT /note="S -> SS (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 96 FT /note="E -> Q (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT NON_TER 1 FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:1JN6" FT HELIX 12..14 FT /evidence="ECO:0007829|PDB:1JN6" FT HELIX 15..18 FT /evidence="ECO:0007829|PDB:1JN6" FT TURN 19..21 FT /evidence="ECO:0007829|PDB:1JN6" FT STRAND 22..35 FT /evidence="ECO:0007829|PDB:1JN6" FT STRAND 38..43 FT /evidence="ECO:0007829|PDB:1JN6" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:1JN6" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:1JN6" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:1JN6" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:1JN6" FT STRAND 64..74 FT /evidence="ECO:0007829|PDB:1JN6" FT HELIX 75..80 FT /evidence="ECO:0007829|PDB:1JN6" FT STRAND 84..90 FT /evidence="ECO:0007829|PDB:1JN6" FT STRAND 93..99 FT /evidence="ECO:0007829|PDB:1JN6" SQ SEQUENCE 105 AA; 11575 MW; A89F2B09BCFCA018 CRC64; QPKSSPSVTL FPPSSEELET NKATLVCTIT DFYPGVVTVD WKVDGTPVTQ GMETTQPSKQ SNNKYMASSY LTLTARAWER HSSYSCQVTH EGHTVEKSLS RADCS //