LAC1_MOUSE
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 25-MAY-2022, entry version 149.
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.
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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=1-100.
DR PDBsum; 1JN6; -.
DR PDBsum; 1JNH; -.
DR AlphaFoldDB; P01843; -.
DR SMR; P01843; -.
DR MINT; P01843; -.
DR iPTMnet; P01843; -.
DR EPD; P01843; -.
DR MaxQB; P01843; -.
DR PeptideAtlas; P01843; -.
DR PRIDE; P01843; -.
DR ABCD; P01843; 1 sequenced antibody.
DR OMA; MACCAQW; -.
DR EvolutionaryTrace; P01843; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01843; protein.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; 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:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
DR GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 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 Pfam; PF07654; C1-set; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
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 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
