LV1B_MOUSE
ID LV1B_MOUSE Reviewed; 129 AA.
AC P01724;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Ig lambda-1 chain V regions MOPC 104E/RPC20/J558/S104;
DE Flags: Precursor;
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 PROTEIN SEQUENCE OF 1-29 (PRECURSOR PROTEIN), AND SEQUENCE REVISION TO 20
RP AND 26.
RX PubMed=403522; DOI=10.1073/pnas.74.2.716;
RA Burstein Y., Schechter I.;
RT "Amino acid sequence of the NH2-terminal extra piece segments of the
RT precursors of mouse immunoglobulin lambda1-type and kappa-type light
RT chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:716-720(1977).
RN [2]
RP PROTEIN SEQUENCE OF 20-129, AND PYROGLUTAMATE FORMATION AT GLN-20.
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).
RN [3]
RP PROTEIN SEQUENCE OF 20-129 (J558 AND S104).
RX PubMed=4516208; DOI=10.1073/pnas.70.7.2112;
RA Cesari I.M., Weigert M.;
RT "Mouse lambda-chain sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 70:2112-2116(1973).
CC -!- MISCELLANEOUS: Compositions and partial sequences of RPC 20 show no
CC differences from MOPC 104E. The sequences of J558 and S104 seems
CC identical with that shown.
CC -!- MISCELLANEOUS: These proteins were isolated from serum or urine of
CC tumor-bearing mice.
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 PIR; B93815; L1MS4E.
DR PIR; PH1089; PH1089.
DR PDB; 1A6U; X-ray; 2.10 A; L=21-128.
DR PDB; 1A6V; X-ray; 1.80 A; L/M/N=20-128.
DR PDB; 1A6W; X-ray; 2.00 A; L=21-128.
DR PDB; 1DL7; X-ray; 2.35 A; L=20-128.
DR PDB; 1OAQ; X-ray; 1.50 A; L=20-129.
DR PDB; 1OAR; X-ray; 2.23 A; L/M/N/O=20-128.
DR PDB; 1OAU; X-ray; 1.80 A; L/M/N/O=20-128.
DR PDB; 1OAX; X-ray; 2.67 A; L/M/N/O=20-128.
DR PDB; 1OAY; X-ray; 2.66 A; L/M/N/O=20-128.
DR PDB; 1OAZ; X-ray; 2.78 A; L/N=20-128.
DR PDB; 1OCW; X-ray; 2.00 A; L=20-128.
DR PDB; 1Q0Y; X-ray; 2.00 A; L=21-129.
DR PDB; 2BJM; X-ray; 2.15 A; L=20-128.
DR PDBsum; 1A6U; -.
DR PDBsum; 1A6V; -.
DR PDBsum; 1A6W; -.
DR PDBsum; 1DL7; -.
DR PDBsum; 1OAQ; -.
DR PDBsum; 1OAR; -.
DR PDBsum; 1OAU; -.
DR PDBsum; 1OAX; -.
DR PDBsum; 1OAY; -.
DR PDBsum; 1OAZ; -.
DR PDBsum; 1OCW; -.
DR PDBsum; 1Q0Y; -.
DR PDBsum; 2BJM; -.
DR AlphaFoldDB; P01724; -.
DR SMR; P01724; -.
DR MINT; P01724; -.
DR MaxQB; P01724; -.
DR PRIDE; P01724; -.
DR PhylomeDB; P01724; -.
DR EvolutionaryTrace; P01724; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01724; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; 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; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Direct protein sequencing; Immunity;
KW Immunoglobulin; Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:403522,
FT ECO:0000269|PubMed:4516208, ECO:0000269|PubMed:5276767"
FT CHAIN 20..129
FT /note="Ig lambda-1 chain V regions MOPC
FT 104E/RPC20/J558/S104"
FT /id="PRO_0000015202"
FT DOMAIN 20..125
FT /note="Ig-like"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:5276767"
FT NON_TER 129
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1OAQ"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1OAQ"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:1OAQ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1OAY"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1OAQ"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1OAQ"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1OAQ"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1OAQ"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1OAQ"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1OAQ"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:1OAQ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1OAQ"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:1OAQ"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1OAQ"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1OAQ"
SQ SEQUENCE 129 AA; 13479 MW; 03629939D5791AC0 CRC64;
MAWISLILSL LALSSGAISQ AVVTQESALT TSPGETVTLT CRSSTGAVTT SNYANWVQQK
PDHLFTGLIG GTNNRAPGVP ARFSGSLIGN KAALTITGAQ TEDEAIYFCA LWYSNHWVFG
GGTKLTVLG