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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.
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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
 
 
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