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HVM20_MOUSE
ID   HVM20_MOUSE             Reviewed;         122 AA.
AC   P01789;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Ig heavy chain V region M603;
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.
RX   PubMed=6769593; DOI=10.1016/0092-8674(80)90089-6;
RA   Early P., Huang H., Davis M., Calame K., Hood L.;
RT   "An immunoglobulin heavy chain variable region gene is generated from three
RT   segments of DNA: VH, D and JH.";
RL   Cell 19:981-992(1980).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-120.
RX   PubMed=4213527; DOI=10.1021/bi00716a034;
RA   Rudikoff S., Potter M.;
RT   "Variable region sequence of the heavy chain from a phosphorylcholine
RT   binding myeloma protein.";
RL   Biochemistry 13:4033-4038(1974).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF FAB FRAGMENT.
RX   PubMed=4530984; DOI=10.1073/pnas.71.11.4298;
RA   Segal D.M., Padlan E.A., Cohen G.H., Rudikoff S., Potter M., Davies D.R.;
RT   "The three-dimensional structure of a phosphorylcholine-binding mouse
RT   immunoglobulin Fab and the nature of the antigen binding site.";
RL   Proc. Natl. Acad. Sci. U.S.A. 71:4298-4302(1974).
CC   -!- MISCELLANEOUS: This chain was isolated from a myeloma protein that
CC       binds phosphorylcholine.
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DR   PIR; A30539; A30539.
DR   PIR; A30556; A30556.
DR   PIR; B30540; B30540.
DR   PIR; B30556; B30556.
DR   PIR; B90795; AVMS63.
DR   PIR; D30556; D30556.
DR   PIR; E30539; E30539.
DR   PIR; H30539; H30539.
DR   PIR; I30535; I30535.
DR   PIR; PT0354; PT0354.
DR   PDB; 1MCP; X-ray; 2.70 A; H=1-122.
DR   PDB; 2CJU; X-ray; 2.50 A; H=1-121.
DR   PDB; 2MCP; X-ray; 3.10 A; H=1-122.
DR   PDBsum; 1MCP; -.
DR   PDBsum; 2CJU; -.
DR   PDBsum; 2MCP; -.
DR   AlphaFoldDB; P01789; -.
DR   SMR; P01789; -.
DR   MINT; P01789; -.
DR   MaxQB; P01789; -.
DR   PRIDE; P01789; -.
DR   EvolutionaryTrace; P01789; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P01789; 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: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; 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; Reference proteome.
FT   CHAIN           1..>122
FT                   /note="Ig heavy chain V region M603"
FT                   /id="PRO_0000059875"
FT   DOMAIN          1..121
FT                   /note="Ig-like"
FT   SITE            33
FT                   /note="H-bond with the phosphate group of
FT                   phosphorylcholine"
FT   SITE            52
FT                   /note="H-bond with the phosphate group of
FT                   phosphorylcholine"
FT   NON_TER         122
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          18..27
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          34..39
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   TURN            76..79
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          94..102
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          109..112
FT                   /evidence="ECO:0007829|PDB:2CJU"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:2CJU"
SQ   SEQUENCE   122 AA;  13626 MW;  BA2C864438B64F0F CRC64;
     EVKLVESGGG LVQPGGSLRL SCATSGFTFS DFYMEWVRQP PGKRLEWIAA SRNKGNKYTT
     EYSASVKGRF IVSRDTSQSI LYLQMNALRA EDTAIYYCAR NYYGSTWYFD VWGAGTTVTV
     SS
 
 
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