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TCB2_MOUSE
ID   TCB2_MOUSE              Reviewed;         173 AA.
AC   P01851;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=T-cell receptor beta-2 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].
RC   STRAIN=B10.A;
RX   PubMed=6336329; DOI=10.1038/310387a0;
RA   Gascoigne N.R.J., Chien Y., Becker D.M., Kavaler J., Davis M.M.;
RT   "Genomic organization and sequence of T-cell receptor beta-chain
RT   constant- and joining-region genes.";
RL   Nature 310:387-391(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (CLONE 2C).
RC   STRAIN=BALB.B;
RX   PubMed=6330561; DOI=10.1038/309757a0;
RA   Saito H., Kranz D.M., Takagaki Y., Hayday A.C., Eisen H.N., Tonegawa S.;
RT   "Complete primary structure of a heterodimeric T-cell receptor deduced from
RT   cDNA sequences.";
RL   Nature 309:757-762(1984).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-124.
RX   PubMed=12015151; DOI=10.1016/s0969-2126(02)00759-1;
RA   Sundberg E.J., Li H., Llera A.S., McCormick J.K., Tormo J.,
RA   Schlievert P.M., Karjalainen K., Mariuzza R.A.;
RT   "Structures of two streptococcal superantigens bound to TCR beta chains
RT   reveal diversity in the architecture of T cell signaling complexes.";
RL   Structure 10:687-699(2002).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Clone B10.A was isolated from a cytotoxic T lymphocyte.
CC   -!- MISCELLANEOUS: Clone 2C was isolated from a cytotoxic T lymphocyte.
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DR   PDB; 1L0X; X-ray; 2.80 A; A/C=1-126.
DR   PDB; 1L0Y; X-ray; 2.50 A; A/C=1-124.
DR   PDB; 1MWA; X-ray; 2.40 A; B/D=1-127.
DR   PDB; 2Q86; X-ray; 1.85 A; B/D=1-141.
DR   PDB; 5M01; X-ray; 1.95 A; H=1-127.
DR   PDB; 5M02; X-ray; 1.75 A; H=1-127.
DR   PDBsum; 1L0X; -.
DR   PDBsum; 1L0Y; -.
DR   PDBsum; 1MWA; -.
DR   PDBsum; 2Q86; -.
DR   PDBsum; 5M01; -.
DR   PDBsum; 5M02; -.
DR   AlphaFoldDB; P01851; -.
DR   SMR; P01851; -.
DR   IntAct; P01851; 1.
DR   MINT; P01851; -.
DR   GlyGen; P01851; 2 sites.
DR   PhosphoSitePlus; P01851; -.
DR   MaxQB; P01851; -.
DR   PRIDE; P01851; -.
DR   EvolutionaryTrace; P01851; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P01851; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..173
FT                   /note="T-cell receptor beta-2 chain C region"
FT                   /id="PRO_0000184528"
FT   TRANSMEM        147..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..173
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..146
FT                   /note="C region"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         50
FT                   /note="K -> R (in clone 2C)"
FT   VARIANT         70
FT                   /note="Y -> H (in clone 2C)"
FT   NON_TER         1
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   STRAND          10..15
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   HELIX           18..24
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   STRAND          25..38
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   STRAND          41..47
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   STRAND          69..79
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   STRAND          89..96
FT                   /evidence="ECO:0007829|PDB:5M02"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:1L0X"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:2Q86"
FT   STRAND          113..122
FT                   /evidence="ECO:0007829|PDB:5M02"
SQ   SEQUENCE   173 AA;  19297 MW;  A5458149614CF295 CRC64;
     EDLRNVTPPK VSLFEPSKAE IANKQKATLV CLARGFFPDH VELSWWVNGK EVHSGVSTDP
     QAYKESNYSY CLSSRLRVSA TFWHNPRNHF RCQVQFHGLS EEDKWPEGSP KPVTQNISAE
     AWGRADCGIT SASYHQGVLS ATILYEILLG KATLYAVLVS GLVLMAMVKK KNS
 
 
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