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CD3G_BOVIN
ID   CD3G_BOVIN              Reviewed;         173 AA.
AC   Q28074; Q3SZA7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=T-cell surface glycoprotein CD3 gamma chain;
DE   AltName: Full=T-cell receptor T3 gamma chain;
DE   AltName: CD_antigen=CD3g;
DE   Flags: Precursor;
GN   Name=CD3G;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-91.
RX   PubMed=1971793; DOI=10.1002/eji.1830200415;
RA   Clevers H., Machugh N.D., Bensaid A., Dunlap S., Baldwin C.L., Kaushal A.,
RA   Iams K., Howard C.J., Morrison W.I.;
RT   "Identification of a bovine surface antigen uniquely expressed on CD4-CD8-T
RT   cell receptor gamma/delta+ T lymphocytes.";
RL   Eur. J. Immunol. 20:809-817(1990).
CC   -!- FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell
CC       surface that plays an essential role in adaptive immune response. When
CC       antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-
CC       mediated signals are transmitted across the cell membrane by the CD3
CC       chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor
CC       tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain.
CC       Upon TCR engagement, these motifs become phosphorylated by Src family
CC       protein tyrosine kinases LCK and FYN, resulting in the activation of
CC       downstream signaling pathways. In addition to this role of signal
CC       transduction in T-cell activation, CD3G plays an essential role in the
CC       dynamic regulation of TCR expression at the cell surface. Indeed,
CC       constitutive TCR cycling is dependent on the di-leucine-based (diL)
CC       receptor-sorting motif present in CD3G. {ECO:0000250|UniProtKB:P09693}.
CC   -!- SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a CD3G/CD3E
CC       heterodimers that preferentially associate with TCRalpha and TCRbeta,
CC       respectively, to form TCRalpha/CD3E/CD3G and TCRbeta/CD3G/CD3E trimers.
CC       In turn, the hexamer interacts with CD3Z homodimer to form the TCR-CD3
CC       complex. Alternatively, TCRalpha and TCRbeta can be replaced by
CC       TCRgamma and TCRdelta. {ECO:0000250|UniProtKB:P09693}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P09693};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09693}.
CC   -!- DOMAIN: A di-leucine motif and a tyrosine-based motif are individually
CC       sufficient to induce both endocytosis and delivery to lysosomes.
CC       {ECO:0000250|UniProtKB:P09693}.
CC   -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC       LCK in association with CD4/CD8. Phosphorylated also by PKC; leading to
CC       the TCR complex down-regulation. {ECO:0000250|UniProtKB:P09693}.
CC   -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC       LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P04234}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA37366.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC103010; AAI03011.1; -; mRNA.
DR   EMBL; X53268; CAA37366.1; ALT_INIT; mRNA.
DR   PIR; A60232; A60232.
DR   AlphaFoldDB; Q28074; -.
DR   SMR; Q28074; -.
DR   STRING; 9913.ENSBTAP00000044200; -.
DR   PaxDb; Q28074; -.
DR   PRIDE; Q28074; -.
DR   eggNOG; ENOG502S4XC; Eukaryota.
DR   HOGENOM; CLU_115449_0_0_1; -.
DR   InParanoid; Q28074; -.
DR   OrthoDB; 1466902at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0042105; C:alpha-beta T cell receptor complex; IBA:GO_Central.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0045059; P:positive thymic T cell selection; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR015484; CD3_esu/gsu/dsu.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032052; Ig_4.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR   PANTHER; PTHR10570; PTHR10570; 1.
DR   Pfam; PF16680; Ig_4; 1.
DR   Pfam; PF02189; ITAM; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00077; ITAM; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS51055; ITAM_1; 1.
PE   2: Evidence at transcript level;
KW   Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..173
FT                   /note="T-cell surface glycoprotein CD3 gamma chain"
FT                   /id="PRO_0000014614"
FT   TOPO_DOM        23..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..173
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          24..94
FT                   /note="Ig-like"
FT   DOMAIN          145..173
FT                   /note="ITAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT   MOTIF           149..150
FT                   /note="Di-leucine motif"
FT                   /evidence="ECO:0000250|UniProtKB:P09693"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09693"
FT   MOD_RES         144
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:P09693"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..83
FT                   /evidence="ECO:0000250|UniProtKB:P09693"
SQ   SEQUENCE   173 AA;  19463 MW;  74ADF52B384AA06C CRC64;
     MEQGKHLAGL ILAVFLLQGT MAHVKEVKVD DNREDGSVIL ICVTNDTTIT WLKDVEQIGS
     GDTKKNTWNL GSSTKDPRGI YKCEGSNNQS KSLQIYYRMC QNCIELNPST VAGFIFTEIV
     SIFLLAVGVY FIAGQEGVRQ SRASDKQTLL NNDQLYQPLK EREDDQYSHL RKN
 
 
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