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CD3E_BOVIN
ID   CD3E_BOVIN              Reviewed;         192 AA.
AC   Q28073; Q3ZCH2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=T-cell surface glycoprotein CD3 epsilon chain;
DE   AltName: CD_antigen=CD3e;
DE   Flags: Precursor;
GN   Name=CD3E;
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 1-52.
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 of this role of signal
CC       transduction in T-cell activation, CD3E plays an essential role in
CC       correct T-cell development. Initiates the TCR-CD3 complex assembly by
CC       forming the two heterodimers CD3D/CD3E and CD3G/CD3E. Participates also
CC       in internalization and cell surface down-regulation of TCR-CD3
CC       complexes via endocytosis sequences present in CD3E cytosolic region.
CC       {ECO:0000250|UniProtKB:P07766}.
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. Interacts with CD6. Interacts with NCK1.
CC       Interacts with NUMB; this interaction is important for TCR-CD3
CC       internalization and subsequent degradation.
CC       {ECO:0000250|UniProtKB:P07766}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P07766};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07766}.
CC   -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC       LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P07766}.
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DR   EMBL; BC102243; AAI02244.1; -; mRNA.
DR   EMBL; X53270; CAA37368.1; -; mRNA.
DR   PIR; C60232; C60232.
DR   RefSeq; NP_776436.1; NM_174011.3.
DR   AlphaFoldDB; Q28073; -.
DR   SMR; Q28073; -.
DR   STRING; 9913.ENSBTAP00000020859; -.
DR   PaxDb; Q28073; -.
DR   PeptideAtlas; Q28073; -.
DR   PRIDE; Q28073; -.
DR   Ensembl; ENSBTAT00000020859; ENSBTAP00000020859; ENSBTAG00000015710.
DR   Ensembl; ENSBTAT00000067918; ENSBTAP00000063144; ENSBTAG00000015710.
DR   GeneID; 281054; -.
DR   KEGG; bta:281054; -.
DR   CTD; 916; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015710; -.
DR   VGNC; VGNC:27029; CD3E.
DR   eggNOG; ENOG502S8KB; Eukaryota.
DR   GeneTree; ENSGT00940000153312; -.
DR   HOGENOM; CLU_117945_0_0_1; -.
DR   InParanoid; Q28073; -.
DR   OMA; RVCENCV; -.
DR   OrthoDB; 1362562at2759; -.
DR   TreeFam; TF335892; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000015710; Expressed in thymus and 103 other tissues.
DR   ExpressionAtlas; Q28073; baseline and differential.
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; IPR003598; Ig_sub2.
DR   InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR   PANTHER; PTHR10570; PTHR10570; 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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..192
FT                   /note="T-cell surface glycoprotein CD3 epsilon chain"
FT                   /id="PRO_0000014604"
FT   TOPO_DOM        23..114
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..97
FT                   /note="Ig-like"
FT   DOMAIN          163..190
FT                   /note="ITAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT   REGION          145..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..177
FT                   /note="NUMB-binding region"
FT                   /evidence="ECO:0000250|UniProtKB:P07766"
FT   MOD_RES         173
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P07766,
FT                   ECO:0000255|PROSITE-ProRule:PRU00379"
FT   MOD_RES         184
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P07766,
FT                   ECO:0000255|PROSITE-ProRule:PRU00379"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..84
FT                   /evidence="ECO:0000250|UniProtKB:P22646"
SQ   SEQUENCE   192 AA;  21523 MW;  8936173F23FC60FF CRC64;
     MQSGNLWRAL GLCLLLVGAW AQDADEQKPY EVSISGNTVE LTCPREFEGE IHWKQNDEQM
     KGYTGKQLLL ENFSEMDNSG YYQCYMTEGN KEAAHTLYLK ARVCQNCMEV NLMEVATIIV
     VDICVTLGLL LLVYYWSKSR KAKASPMTRG AGAGGRPRGQ NKGRPPPVPN PDYEPIRKGQ
     RDLYAGLNQR GV
 
 
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