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CD3D_MACFA
ID   CD3D_MACFA              Reviewed;         171 AA.
AC   Q95LI8;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=T-cell surface glycoprotein CD3 delta chain;
DE   AltName: Full=T-cell receptor T3 delta chain;
DE   AltName: CD_antigen=CD3d;
DE   Flags: Precursor;
GN   Name=CD3D;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11515669; DOI=10.1111/j.1600-0684.2001.tb00002.x;
RA   Uda A., Tanabayashi K., Mukai R., Yachi M., Nam K., Yamada A.;
RT   "CD3 polymorphism in cynomolgus monkeys (Macaca fascicularis).";
RL   J. Med. Primatol. 30:141-147(2001).
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, CD3D plays an essential role in
CC       thymocyte differentiation. Indeed, participates in correct
CC       intracellular TCR-CD3 complex assembly and surface expression. In
CC       absence of a functional TCR-CD3 complex, thymocytes are unable to
CC       differentiate properly. Interacts with CD4 and CD8 and thus serves to
CC       establish a functional link between the TCR and coreceptors CD4 and
CC       CD8, which is needed for activation and positive selection of CD4 or
CC       CD8 T-cells. {ECO:0000250|UniProtKB:P04234}.
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 coreceptors CD4 and CD8.
CC       {ECO:0000250|UniProtKB:P04234}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04234};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04234}.
CC   -!- TISSUE SPECIFICITY: CD3D is mostly present on T-lymphocytes with its
CC       TCR-CD3 partners. Present also in fetal NK-cells.
CC       {ECO:0000250|UniProtKB:P04234}.
CC   -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC       LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P04234}.
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DR   EMBL; AB073991; BAB71847.1; -; mRNA.
DR   RefSeq; NP_001274617.1; NM_001287688.1.
DR   AlphaFoldDB; Q95LI8; -.
DR   SMR; Q95LI8; -.
DR   STRING; 9541.XP_005579855.1; -.
DR   GeneID; 102133701; -.
DR   CTD; 915; -.
DR   VEuPathDB; HostDB:ENSMFAG00000045644; -.
DR   eggNOG; ENOG502S4XC; Eukaryota.
DR   OMA; YQPLRDH; -.
DR   Proteomes; UP000233100; Chromosome 14.
DR   GO; GO:0042105; C:alpha-beta T cell receptor complex; IEA:UniProt.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0045059; P:positive thymic T cell selection; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR015484; CD3_esu/gsu/dsu.
DR   InterPro; IPR015485; CD3D.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032052; Ig_4.
DR   InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR   PANTHER; PTHR10570; PTHR10570; 1.
DR   PANTHER; PTHR10570:SF5; PTHR10570:SF5; 1.
DR   Pfam; PF16680; Ig_4; 1.
DR   Pfam; PF02189; ITAM; 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   Membrane; Phosphoprotein; Receptor; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..171
FT                   /note="T-cell surface glycoprotein CD3 delta chain"
FT                   /id="PRO_0000016488"
FT   TOPO_DOM        22..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..171
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          138..166
FT                   /note="ITAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT   MOD_RES         149
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P04234,
FT                   ECO:0000255|PROSITE-ProRule:PRU00379"
FT   MOD_RES         160
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P04234,
FT                   ECO:0000255|PROSITE-ProRule:PRU00379"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..73
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   171 AA;  18960 MW;  9C48629081DDFF42 CRC64;
     MEHSTFLSGL VLATLLSQVS PFKIPVEELE DRVFVKCNTS VTWVEGTVGT LLTNNTRLDL
     GKRILDPRGI YRCNGTDIYK DKESAVQVHY RMCQNCVELD PATLAGIIVT DVIATLLLAL
     GVFCFAGHET GRLSGAADTQ ALLRNDQVYQ PLRDRDDAQY SRLGGNWARN K
 
 
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