CD3D_RAT
ID CD3D_RAT Reviewed; 173 AA.
AC P19377;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 140.
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; Synonyms=T3d;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=2143819; DOI=10.1093/nar/18.15.4617;
RA Davies J.D., Mueller D., Wilson D.B., Gold D.P.;
RT "Nucleotide sequence of a cDNA encoding the rat T3 delta chain.";
RL Nucleic Acids Res. 18:4617-4617(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, 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; X53430; CAA37521.1; -; mRNA.
DR PIR; S10975; S10975.
DR RefSeq; NP_037301.1; NM_013169.1.
DR AlphaFoldDB; P19377; -.
DR SMR; P19377; -.
DR ELM; P19377; -.
DR IntAct; P19377; 1.
DR STRING; 10116.ENSRNOP00000021489; -.
DR GlyGen; P19377; 3 sites.
DR PaxDb; P19377; -.
DR GeneID; 25710; -.
DR KEGG; rno:25710; -.
DR UCSC; RGD:2304; rat.
DR CTD; 915; -.
DR RGD; 2304; Cd3d.
DR VEuPathDB; HostDB:ENSRNOG00000015994; -.
DR eggNOG; ENOG502S4XC; Eukaryota.
DR HOGENOM; CLU_115449_0_0_1; -.
DR InParanoid; P19377; -.
DR OMA; YQPLRDH; -.
DR OrthoDB; 1466902at2759; -.
DR PhylomeDB; P19377; -.
DR TreeFam; TF335892; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-202424; Downstream TCR signaling.
DR Reactome; R-RNO-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-RNO-202430; Translocation of ZAP-70 to Immunological synapse.
DR Reactome; R-RNO-202433; Generation of second messenger molecules.
DR Reactome; R-RNO-389948; PD-1 signaling.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P19377; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000015994; Expressed in thymus and 16 other tissues.
DR Genevisible; P19377; RN.
DR GO; GO:0042105; C:alpha-beta T cell receptor complex; ISO:RGD.
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:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042101; C:T cell receptor complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; 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 CHAIN 22..173
FT /note="T-cell surface glycoprotein CD3 delta chain"
FT /id="PRO_0000016491"
FT TOPO_DOM 22..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..173
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 55
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 173 AA; 19356 MW; C462DFF34E7FDB60 CRC64;
MEHYGILVSL LLATVLPQGS PFKIEVVEYE DKVFVNCNTS IRHLDGSVER WLTKNKSLIL
GKGILDPRGM YMCNGTEELA KEVSTVQVYY RMCQNCVELD SATLAGVIIT DLIATLLLAL
GVYCFAGHET GRLSGAVDTQ VLLKNEQLYQ PLRDRDDAQY SRLGGNWPRN KRS
