CD3D_SHEEP
ID CD3D_SHEEP Reviewed; 167 AA.
AC P18438;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphocyte;
RX PubMed=2143727; DOI=10.1002/eji.1830200715;
RA Hein W.R., Tunnacliffe A.;
RT "Characterization of the CD3 gamma and delta invariant subunits of the
RT sheep T cell antigen receptor.";
RL Eur. J. Immunol. 20:1505-1511(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; X52993; CAA37182.1; -; mRNA.
DR PIR; B43547; RWSHD3.
DR RefSeq; NP_001009382.1; NM_001009382.1.
DR PDB; 1XMW; NMR; -; A=22-88.
DR PDBsum; 1XMW; -.
DR AlphaFoldDB; P18438; -.
DR SMR; P18438; -.
DR STRING; 9940.ENSOARP00000009839; -.
DR GeneID; 443397; -.
DR KEGG; oas:443397; -.
DR CTD; 915; -.
DR eggNOG; ENOG502S4XC; Eukaryota.
DR OrthoDB; 1466902at2759; -.
DR EvolutionaryTrace; P18438; -.
DR Proteomes; UP000002356; Unplaced.
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 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..167
FT /note="T-cell surface glycoprotein CD3 delta chain"
FT /id="PRO_0000016492"
FT TOPO_DOM 22..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 134..162
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 145
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04234,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 156
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 DISULFID 37..73
FT /evidence="ECO:0000250"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:1XMW"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1XMW"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1XMW"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1XMW"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:1XMW"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1XMW"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1XMW"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1XMW"
SQ SEQUENCE 167 AA; 18562 MW; 35D55493AE369714 CRC64;
MEHSRCLSCL ILAALLSQVN PRALEVLEAE DKVILKCNSS ITLLQGTAGQ EVSDNKTLNL
GKRIEDPRGM YQCGENAKSF TLQVYYRMCQ NCVELDSATL AGLIITDIIA TVLLALGVYC
FAGHETGRFS RAADTQVLMG NDQLYQPLRE RNDAQYSRLG DKWARNK
