CD3Z_PIG
ID CD3Z_PIG Reviewed; 163 AA.
AC Q9XSJ9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=T-cell surface glycoprotein CD3 zeta chain;
DE AltName: Full=T-cell receptor T3 zeta chain;
DE AltName: CD_antigen=CD247;
DE Flags: Precursor;
GN Name=CD247; Synonyms=CD3Z;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Minnesota miniature;
RA Jie H.-B., Yim D., Kim Y.B.;
RT "The molecular cloning of porcine CD3 zeta.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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. CD3Z ITAMs phosphorylation creates
CC multiple docking sites for the protein kinase ZAP70 leading to ZAP70
CC phosphorylation and its conversion into a catalytically active enzyme.
CC Plays an important role in intrathymic T-cell differentiation.
CC Additionally, participates in the activity-dependent synapse formation
CC of retinal ganglion cells (RGCs) in both the retina and dorsal lateral
CC geniculate nucleus (dLGN). {ECO:0000250|UniProtKB:P20963}.
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 SLA. Interacts with TRAT1.
CC Interacts with DOCK2. Interacts with SLA2. Interacts with SHB.
CC Interacts with ZAP70. Interacts (tyrosine phosphorylated) with SHC1
CC (via SH2 domain). Interacts with PTPRC. Interacts with CRK; this
CC interaction regulates CD3Z phosphorylation. Interacts (on T cell side)
CC with CD81, ICAM1 and CD9 at immunological synapses between antigen-
CC presenting cells and T cells. Interacts with CD160. Interacts with
CC LY6E. Interacts with LY6E (By similarity). The signaling subunit of
CC immunoglobulin gamma (IgG) Fc receptor complex. As a homodimer or a
CC heterodimer with FCER1G, associates with the ligand binding subunit
CC FCGR3A (via transmembrane domain); this interaction is a prerequisite
CC for Fc receptor complex expression on the cell surface.
CC {ECO:0000250|UniProtKB:P20963, ECO:0000250|UniProtKB:P24161}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P24161};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20963}.
CC -!- DOMAIN: The ITAM domains mediate interaction with SHB.
CC {ECO:0000250|UniProtKB:P20963}.
CC -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P20963}.
CC -!- SIMILARITY: Belongs to the CD3Z/FCER1G family. {ECO:0000305}.
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DR EMBL; AF153830; AAD34640.1; -; mRNA.
DR AlphaFoldDB; Q9XSJ9; -.
DR BMRB; Q9XSJ9; -.
DR SMR; Q9XSJ9; -.
DR InParanoid; Q9XSJ9; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0042105; C:alpha-beta T cell receptor complex; IBA:GO_Central.
DR GO; GO:0033001; C:Fc-gamma receptor III complex; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR021663; CD3_zeta/IgE_Fc_rcpt_gamma.
DR InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR InterPro; IPR024128; T-cell_CD3_zeta.
DR PANTHER; PTHR10035; PTHR10035; 1.
DR Pfam; PF02189; ITAM; 3.
DR Pfam; PF11628; TCR_zetazeta; 1.
DR SMART; SM00077; ITAM; 3.
DR PROSITE; PS51055; ITAM_1; 3.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Immunity; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..163
FT /note="T-cell surface glycoprotein CD3 zeta chain"
FT /id="PRO_0000016496"
FT TOPO_DOM 22..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 61..89
FT /note="ITAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT DOMAIN 99..127
FT /note="ITAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT DOMAIN 130..158
FT /note="ITAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT REGION 83..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20963"
FT MOD_RES 64
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 72
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 83
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 110
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 122
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 141
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 152
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT DISULFID 32
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 163 AA; 18568 MW; 34898620B67167C7 CRC64;
MKWKALFTAA ILQAQLPITE AQSFGLLDPK LCYLLDGILF IYGVILTALF LRVKFSRSAD
APAYQQGQNQ LYNELNLGRR EEYDVLDKRR GRDPEMGGKP RRKNPQEGLY NELQKDKMAE
AYSEIGMKGE RRRGKGHDGL YQGLSTATKD TYDALHMQAL PPR
