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T-cell surface glycoprotein CD3 zeta chain (T-cell receptor T3 zeta chain) (CD antigen CD247)

 CD3Z_PIG                Reviewed;         163 AA.
Q9XSJ9;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 84.
RecName: Full=T-cell surface glycoprotein CD3 zeta chain;
AltName: Full=T-cell receptor T3 zeta chain;
AltName: CD_antigen=CD247;
Flags: Precursor;
Name=CD247; Synonyms=CD3Z;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Minnesota miniature;
Jie H.-B., Yim D., Kim Y.B.;
"The molecular cloning of porcine CD3 zeta.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell
surface that plays an essential role in adaptive immune response.
When antigen presenting cells (APCs) activate T-cell receptor
(TCR), TCR-mediated signals are transmitted across the cell
membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3
chains contain immunoreceptor tyrosine-based activation motifs
(ITAMs) in their cytoplasmic domain. Upon TCR engagement, these
motifs become phosphorylated by Src family protein tyrosine
kinases LCK and FYN, resulting in the activation of downstream
signaling pathways. CD3Z ITAMs phosphorylation creates multiple
docking sites for the protein kinase ZAP70 leading to ZAP70
phosphorylation and its conversion into a catalytically active
enzyme. Plays an important role in intrathymic T-cell
differentiation. Additionally, participates in the activity-
dependent synapse formation of retinal ganglion cells (RGCs) in
both the retina and dorsal lateral geniculate nucleus (dLGN).
{ECO:0000250|UniProtKB:P20963}.
-!- SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a
CD3G/CD3E heterodimers that preferentially associate with TCRalpha
and TCRbeta, respectively, to form TCRalpha/CD3E/CD3G and
TCRbeta/CD3G/CD3E trimers. In turn, the hexamer interacts with
CD3Z homodimer to form the TCR-CD3 complex. Alternatively,
TCRalpha and TCRbeta can be replaced by TCRgamma and TCRdelta.
Interacts with SLA. Interacts with TRAT1. Interacts with DOCK2.
Interacts with SLA2. Interacts with SHB. Interacts with ZAP70.
Interacts (tyrosine phosphorylated) with SHC1 (via SH2 domain).
Interacts with PTPRC. Interacts with CRK; this interaction
regulates CD3Z phosphorylation. {ECO:0000250|UniProtKB:P20963}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P20963};
Single-pass type I membrane protein
{ECO:0000250|UniProtKB:P20963}.
-!- DOMAIN: The ITAM domains mediate interaction with SHB.
{ECO:0000250|UniProtKB:P20963}.
-!- PTM: Phosphorylated on Tyr residues after T-cell receptor
triggering by LCK in association with CD4/CD8.
{ECO:0000250|UniProtKB:P20963}.
-!- SIMILARITY: Belongs to the CD3Z/FCER1G family. {ECO:0000305}.
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EMBL; AF153830; AAD34640.1; -; mRNA.
UniGene; Ssc.50307; -.
ProteinModelPortal; Q9XSJ9; -.
SMR; Q9XSJ9; -.
PRIDE; Q9XSJ9; -.
HOVERGEN; HBG005280; -.
InParanoid; Q9XSJ9; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
InterPro; IPR021663; CD3_zeta/IgE_Fc_rcpt_gamma.
InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
InterPro; IPR024128; T-cell_CD3_zeta.
PANTHER; PTHR10035; PTHR10035; 1.
Pfam; PF02189; ITAM; 3.
Pfam; PF11628; TCR_zetazeta; 1.
SMART; SM00077; ITAM; 3.
PROSITE; PS51055; ITAM_1; 3.
2: Evidence at transcript level;
Adaptive immunity; Complete proteome; Disulfide bond; Immunity;
Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000250}.
CHAIN 22 163 T-cell surface glycoprotein CD3 zeta
chain.
/FTId=PRO_0000016496.
TOPO_DOM 22 30 Extracellular. {ECO:0000255}.
TRANSMEM 31 51 Helical. {ECO:0000255}.
TOPO_DOM 52 163 Cytoplasmic. {ECO:0000255}.
DOMAIN 61 89 ITAM 1. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
DOMAIN 99 127 ITAM 2. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
DOMAIN 130 158 ITAM 3. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:P20963}.
MOD_RES 64 64 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 72 72 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 83 83 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 110 110 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 122 122 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 141 141 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 152 152 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
DISULFID 32 32 Interchain. {ECO:0000255}.
SEQUENCE 163 AA; 18568 MW; 34898620B67167C7 CRC64;
MKWKALFTAA ILQAQLPITE AQSFGLLDPK LCYLLDGILF IYGVILTALF LRVKFSRSAD
APAYQQGQNQ LYNELNLGRR EEYDVLDKRR GRDPEMGGKP RRKNPQEGLY NELQKDKMAE
AYSEIGMKGE RRRGKGHDGL YQGLSTATKD TYDALHMQAL PPR


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