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

 CD3Z_MOUSE              Reviewed;         164 AA.
P24161; P29020; Q9D3G3;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
27-SEP-2017, entry version 157.
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, Tcrz;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CD-3-ZETA), AND PARTIAL
PROTEIN SEQUENCE.
PubMed=3278377; DOI=10.1126/science.3278377;
Weissman A.M., Baniyash M., Hou D., Samelson L.E., Burgess W.H.,
Klausner R.D.;
"Molecular cloning of the zeta chain of the T cell antigen receptor.";
Science 239:1018-1021(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CD-3-ZETA).
TISSUE=Liver;
PubMed=2787796;
Baniyash M., Hsu V.W., Seldin M.F., Klausner R.D.;
"The isolation and characterization of the murine T cell antigen
receptor zeta chain gene.";
J. Biol. Chem. 264:13252-13257(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CD-3-ETA), PARTIAL PROTEIN
SEQUENCE, AND BLOCKAGE OF N-TERMINUS.
PubMed=2139725; DOI=10.1073/pnas.87.9.3319;
Jin Y.J., Clayton L.K., Howard F.D., Koyasu S., Sieh M.,
Steinbrich R., Tarr G.E., Reinherz E.L.;
"Molecular cloning of the CD3 eta subunit identifies a CD3 zeta-
related product in thymus-derived cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:3319-3323(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CD-3-ZETA).
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CD-3-ZETA).
STRAIN=C57BL/6J; TISSUE=Hematopoietic;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM CD-3-ETA), AND ALTERNATIVE
SPLICING.
PubMed=2150596; DOI=10.1093/intimm/2.11.1117;
Ohno H., Saito T.;
"CD3 zeta and eta chains are produced by alternative splicing from a
common gene.";
Int. Immunol. 2:1117-1119(1990).
[7]
ERRATUM.
Ohno H., Saito T.;
Int. Immunol. 4:1339-1339(1992).
[8]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CD-3-ETA).
PubMed=1828894; DOI=10.1073/pnas.88.12.5202;
Clayton L.K., D'Adamio L., Sieh M., Hussey R.E., Koyasu S.,
Reinherz E.L., Howard F.B.;
"CD3 eta and CD3 zeta are alternatively spliced products of a common
genetic locus and are transcriptionally and/or post-transcriptionally
regulated during T-cell development.";
Proc. Natl. Acad. Sci. U.S.A. 88:5202-5206(1991).
[9]
INTERACTION WITH SLA.
PubMed=10662792; DOI=10.1084/jem.191.3.463;
Sosinowski T., Pandey A., Dixit V.M., Weiss A.;
"Src-like adaptor protein (SLAP) is a negative regulator of T cell
receptor signaling.";
J. Exp. Med. 191:463-474(2000).
[10]
INTERACTION WITH SLA2.
PubMed=11891219; DOI=10.1074/jbc.M110318200;
Pandey A., Ibarrola N., Kratchmarova I., Fernandez M.M.,
Constantinescu S.N., Ohara O., Sawasdikosol S., Lodish H.F., Mann M.;
"A novel Src homology 2 domain-containing molecule, Src-like adapter
protein-2 (SLAP-2), which negatively regulates T cell receptor
signaling.";
J. Biol. Chem. 277:19131-19138(2002).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Probable role in assembly and expression of the TCR
complex as well as signal transduction upon antigen triggering.
-!- SUBUNIT: The TCR/CD3 complex of T-lymphocytes consists of either a
TCR alpha/beta or TCR gamma/delta heterodimer coexpressed at the
cell surface with the invariant subunits of CD3 labeled gamma,
delta, epsilon, zeta, and eta. CD3-zeta forms either homodimers or
heterodimers with CD3-eta (By similarity). Interacts with SLA
(PubMed:10662792). Interacts with SLA2 (PubMed:11891219).
Interacts with TRAT1. Interacts with DOCK2. Interacts with SHB.
Interacts with ZAP70. Interacts (tyrosine phosphorylated) with
SHC1 (via SH2 domain). Interacts with PTPRC (By similarity).
{ECO:0000250|UniProtKB:P20963, ECO:0000269|PubMed:10662792,
ECO:0000269|PubMed:11891219}.
-!- INTERACTION:
Q9WU22:Ptpn4; NbExp=3; IntAct=EBI-7803400, EBI-7249866;
P43404:Zap70; NbExp=4; IntAct=EBI-7803400, EBI-3862932;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=CD-3-zeta;
IsoId=P24161-1; Sequence=Displayed;
Name=CD-3-eta;
IsoId=P24161-2; Sequence=VSP_058346;
-!- DOMAIN: The ITAM domains mediate interaction with SHB.
{ECO:0000250}.
-!- PTM: Phosphorylated on Tyr residues after T-cell receptor
triggering.
-!- SIMILARITY: Belongs to the CD3Z/FCER1G family. {ECO:0000305}.
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EMBL; M19729; AAA40171.1; -; Genomic_DNA.
EMBL; J04967; AAA50301.1; -; mRNA.
EMBL; M33158; AAA37398.1; -; mRNA.
EMBL; AK017904; BAB30997.1; -; mRNA.
EMBL; BC052824; AAH52824.1; -; mRNA.
EMBL; M76711; AAA40403.1; -; Genomic_DNA.
CCDS; CCDS15443.1; -. [P24161-2]
CCDS; CCDS48427.1; -. [P24161-1]
PIR; A35900; A35900.
PIR; A40104; A40104.
RefSeq; NP_001106862.1; NM_001113391.2. [P24161-1]
RefSeq; NP_112439.1; NM_031162.4. [P24161-2]
RefSeq; XP_011237047.1; XM_011238745.2. [P24161-1]
RefSeq; XP_017168774.1; XM_017313285.1. [P24161-1]
UniGene; Mm.217308; -.
UniGene; Mm.245261; -.
UniGene; Mm.475205; -.
ProteinModelPortal; P24161; -.
SMR; P24161; -.
BioGrid; 198598; 5.
CORUM; P24161; -.
ELM; P24161; -.
IntAct; P24161; 7.
MINT; MINT-7895650; -.
STRING; 10090.ENSMUSP00000027849; -.
iPTMnet; P24161; -.
PhosphoSitePlus; P24161; -.
EPD; P24161; -.
PaxDb; P24161; -.
PRIDE; P24161; -.
DNASU; 12503; -.
Ensembl; ENSMUST00000005907; ENSMUSP00000005907; ENSMUSG00000005763. [P24161-1]
Ensembl; ENSMUST00000027849; ENSMUSP00000027849; ENSMUSG00000005763. [P24161-2]
Ensembl; ENSMUST00000086002; ENSMUSP00000083165; ENSMUSG00000005763. [P24161-2]
Ensembl; ENSMUST00000187313; ENSMUSP00000140926; ENSMUSG00000005763. [P24161-2]
GeneID; 12503; -.
KEGG; mmu:12503; -.
UCSC; uc007djn.2; mouse. [P24161-1]
CTD; 919; -.
MGI; MGI:88334; Cd247.
eggNOG; ENOG410J0ID; Eukaryota.
eggNOG; ENOG411241T; LUCA.
GeneTree; ENSGT00390000018208; -.
HOGENOM; HOG000234398; -.
HOVERGEN; HBG005280; -.
InParanoid; P29020; -.
KO; K06453; -.
OMA; LHMQTLP; -.
OrthoDB; EOG091G0QJC; -.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-MMU-202433; Generation of second messenger molecules.
Reactome; R-MMU-2029481; FCGR activation.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
Reactome; R-MMU-389948; PD-1 signaling.
ChiTaRS; Cd247; mouse.
PRO; PR:P24161; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000005763; -.
CleanEx; MM_CD247; -.
ExpressionAtlas; P24161; baseline and differential.
Genevisible; P24161; MM.
GO; GO:0042105; C:alpha-beta T cell receptor complex; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0042101; C:T cell receptor complex; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI.
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.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disulfide bond; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21
CHAIN 22 164 T-cell surface glycoprotein CD3 zeta
chain.
/FTId=PRO_0000016494.
TOPO_DOM 22 30 Extracellular. {ECO:0000255}.
TRANSMEM 31 51 Helical. {ECO:0000255}.
TOPO_DOM 52 164 Cytoplasmic. {ECO:0000255}.
DOMAIN 61 89 ITAM 1. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
DOMAIN 100 128 ITAM 2. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
DOMAIN 131 159 ITAM 3. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
MOD_RES 22 22 Blocked amino end (Gln).
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:P20963}.
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 111 111 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 123 123 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 142 142 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
MOD_RES 153 153 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20963,
ECO:0000255|PROSITE-ProRule:PRU00379}.
DISULFID 32 32 Interchain. {ECO:0000255}.
VAR_SEQ 144 164 GLSTATKDTYDALHMQTLAPR -> DSHFQAVQFGNRRERE
GSELTRTLGLRARPKGESTQQSSQSCASVFSIPTLWSPWPP
SSSSQL (in isoform CD-3-eta).
/FTId=VSP_058346.
CONFLICT 153 153 Y -> C (in Ref. 4; BAB30997).
{ECO:0000305}.
SEQUENCE 164 AA; 18637 MW; 1B8022035A312831 CRC64;
MKWKVSVLAC ILHVRFPGAE AQSFGLLDPK LCYLLDGILF IYGVIITALY LRAKFSRSAE
TAANLQDPNQ LYNELNLGRR EEYDVLEKKR ARDPEMGGKQ QRRRNPQEGV YNALQKDKMA
EAYSEIGTKG ERRRGKGHDG LYQGLSTATK DTYDALHMQT LAPR


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