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P24161

- CD3Z_MOUSE

UniProt

P24161 - CD3Z_MOUSE

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Protein
T-cell surface glycoprotein CD3 zeta chain
Gene
Cd247, Cd3z, Tcrz
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probable role in assembly and expression of the TCR complex as well as signal transduction upon antigen triggering.

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. transmembrane signaling receptor activity Source: InterPro

GO - Biological processi

  1. T cell receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiREACT_196487. FCGR activation.
REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_202937. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_215414. Translocation of ZAP-70 to Immunological synapse.
REACT_216080. Phosphorylation of CD3 and TCR zeta chains.
REACT_225145. Downstream TCR signaling.
REACT_225768. Generation of second messenger molecules.

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell surface glycoprotein CD3 zeta chain
Alternative name(s):
T-cell receptor T3 zeta chain
CD_antigen: CD247
Gene namesi
Name:Cd247
Synonyms:Cd3z, Tcrz
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:88334. Cd247.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 309Extracellular Reviewed prediction
Transmembranei31 – 5121Helical; Reviewed prediction
Add
BLAST
Topological domaini52 – 164113Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. alpha-beta T cell receptor complex Source: MGI
  2. cytoplasm Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121
Add
BLAST
Chaini22 – 164143T-cell surface glycoprotein CD3 zeta chain
PRO_0000016494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Blocked amino end (Gln)
Disulfide bondi32 – 32Interchain Reviewed prediction
Modified residuei58 – 581Phosphoserine By similarity
Modified residuei72 – 721Phosphotyrosine By similarity
Modified residuei83 – 831Phosphotyrosine By similarity
Modified residuei111 – 1111Phosphotyrosine By similarity
Modified residuei123 – 1231Phosphotyrosine By similarity
Modified residuei142 – 1421Phosphotyrosine By similarity
Modified residuei153 – 1531Phosphotyrosine By similarity

Post-translational modificationi

Phosphorylated on Tyr residues after T-cell receptor triggering.

Keywords - PTMi

Disulfide bond, Phosphoprotein

PTM databases

PhosphoSiteiP24161.

Expressioni

Gene expression databases

ArrayExpressiP24161.
BgeeiP24161.
CleanExiMM_CD247.
GenevestigatoriP24161.

Interactioni

Subunit structurei

Interacts with DOCK2 and TRAT1. Interacts with SHB. Interacts with ZAP70. Interacts (tyrosine phosphorylated) with SHC1 (via SH2 domain). Interacts with PTPRC By similarity. 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. Interacts with SLA and SLA2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ptpn4Q9WU223EBI-7803400,EBI-7249866

Protein-protein interaction databases

BioGridi198598. 5 interactions.
IntActiP24161. 5 interactions.
MINTiMINT-7895650.

Structurei

3D structure databases

ProteinModelPortaliP24161.
SMRiP24161. Positions 28-60.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 8929ITAM 1
Add
BLAST
Domaini100 – 12829ITAM 2
Add
BLAST
Domaini131 – 15929ITAM 3
Add
BLAST

Domaini

The ITAM domains mediate interaction with SHB By similarity.

Sequence similaritiesi

Belongs to the CD3Z/FCER1G family.
Contains 3 ITAM domains.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000018208.
HOGENOMiHOG000234398.
HOVERGENiHBG005280.
KOiK06453.
OMAiLHMQTLP.

Family and domain databases

InterProiIPR021663. CR3_zeta/IgE_Fc_rcpt_gamma.
IPR003110. Phos_immunorcpt_sig_ITAM.
IPR024128. T-cell_CD3_zeta/eta.
[Graphical view]
PANTHERiPTHR10035. PTHR10035. 1 hit.
PfamiPF02189. ITAM. 3 hits.
PF11628. TCR_zetazeta. 1 hit.
[Graphical view]
SMARTiSM00077. ITAM. 3 hits.
[Graphical view]
PROSITEiPS51055. ITAM_1. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform CD-3-zeta (identifier: P24161-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MKWKVSVLAC ILHVRFPGAE AQSFGLLDPK LCYLLDGILF IYGVIITALY    50
LRAKFSRSAE TAANLQDPNQ LYNELNLGRR EEYDVLEKKR ARDPEMGGKQ 100
QRRRNPQEGV YNALQKDKMA EAYSEIGTKG ERRRGKGHDG LYQGLSTATK 150
DTYDALHMQT LAPR 164
Length:164
Mass (Da):18,637
Last modified:March 1, 1992 - v1
Checksum:i1B8022035A312831
GO
Isoform CD-3-eta (identifier: P29020-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry P29020.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:206
Mass (Da):23,339
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531Y → C in BAB30997. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19729 Genomic DNA. Translation: AAA40171.1.
J04967 mRNA. Translation: AAA50301.1.
AK017904 mRNA. Translation: BAB30997.1.
BC052824 mRNA. Translation: AAH52824.1.
CCDSiCCDS48427.1. [P24161-1]
PIRiA40104.
RefSeqiNP_001106862.1. NM_001113391.2. [P24161-1]
XP_006496696.1. XM_006496633.1. [P24161-1]
UniGeneiMm.217308.
Mm.245261.
Mm.475205.

Genome annotation databases

EnsembliENSMUST00000005907; ENSMUSP00000005907; ENSMUSG00000005763. [P24161-1]
GeneIDi12503.
KEGGimmu:12503.
UCSCiuc007djn.2. mouse. [P24161-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19729 Genomic DNA. Translation: AAA40171.1 .
J04967 mRNA. Translation: AAA50301.1 .
AK017904 mRNA. Translation: BAB30997.1 .
BC052824 mRNA. Translation: AAH52824.1 .
CCDSi CCDS48427.1. [P24161-1 ]
PIRi A40104.
RefSeqi NP_001106862.1. NM_001113391.2. [P24161-1 ]
XP_006496696.1. XM_006496633.1. [P24161-1 ]
UniGenei Mm.217308.
Mm.245261.
Mm.475205.

3D structure databases

ProteinModelPortali P24161.
SMRi P24161. Positions 28-60.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198598. 5 interactions.
IntActi P24161. 5 interactions.
MINTi MINT-7895650.

PTM databases

PhosphoSitei P24161.

Protocols and materials databases

DNASUi 12503.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005907 ; ENSMUSP00000005907 ; ENSMUSG00000005763 . [P24161-1 ]
GeneIDi 12503.
KEGGi mmu:12503.
UCSCi uc007djn.2. mouse. [P24161-1 ]

Organism-specific databases

CTDi 919.
MGIi MGI:88334. Cd247.

Phylogenomic databases

GeneTreei ENSGT00390000018208.
HOGENOMi HOG000234398.
HOVERGENi HBG005280.
KOi K06453.
OMAi LHMQTLP.

Enzyme and pathway databases

Reactomei REACT_196487. FCGR activation.
REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_202937. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_210240. Role of phospholipids in phagocytosis.
REACT_215414. Translocation of ZAP-70 to Immunological synapse.
REACT_216080. Phosphorylation of CD3 and TCR zeta chains.
REACT_225145. Downstream TCR signaling.
REACT_225768. Generation of second messenger molecules.

Miscellaneous databases

ChiTaRSi CD247. mouse.
NextBioi 281458.
PROi P24161.
SOURCEi Search...

Gene expression databases

ArrayExpressi P24161.
Bgeei P24161.
CleanExi MM_CD247.
Genevestigatori P24161.

Family and domain databases

InterProi IPR021663. CR3_zeta/IgE_Fc_rcpt_gamma.
IPR003110. Phos_immunorcpt_sig_ITAM.
IPR024128. T-cell_CD3_zeta/eta.
[Graphical view ]
PANTHERi PTHR10035. PTHR10035. 1 hit.
Pfami PF02189. ITAM. 3 hits.
PF11628. TCR_zetazeta. 1 hit.
[Graphical view ]
SMARTi SM00077. ITAM. 3 hits.
[Graphical view ]
PROSITEi PS51055. ITAM_1. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the zeta chain of the T cell antigen receptor."
    Weissman A.M., Baniyash M., Hou D., Samelson L.E., Burgess W.H., Klausner R.D.
    Science 239:1018-1021(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "The isolation and characterization of the murine T cell antigen receptor zeta chain gene."
    Baniyash M., Hsu V.W., Seldin M.F., Klausner R.D.
    J. Biol. Chem. 264:13252-13257(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Thymus.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Hematopoietic.
  5. "Molecular cloning of the CD3 eta subunit identifies a CD3 zeta-related product in thymus-derived cells."
    Jin Y.J., Clayton L.K., Howard F.D., Koyasu S., Sieh M., Steinbrich R., Tarr G.E., Reinherz E.L.
    Proc. Natl. Acad. Sci. U.S.A. 87:3319-3323(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, BLOCKAGE OF N-TERMINUS.
  6. "CD3 zeta and eta chains are produced by alternative splicing from a common gene."
    Ohno H., Saito T.
    Int. Immunol. 2:1117-1119(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  7. Erratum
    Ohno H., Saito T.
    Int. Immunol. 4:1339-1339(1992)
  8. "Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor signaling."
    Sosinowski T., Pandey A., Dixit V.M., Weiss A.
    J. Exp. Med. 191:463-474(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLA.
  9. "A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signaling."
    Pandey A., Ibarrola N., Kratchmarova I., Fernandez M.M., Constantinescu S.N., Ohara O., Sawasdikosol S., Lodish H.F., Mann M.
    J. Biol. Chem. 277:19131-19138(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLA2.

Entry informationi

Entry nameiCD3Z_MOUSE
AccessioniPrimary (citable) accession number: P24161
Secondary accession number(s): Q9D3G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: September 3, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi