CD3Z_MOUSE
ID CD3Z_MOUSE Reviewed; 164 AA.
AC P24161; P29020; Q9D3G3;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 186.
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, Tcrz;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CD-3-ZETA), AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=3278377; DOI=10.1126/science.3278377;
RA Weissman A.M., Baniyash M., Hou D., Samelson L.E., Burgess W.H.,
RA Klausner R.D.;
RT "Molecular cloning of the zeta chain of the T cell antigen receptor.";
RL Science 239:1018-1021(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CD-3-ZETA).
RC TISSUE=Liver;
RX PubMed=2787796; DOI=10.1016/s0021-9258(18)51622-7;
RA Baniyash M., Hsu V.W., Seldin M.F., Klausner R.D.;
RT "The isolation and characterization of the murine T cell antigen receptor
RT zeta chain gene.";
RL J. Biol. Chem. 264:13252-13257(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CD-3-ETA), PARTIAL PROTEIN SEQUENCE,
RP AND BLOCKAGE OF N-TERMINUS.
RX PubMed=2139725; DOI=10.1073/pnas.87.9.3319;
RA Jin Y.J., Clayton L.K., Howard F.D., Koyasu S., Sieh M., Steinbrich R.,
RA Tarr G.E., Reinherz E.L.;
RT "Molecular cloning of the CD3 eta subunit identifies a CD3 zeta-related
RT product in thymus-derived cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3319-3323(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CD-3-ZETA).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CD-3-ZETA).
RC STRAIN=C57BL/6J; TISSUE=Hematopoietic;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM CD-3-ETA), AND ALTERNATIVE SPLICING.
RX PubMed=2150596; DOI=10.1093/intimm/2.11.1117;
RA Ohno H., Saito T.;
RT "CD3 zeta and eta chains are produced by alternative splicing from a common
RT gene.";
RL Int. Immunol. 2:1117-1119(1990).
RN [7]
RP ERRATUM OF PUBMED:2150596.
RA Ohno H., Saito T.;
RL Int. Immunol. 4:1339-1339(1992).
RN [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CD-3-ETA).
RX PubMed=1828894; DOI=10.1073/pnas.88.12.5202;
RA Clayton L.K., D'Adamio L., Sieh M., Hussey R.E., Koyasu S., Reinherz E.L.,
RA Howard F.B.;
RT "CD3 eta and CD3 zeta are alternatively spliced products of a common
RT genetic locus and are transcriptionally and/or post-transcriptionally
RT regulated during T-cell development.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5202-5206(1991).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=8223495; DOI=10.1002/j.1460-2075.1993.tb06176.x;
RA Liu C.P., Ueda R., She J., Sancho J., Wang B., Weddell G., Loring J.,
RA Kurahara C., Dudley E.C., Hayday A.;
RT "Abnormal T cell development in CD3-zeta-/- mutant mice and identification
RT of a novel T cell population in the intestine.";
RL EMBO J. 12:4863-4875(1993).
RN [10]
RP INTERACTION WITH LY6E, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=9575182; DOI=10.1074/jbc.273.20.12301;
RA Kosugi A., Saitoh S., Noda S., Miyake K., Yamashita Y., Kimoto M.,
RA Ogata M., Hamaoka T.;
RT "Physical and functional association between thymic shared antigen-1/stem
RT cell antigen-2 and the T cell receptor complex.";
RL J. Biol. Chem. 273:12301-12306(1998).
RN [11]
RP INTERACTION WITH SLA.
RX PubMed=10662792; DOI=10.1084/jem.191.3.463;
RA Sosinowski T., Pandey A., Dixit V.M., Weiss A.;
RT "Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor
RT signaling.";
RL J. Exp. Med. 191:463-474(2000).
RN [12]
RP INTERACTION WITH SLA2.
RX PubMed=11891219; DOI=10.1074/jbc.m110318200;
RA Pandey A., Ibarrola N., Kratchmarova I., Fernandez M.M.,
RA Constantinescu S.N., Ohara O., Sawasdikosol S., Lodish H.F., Mann M.;
RT "A novel Src homology 2 domain-containing molecule, Src-like adapter
RT protein-2 (SLAP-2), which negatively regulates T cell receptor signaling.";
RL J. Biol. Chem. 277:19131-19138(2002).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=20188655; DOI=10.1016/j.neuron.2010.01.035;
RA Xu H.P., Chen H., Ding Q., Xie Z.H., Chen L., Diao L., Wang P., Gan L.,
RA Crair M.C., Tian N.;
RT "The immune protein CD3zeta is required for normal development of neural
RT circuits in the retina.";
RL Neuron 65:503-515(2010).
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 ECO:0000269|PubMed:20188655, ECO:0000269|PubMed:8223495}.
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 (PubMed:10662792). Interacts
CC with SLA2 (PubMed:11891219). Interacts with TRAT1. Interacts with
CC DOCK2. Interacts with SHB. Interacts with ZAP70. Interacts (tyrosine
CC phosphorylated) with SHC1 (via SH2 domain). Interacts with PTPRC (By
CC similarity). Interacts with CRK; this interaction regulates CD3Z
CC phosphorylation (By similarity). Interacts (on T cell side) with CD81,
CC ICAM1 and CD9 at immunological synapses between antigen-presenting
CC cells and T cells. Interacts with CD160. Interacts with LY6E. Interacts
CC with LY6E (By similarity). The signaling subunit of immunoglobulin
CC gamma (IgG) Fc receptor complex. As a homodimer or a heterodimer with
CC FCER1G, associates with the ligand binding subunit FCGR3A (via
CC transmembrane domain); this interaction is a prerequisite for Fc
CC receptor complex expression on the cell surface.
CC {ECO:0000250|UniProtKB:P20963, ECO:0000269|PubMed:10662792,
CC ECO:0000269|PubMed:11891219, ECO:0000269|PubMed:9575182}.
CC -!- INTERACTION:
CC P24161; Q9WU22: Ptpn4; NbExp=3; IntAct=EBI-7803400, EBI-7249866;
CC P24161; P43404: Zap70; NbExp=4; IntAct=EBI-7803400, EBI-3862932;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9575182};
CC Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=CD-3-zeta;
CC IsoId=P24161-1; Sequence=Displayed;
CC Name=CD-3-eta;
CC IsoId=P24161-2; Sequence=VSP_058346;
CC -!- TISSUE SPECIFICITY: CD3Z is expressed in normal lymphoid tissue and in
CC peripheral blood mononuclear cells (PBMCs). Expressed also in retinal
CC ganglion cells (PubMed:20188655). {ECO:0000269|PubMed:20188655,
CC ECO:0000305}.
CC -!- DOMAIN: The ITAM domains mediate interaction with SHB. {ECO:0000250}.
CC -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC LCK in association with CD4/CD8. {ECO:0000269|PubMed:9575182}.
CC -!- DISRUPTION PHENOTYPE: CD3Z deletion causes severely defective thymocyte
CC differentiation (PubMed:8223495). Absence of CD3Z also leads to altered
CC dendritic structure and motility in developing retina
CC (PubMed:20188655). {ECO:0000269|PubMed:20188655,
CC ECO:0000269|PubMed:8223495}.
CC -!- SIMILARITY: Belongs to the CD3Z/FCER1G family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M19729; AAA40171.1; -; Genomic_DNA.
DR EMBL; J04967; AAA50301.1; -; mRNA.
DR EMBL; M33158; AAA37398.1; -; mRNA.
DR EMBL; AK017904; BAB30997.1; -; mRNA.
DR EMBL; BC052824; AAH52824.1; -; mRNA.
DR EMBL; M76711; AAA40403.1; -; Genomic_DNA.
DR CCDS; CCDS15443.1; -. [P24161-2]
DR CCDS; CCDS48427.1; -. [P24161-1]
DR PIR; A35900; A35900.
DR PIR; A40104; A40104.
DR RefSeq; NP_001106862.1; NM_001113391.2. [P24161-1]
DR RefSeq; NP_112439.1; NM_031162.4. [P24161-2]
DR RefSeq; XP_011237047.1; XM_011238745.2. [P24161-1]
DR RefSeq; XP_017168774.1; XM_017313285.1. [P24161-1]
DR AlphaFoldDB; P24161; -.
DR SMR; P24161; -.
DR BioGRID; 198598; 7.
DR CORUM; P24161; -.
DR ELM; P24161; -.
DR IntAct; P24161; 7.
DR MINT; P24161; -.
DR STRING; 10090.ENSMUSP00000124297; -.
DR iPTMnet; P24161; -.
DR PhosphoSitePlus; P24161; -.
DR EPD; P24161; -.
DR jPOST; P24161; -.
DR PRIDE; P24161; -.
DR ProteomicsDB; 281135; -. [P24161-1]
DR ProteomicsDB; 281136; -. [P24161-2]
DR ABCD; P24161; 1 sequenced antibody.
DR Antibodypedia; 1663; 1501 antibodies from 45 providers.
DR DNASU; 12503; -.
DR Ensembl; ENSMUST00000005907; ENSMUSP00000005907; ENSMUSG00000005763. [P24161-1]
DR Ensembl; ENSMUST00000027849; ENSMUSP00000027849; ENSMUSG00000005763. [P24161-2]
DR Ensembl; ENSMUST00000086002; ENSMUSP00000083165; ENSMUSG00000005763. [P24161-2]
DR Ensembl; ENSMUST00000187313; ENSMUSP00000140926; ENSMUSG00000005763. [P24161-2]
DR GeneID; 12503; -.
DR KEGG; mmu:12503; -.
DR UCSC; uc007djn.2; mouse. [P24161-1]
DR CTD; 919; -.
DR MGI; MGI:88334; Cd247.
DR VEuPathDB; HostDB:ENSMUSG00000005763; -.
DR eggNOG; ENOG502S5AZ; Eukaryota.
DR GeneTree; ENSGT00390000018208; -.
DR HOGENOM; CLU_119104_0_0_1; -.
DR OMA; MKWKRIA; -.
DR OrthoDB; 1389458at2759; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
DR Reactome; R-MMU-202433; Generation of second messenger molecules.
DR Reactome; R-MMU-2029481; FCGR activation.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-MMU-389948; PD-1 signaling.
DR BioGRID-ORCS; 12503; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Cd247; mouse.
DR PRO; PR:P24161; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P24161; protein.
DR Bgee; ENSMUSG00000005763; Expressed in thymus and 87 other tissues.
DR ExpressionAtlas; P24161; baseline and differential.
DR Genevisible; P24161; MM.
DR GO; GO:0042105; C:alpha-beta T cell receptor complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0033001; C:Fc-gamma receptor III complex; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0042101; C:T cell receptor complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0038094; P:Fc-gamma receptor signaling pathway; ISO:MGI.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI.
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 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Immunity; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..164
FT /note="T-cell surface glycoprotein CD3 zeta chain"
FT /id="PRO_0000016494"
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..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 61..89
FT /note="ITAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT DOMAIN 100..128
FT /note="ITAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT DOMAIN 131..159
FT /note="ITAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT REGION 87..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Blocked amino end (Gln)"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20963"
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 111
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 123
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 142
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 153
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20963,
FT ECO:0000255|PROSITE-ProRule:PRU00379"
FT VAR_SEQ 144..164
FT /note="GLSTATKDTYDALHMQTLAPR -> DSHFQAVQFGNRREREGSELTRTLGLR
FT ARPKGESTQQSSQSCASVFSIPTLWSPWPPSSSSQL (in isoform CD-3-eta)"
FT /id="VSP_058346"
FT CONFLICT 153
FT /note="Y -> C (in Ref. 4; BAB30997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 18637 MW; 1B8022035A312831 CRC64;
MKWKVSVLAC ILHVRFPGAE AQSFGLLDPK LCYLLDGILF IYGVIITALY LRAKFSRSAE
TAANLQDPNQ LYNELNLGRR EEYDVLEKKR ARDPEMGGKQ QRRRNPQEGV YNALQKDKMA
EAYSEIGTKG ERRRGKGHDG LYQGLSTATK DTYDALHMQT LAPR
