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Database: UniProt
Entry: A0A2Y9K6L6_ENHLU
LinkDB: A0A2Y9K6L6_ENHLU
Original site: A0A2Y9K6L6_ENHLU 
ID   A0A2Y9K6L6_ENHLU        Unreviewed;       192 AA.
AC   A0A2Y9K6L6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=T-cell surface glycoprotein CD3 epsilon chain {ECO:0000256|ARBA:ARBA00021773};
GN   Name=LOC111153962 {ECO:0000313|RefSeq:XP_022369026.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022369026.1};
RN   [1] {ECO:0000313|RefSeq:XP_022369026.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022369026.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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. In addition of this role of signal
CC       transduction in T-cell activation, CD3E plays an essential role in
CC       correct T-cell development. Initiates the TCR-CD3 complex assembly by
CC       forming the two heterodimers CD3D/CD3E and CD3G/CD3E. Participates also
CC       in internalization and cell surface down-regulation of TCR-CD3
CC       complexes via endocytosis sequences present in CD3E cytosolic region.
CC       {ECO:0000256|ARBA:ARBA00037671}.
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 CD6. Interacts with NCK1.
CC       Interacts with NUMB; this interaction is important for TCR-CD3
CC       internalization and subsequent degradation.
CC       {ECO:0000256|ARBA:ARBA00038787}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   RefSeq; XP_022369026.1; XM_022513318.1.
DR   AlphaFoldDB; A0A2Y9K6L6; -.
DR   STRING; 391180.A0A2Y9K6L6; -.
DR   KEGG; elk:111153962; -.
DR   OrthoDB; 5358054at2759; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0042105; C:alpha-beta T cell receptor complex; IEA:UniProt.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR015484; CD3_esu/gsu/dsu.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR   PANTHER; PTHR10570:SF9; T-CELL SURFACE GLYCOPROTEIN CD3 EPSILON CHAIN; 1.
DR   PANTHER; PTHR10570; T-CELL SURFACE GLYCOPROTEIN CD3 GAMMA CHAIN / DELTA CHAIN; 1.
DR   Pfam; PF16681; Ig_5; 1.
DR   Pfam; PF02189; ITAM; 1.
DR   SMART; SM00077; ITAM; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51055; ITAM_1; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..192
FT                   /note="T-cell surface glycoprotein CD3 epsilon chain"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016001802"
FT   TRANSMEM        112..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          38..98
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          150..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   192 AA;  21197 MW;  B35250004ED0767A CRC64;
     MQPGSLWRIL GLCLLLVGSW GQEEDMEEPS GYKVSISGTM VVLTCPVEVD PKSTKWEKNG
     KTIEGAIETQ YIMPTFSEVE DSGSYTCFSD QSKKNSLYLK ARVCKNCIEV DLMAVVAIIV
     ADICITLGVL LLVYYWSKNR KANATAVMRA KGAGGRTRGQ NKEKPPPVPN PDYEPIRKGQ
     QDLYSGLNQR GV
//
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