ID W5MFY3_LEPOC Unreviewed; 128 AA.
AC W5MFY3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Ig-like domain-containing protein {ECO:0000259|PROSITE:PS50835};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000007292.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000007292.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: Alpha-beta TR is a heterodimer composed of an alpha and beta
CC chain; disulfide-linked. The alpha-beta TR is associated with the
CC transmembrane signaling CD3 coreceptor proteins to form the TR-CD3 (TcR
CC or TCR). The assembly of alpha-beta TR heterodimers with CD3 occurs in
CC the endoplasmic reticulum where a single alpha-beta TR heterodimer
CC associates with one CD3D-CD3E heterodimer, one CD3G-CD3E heterodimer
CC and one CD247 homodimer forming a stable octameric structure. CD3D-CD3E
CC and CD3G-CD3E heterodimers preferentially associate with TR alpha and
CC TR beta chains, respectively. The association of the CD247 homodimer is
CC the last step of TcR assembly in the endoplasmic reticulum and is
CC required for transport to the cell surface.
CC {ECO:0000256|ARBA:ARBA00038651}.
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DR EMBL; AHAT01019593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MFY3; -.
DR STRING; 7918.ENSLOCP00000007292; -.
DR Ensembl; ENSLOCT00000007300.1; ENSLOCP00000007292.1; ENSLOCG00000006040.1.
DR eggNOG; ENOG502SHCJ; Eukaryota.
DR GeneTree; ENSGT01070000254882; -.
DR HOGENOM; CLU_077975_8_3_1; -.
DR InParanoid; W5MFY3; -.
DR OMA; MELEMRI; -.
DR Proteomes; UP000018468; Linkage group LG24.
DR Bgee; ENSLOCG00000006040; Expressed in pharyngeal gill and 6 other cell types or tissues.
DR GO; GO:0042605; F:peptide antigen binding; IBA:GO_Central.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR19343:SF13; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR19343; T CELL RECEPTOR ALPHA VARIABLE 1-2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 4: Predicted;
KW Adaptive immunity {ECO:0000256|ARBA:ARBA00043266};
KW Immunity {ECO:0000256|ARBA:ARBA00043266};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Signal {ECO:0000256|SAM:SignalP};
KW T cell receptor {ECO:0000256|ARBA:ARBA00043266}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..128
FT /note="Ig-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004866018"
FT DOMAIN 23..112
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 128 AA; 14604 MW; E7CEBBB734514C55 CRC64;
SEKGWLFLLL HTVTHLHYVR SAEQVSQIPA QVTVAEGRTA SIHCNYTDSR VTVVHWYRQQ
PSTKPEKVIS SYGDLERENQ LSAWLNTKGR FGVFNISLSQ TGDSALYYCA VEAQVHFQYV
ENIHNPHS
//