ID   Q8AXI4_GINCI            Unreviewed;       113 AA.
AC   Q8AXI4;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Novel antigen receptor {ECO:0000313|EMBL:AAN75852.1};
DE   Flags: Fragment;
OS   Ginglymostoma cirratum (Nurse shark) (Squalus cirratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes;
OC   Ginglymostomatidae; Ginglymostoma.
OX   NCBI_TaxID=7801 {ECO:0000313|EMBL:AAN75852.1};
RN   [1] {ECO:0000313|EMBL:AAN75852.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12909128; DOI=10.1016/S0161-5890(03)00084-1;
RA   Dooley H., Flajnik M.F., Porter A.J.;
RT   "Selection and characterization of naturally occurring single-domain
RT   (IgNAR) antibody fragments from immunized sharks by phage display.";
RL   Mol. Immunol. 40:25-33(2003).
RN   [2] {ECO:0007829|PDB:1SQ2, ECO:0007829|PDB:1T6V}
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=15319492; DOI=10.1126/science.1101148;
RA   Stanfield R.L., Dooley H., Flajnik M.F., Wilson I.A.;
RT   "Crystal structure of a shark single-domain antibody V region in complex
RT   with lysozyme.";
RL   Science 305:1770-1773(2004).
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; AF447096; AAN75852.1; -; mRNA.
DR   PDB; 1SQ2; X-ray; 1.45 A; N=1-113.
DR   PDB; 1T6V; X-ray; 1.70 A; N/O=1-113.
DR   PDBsum; 1SQ2; -.
DR   PDBsum; 1T6V; -.
DR   AlphaFoldDB; Q8AXI4; -.
DR   SMR; Q8AXI4; -.
DR   EvolutionaryTrace; Q8AXI4; -.
DR   CDD; cd00099; IgV; 1.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1SQ2, ECO:0007829|PDB:1T6V};
KW   Adaptive immunity {ECO:0000256|ARBA:ARBA00043266};
KW   Immunity {ECO:0000256|ARBA:ARBA00043266};
KW   Receptor {ECO:0000313|EMBL:AAN75852.1};
KW   T cell receptor {ECO:0000256|ARBA:ARBA00043266}.
FT   DOMAIN          1..83
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DISULFID        22..83
FT                   /evidence="ECO:0007829|PDB:1SQ2, ECO:0007829|PDB:1T6V"
FT   DISULFID        35..92
FT                   /evidence="ECO:0007829|PDB:1SQ2, ECO:0007829|PDB:1T6V"
FT   DISULFID        97..104
FT                   /evidence="ECO:0007829|PDB:1SQ2, ECO:0007829|PDB:1T6V"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAN75852.1"
FT   NON_TER         113
FT                   /evidence="ECO:0000313|EMBL:AAN75852.1"
SQ   SEQUENCE   113 AA;  12042 MW;  71522771FEA75661 CRC64;
     ARVDQTPRSV TKETGESLTI NCVLRDASYA LGSTCWYRKK SGEGNEESIS KGGRYVETVN
     SGSKSFSLRI NDLTVEDGGT YRCGLGVAGG YCDYALCSSR YAECGDGTAV TVN
//