ID   CD1B3_SHEEP             Reviewed;         232 AA.
AC   P80943;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=T-cell surface glycoprotein CD1b-3;
DE   AltName: Full=sCD1-T10;
DE   AltName: CD_antigen=CD1b-3;
DE   Flags: Fragment;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal thymocyte;
RX   PubMed=8662069; DOI=10.1007/bf02660055;
RA   Ferguson E.E., Dutia B.M., Hein W.R., Hopkins J.;
RT   "The sheep CD1 gene family contains at least four CD1B homologues.";
RL   Immunogenetics 44:86-96(1996).
CC   -!- FUNCTION: Antigen-presenting protein that binds self and non-self lipid
CC       and glycolipid antigens and presents them to T-cell receptors on
CC       natural killer T-cells. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with
CC       saposin C (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}.
CC       Lysosome membrane {ECO:0000250}. Note=Subject to intracellular
CC       trafficking between the cell membrane, endosomes and lysosomes.
CC       Localizes to cell surface lipid rafts (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: During protein synthesis and maturation, CD1 family
CC       members bind endogenous lipids that are replaced by lipid or glycolipid
CC       antigens when the proteins are internalized and pass through endosomes
CC       or lysosomes, before trafficking back to the cell surface. Interaction
CC       with saposin C is required for the loading of bacterial lipid antigens
CC       onto CD1B in the lysosome (By similarity). {ECO:0000250}.
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DR   EMBL; X90567; CAA62187.1; -; mRNA.
DR   PIR; S58353; S58353.
DR   AlphaFoldDB; P80943; -.
DR   SMR; P80943; -.
DR   STRING; 9940.ENSOARP00000007813; -.
DR   eggNOG; ENOG502SJH6; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.500.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR011161; MHC_I-like_Ag-recog.
DR   InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR   InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF16497; MHC_I_3; 1.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF54452; SSF54452; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Adaptive immunity; Cell membrane; Disulfide bond; Endosome; Glycoprotein;
KW   Immunity; Immunoglobulin domain; Lysosome; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..232
FT                   /note="T-cell surface glycoprotein CD1b-3"
FT                   /id="PRO_0000072670"
FT   TOPO_DOM        <1..201
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..232
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          84..194
FT                   /note="Ig-like"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        19..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        48..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        123..178
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   NON_TER         1
SQ   SEQUENCE   232 AA;  26023 MW;  C96DB93840B56158 CRC64;
     GLQEFQFEYP FVIQGIAGCE LHSGKAIQSF LRAGFEGLDF VSIENHSCVP EPEGGSEAQW
     FCVFITQYQG ILAIIDRLLS KTCPRYLLGV LDAGKAELHR QVKPEAWLSS GPTPGPGRLL
     LVCHVSGFYP KPVRVMWMRG EQEQPGTQQG NIILNADWTW YLRVTLDVAA GEAAGLSCRV
     KHSSLGDQDI ILYWGHPMYI GLIFVAIIVP SLILLICLAL WFWRRWSYQT VL