ID   CD1B2_SHEEP             Reviewed;         333 AA.
AC   Q29422;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=T-cell surface glycoprotein CD1b-2;
DE   AltName: Full=Antigen IAH-CC14;
DE   AltName: Full=sCD1B-42;
DE   AltName: CD_antigen=CD1b-2;
DE   Flags: Precursor;
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=Thymus;
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-33.
RX   PubMed=9914336; DOI=10.1007/s002510050483;
RA   Rhind S.M., Hopkins J., Dutia B.M.;
RT   "Amino-terminal sequencing of sheep CD1 antigens and identification of a
RT   sheep CD1D gene.";
RL   Immunogenetics 49:225-230(1999).
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; Z36891; CAA85360.1; -; mRNA.
DR   PIR; S47246; S47246.
DR   RefSeq; NP_001009423.1; NM_001009423.1.
DR   AlphaFoldDB; Q29422; -.
DR   SMR; Q29422; -.
DR   GeneID; 443441; -.
DR   KEGG; oas:443441; -.
DR   eggNOG; ENOG502SJH6; Eukaryota.
DR   OrthoDB; 827472at2759; -.
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   1: Evidence at protein level;
KW   Adaptive immunity; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Endosome; Glycoprotein; Immunity; Immunoglobulin domain;
KW   Lysosome; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:9914336"
FT   CHAIN           21..333
FT                   /note="T-cell surface glycoprotein CD1b-2"
FT                   /id="PRO_0000014597"
FT   TOPO_DOM        21..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..333
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          185..295
FT                   /note="Ig-like"
FT   MOTIF           329..332
FT                   /note="Internalization signal"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        120..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        149..163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        224..279
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   333 AA;  37040 MW;  861BAE9617DB9BA1 CRC64;
     MLLLPLLLLG VILPGGDNED VFQGPTSFHL KQISTFVNST WAQNLGSGWL DDLQIHGWES
     DSGTAIFLKP WSKGNFSDEE ITELVDLFRV YLIGFIREVQ DRVNEFQLEY PFVIQVIEGC
     ELHSGEAIES SLRGALGGLD VLRIQNHSCM PAPDSGNRGQ KLCALLSQYQ GTSDIIERLV
     SETCPRYLLG VLDAGKAELQ RQVKPEAWLS SGPTPGPGRL LLVCHVSGFY PKPVQVIWMR
     GKQEQPGTQQ GDIMPNADWT WYLRVTLNVA AGEAAGLSCR VKHSSLGDQD IILYWGHPTS
     IGLILVAIIV PSLILSICLA LWFWRRWSYQ NIL