ID   CD1B1_SHEEP             Reviewed;         333 AA.
AC   Q28565;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=T-cell surface glycoprotein CD1b-1;
DE   AltName: Full=sCD1A-25;
DE   AltName: CD_antigen=CD1b-1;
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=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; Z36890; CAA85359.1; -; mRNA.
DR   RefSeq; NP_001116474.1; NM_001123002.2.
DR   AlphaFoldDB; Q28565; -.
DR   SMR; Q28565; -.
DR   STRING; 9940.ENSOARP00000007799; -.
DR   GeneID; 100144425; -.
DR   KEGG; oas:100144425; -.
DR   CTD; 111334; -.
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   2: Evidence at transcript level;
KW   Adaptive immunity; Cell membrane; Disulfide bond; Endosome; Glycoprotein;
KW   Immunity; Immunoglobulin domain; Lysosome; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..333
FT                   /note="T-cell surface glycoprotein CD1b-1"
FT                   /id="PRO_0000014596"
FT   TOPO_DOM        19..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   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        120..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        224..279
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   333 AA;  37137 MW;  0144767E25525509 CRC64;
     MLLLPLLLLA VIVPGGDNED VFQGPTSFHV IQISTFANST WAQNQGSGWL DNLQLYGWDS
     DPGTTIFLKP WSKGNFSDEE VTELEELFRV YLIGFTLEVQ DHVSEFQLEY PFVIQDIAGC
     ELHPGKAVES FLKGAFGGLD FVSIKNDSCA PVPEGGSMAQ RFYELIIQYH AICDTIAKLL
     LETCPRYFLS VLDAGKAELQ RQVKPEAWLS SGPTPGPGRL LLVCHVSGFY PKPVWVMWMR
     GEQEEPGTQQ GDIMPNANWT WHLRATLDVA AGEAAGLSCR VKHSSLGDQD IVLYWGHPTS
     TGLIFVAIIV SSLILLICLA LWFWRRWSYL TIL