ID   CD1B3_CAVPO             Reviewed;         332 AA.
AC   Q9QZZ0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=T-cell surface glycoprotein CD1b3;
DE   AltName: CD_antigen=CD1b-3;
DE   Flags: Precursor;
GN   Name=CD1B3;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hartley, and NIH 2; TISSUE=Thymus;
RX   PubMed=10553074;
RA   Dascher C.C., Hiromatsu K., Naylor J.W., Brauer P.P., Brown K.A.,
RA   Storey J.R., Behar S.M., Kawasaki E.S., Porcelli S.A., Brenner M.B.,
RA   LeClair K.P.;
RT   "Conservation of a CD1 multigene family in the guinea pig.";
RL   J. Immunol. 163:5478-5488(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; AF145485; AAF12740.1; -; mRNA.
DR   RefSeq; NP_001166322.1; NM_001172851.1.
DR   AlphaFoldDB; Q9QZZ0; -.
DR   SMR; Q9QZZ0; -.
DR   STRING; 10141.ENSCPOP00000020278; -.
DR   GeneID; 100379551; -.
DR   KEGG; cpoc:100379551; -.
DR   CTD; 100379551; -.
DR   eggNOG; ENOG502SJH6; Eukaryota.
DR   InParanoid; Q9QZZ0; -.
DR   OrthoDB; 827472at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..332
FT                   /note="T-cell surface glycoprotein CD1b3"
FT                   /id="PRO_0000014585"
FT   TOPO_DOM        18..300
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        322..332
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          185..295
FT                   /note="Ig-like"
FT   MOTIF           328..331
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   332 AA;  37259 MW;  AD2181E42AC6171A CRC64;
     MLLLELVFFA VLFPVGDTQD AFQEPISFHI TQITSFVNSS WVKYQLSGWL GDLQIHGMDS
     DSGTAIFLKP WSKGNFSNEE MSEVVELFRV YIVAFIRETK AHVNALQMEY PFEIQGIAGC
     ELHSGGAIVS FLQGAFGGLD FVSFKNSSCV PAPEGGSRAQ TVCKLLAPYH DIFYTVEKLL
     YETCPQYLLG VLQAGKADLH RQVKPKAWLS SGSTHEPGHL QLVCHVSGFY PKPVWVMWMR
     GEQELPETQR GDILPNADGT WYLRVTLDVV TEEATGLSCR VKHSSLGGQD IVLYWGHSNP
     IGWVILAIVS CLIFFLCFAL WYFRRLRCEG IF