ID   CD1B1_CAVPO             Reviewed;         333 AA.
AC   Q9QZZ2;
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 CD1b1;
DE   AltName: CD_antigen=CD1b-1;
DE   Flags: Precursor;
GN   Name=CD1B1;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF145483; AAF12738.1; -; mRNA.
DR   RefSeq; NP_001166320.1; NM_001172849.1.
DR   AlphaFoldDB; Q9QZZ2; -.
DR   SMR; Q9QZZ2; -.
DR   ABCD; Q9QZZ2; 1 sequenced antibody.
DR   GeneID; 100379549; -.
DR   KEGG; cpoc:100379549; -.
DR   CTD; 100034038; -.
DR   eggNOG; ENOG502SJH6; Eukaryota.
DR   InParanoid; Q9QZZ2; -.
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..333
FT                   /note="T-cell surface glycoprotein CD1b1"
FT                   /id="PRO_0000014583"
FT   TOPO_DOM        18..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          197..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;  37563 MW;  EC92C91D24FA08DE CRC64;
     MLLVALALLA FLFPAGDTQN ALQWPTSVHG IQISSFFNHT MAQSRCSGWL GNMELGSFDS
     DTGTIIFKKP WSKANFSNEE VLELEELFQV YMLGFIREVQ ERMSDFQMEY PFEIQGIAGC
     ELISGGTIDF FLRGALEGLD FLSIKNSTCW PAPEGGTKAK KFCTLILQYK GIWDIMENLL
     TKTCPRYVLS VLESGKPDIQ KQVKPDAWLS QGPSPGPGLL QLVCHVSGFY PKPVWVMWMR
     GEQEQPETQK GDVLPNADET WYLQVTLDVA AEEAAGLSCR VKHSSLEGQD IILYWGHSIS
     IGWIILAVLV PCLIVLVLFV LWFYRRWSYE DIL