ID   CD1B4_CAVPO             Reviewed;         330 AA.
AC   Q9QZY9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=T-cell surface glycoprotein CD1b4;
DE   AltName: CD_antigen=CD1b-4;
DE   Flags: Precursor;
GN   Name=CD1B4;
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; AF145486; AAF12741.1; -; mRNA.
DR   RefSeq; NP_001166323.1; NM_001172852.1.
DR   AlphaFoldDB; Q9QZY9; -.
DR   SMR; Q9QZY9; -.
DR   STRING; 10141.ENSCPOP00000021220; -.
DR   GeneID; 100379552; -.
DR   KEGG; cpoc:100379552; -.
DR   CTD; 100379552; -.
DR   eggNOG; ENOG502SJH6; Eukaryota.
DR   InParanoid; Q9QZY9; -.
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..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..330
FT                   /note="T-cell surface glycoprotein CD1b4"
FT                   /id="PRO_0000014586"
FT   TOPO_DOM        16..299
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..330
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          182..292
FT                   /note="Ig-like"
FT   MOTIF           326..329
FT                   /note="Internalization signal"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        117..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        221..276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   330 AA;  37967 MW;  0A1FC163571CDD71 CRC64;
     MLLLALAFFF PAGDTQNVLP GKISFYGIQI STFFNHTVVE NRGSGWLGDM EISSWDSEKE
     TIIFRKPWSK GNFSNDEILE VEEIFQVYFF GFVREAQKHM SDFQVEYPFE IQVISGCEVN
     SHRSFDYFMR VAVKGLDLLS IKNHSCWPAP EGVSRAQEIW TLILQYKRIC DTVEILLTKT
     CPRYLMSVIE AGKSDLQKQV KPDAWLSQGP SPGPGLLQLV CHVSGFYPKP VWVMWMRGDK
     ELPETQKRDV LPNADETWYL RVTLDVAAEE AAGLSCRVKH SSLEGQDIIL YWGHSISIGW
     IILAVLVPCL IVLVLFILWF YRRWSYEDIF