ID   CD1C3_CAVPO             Reviewed;         332 AA.
AC   Q9QZY6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=T-cell surface glycoprotein CD1c3;
DE   AltName: CD_antigen=CD1c-3;
DE   Flags: Precursor;
GN   Name=CD1C3;
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}.
CC       Note=Subject to intracellular trafficking between the cell membrane and
CC       endosomes. {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.
CC       {ECO:0000250}.
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DR   EMBL; AF145489; AAF12744.1; -; mRNA.
DR   RefSeq; NP_001166326.1; NM_001172855.1.
DR   AlphaFoldDB; Q9QZY6; -.
DR   SMR; Q9QZY6; -.
DR   STRING; 10141.ENSCPOP00000020952; -.
DR   Ensembl; ENSCPOT00000046800; ENSCPOP00000026320; ENSCPOG00000032010.
DR   GeneID; 100379555; -.
DR   KEGG; cpoc:100379555; -.
DR   CTD; 100379555; -.
DR   eggNOG; ENOG502SJH6; Eukaryota.
DR   GeneTree; ENSGT01040000240396; -.
DR   HOGENOM; CLU_047501_9_2_1; -.
DR   InParanoid; Q9QZY6; -.
DR   OMA; FVNQSWA; -.
DR   OrthoDB; 827472at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000032010; Expressed in zone of skin.
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: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; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..332
FT                   /note="T-cell surface glycoprotein CD1c3"
FT                   /id="PRO_0000014589"
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          205..292
FT                   /note="Ig-like"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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        224..279
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   332 AA;  37437 MW;  19DA52E30CC05DFC CRC64;
     MLFLQFLFLD VVLGGSITKN VVQENISFYL MQISSYANQS WVQNCGSGWL GELQTHGWDS
     ESGTIIFLHT WSRGNFSNEE LEDIPLLFHV YFSGLSLEVQ DRVSQLQIKY PFDIQARAGC
     ELHSGEPPKG FLYGALNGLN FLSYQNKSWV PSPEGGNRAQ KVCDLLNTYE GIKETAYHLI
     RDTCPRFLLG LLDAGKMDLQ RQVRPEVWLS SSPNLKPGRL LLACHVSGFY PKPIWVMWMR
     GAQEQLETKQ GDILPHADGT WYLRVTLDVA AKEAAGLSCR VRHSSLRDQD IILYWGHGLS
     VILITFAVIV PLVLLIILVL LCKKCCTYQG IP