ID   CD1C2_CAVPO             Reviewed;         332 AA.
AC   Q9QZY7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=T-cell surface glycoprotein CD1c2;
DE   AltName: CD_antigen=CD1c-2;
DE   Flags: Precursor;
GN   Name=CD1C2;
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; AF145488; AAF12743.1; -; mRNA.
DR   RefSeq; NP_001166325.1; NM_001172854.1.
DR   AlphaFoldDB; Q9QZY7; -.
DR   SMR; Q9QZY7; -.
DR   STRING; 10141.ENSCPOP00000011765; -.
DR   Ensembl; ENSCPOT00000038079; ENSCPOP00000030253; ENSCPOG00000038675.
DR   GeneID; 100379554; -.
DR   KEGG; cpoc:100379554; -.
DR   CTD; 100379554; -.
DR   eggNOG; ENOG502SJH6; Eukaryota.
DR   GeneTree; ENSGT01040000240396; -.
DR   HOGENOM; CLU_047501_9_2_1; -.
DR   InParanoid; Q9QZY7; -.
DR   OrthoDB; 827472at2759; -.
DR   TreeFam; TF336723; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000038675; Expressed in zone of skin and 1 other tissue.
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 CD1c2"
FT                   /id="PRO_0000014588"
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   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;  37736 MW;  9D0434EF826A05BC CRC64;
     MLFLQFLFVD VVLGGSITEN VVQENISLYL MQISSYANQS WTQNLGSAWL DQLQTHSWDS
     ESGTIIFLHA WSRGNFSNEE VTDMQLLLRV HFAELTLDVH QQASQLQFKY PFDIQVRLGC
     ELHSRETTKS FLHVAFNGLN FLSFQHKSCV PSPEGETRAQ KACDILNTYE ATKEIAYYVM
     NDICPRLLLS LLEAGKMDLQ RQVRPEVWLS SSPNLEPGRL LLACHVSGFY PKPIWVMWMR
     GAQEQLETKQ GDILPHADGT WYLRVTLNVV AEEAAGLSCR VRHSSLRDQD IILYWGHGLS
     VILIALAVIV PLVLLIVLVL LCKKRCTYQG IP