ID   CD1E_CAVPO              Reviewed;         390 AA.
AC   Q9QZY5;
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 CD1e, membrane-associated;
DE            Short=mCD1e;
DE   AltName: CD_antigen=CD1e;
DE   Contains:
DE     RecName: Full=T-cell surface glycoprotein CD1e, soluble;
DE              Short=sCD1e;
DE   Flags: Precursor;
GN   Name=CD1E;
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: T-cell surface glycoprotein CD1e, soluble is required for the
CC       presentation of glycolipid antigens on the cell surface. The membrane-
CC       associated form is not active (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). The association
CC       with B2M appears to be facilitated by the presence of the propeptide
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [T-cell surface glycoprotein CD1e, membrane-
CC       associated]: Golgi apparatus membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Late
CC       endosome {ECO:0000250}. Note=Predominantly localized in the trans-Golgi
CC       network in immature dendritic cells, and as a cleaved, soluble protein
CC       in the lysosome lumen of mature dendritic cells.
CC   -!- SUBCELLULAR LOCATION: [T-cell surface glycoprotein CD1e, soluble]:
CC       Lysosome lumen {ECO:0000250}.
CC   -!- PTM: Mono-ubiquitinated. {ECO:0000250}.
CC   -!- PTM: Proteolytically cleaved in endosomes to yield a soluble form.
CC       {ECO:0000250}.
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DR   EMBL; AF145490; AAF12745.1; -; mRNA.
DR   RefSeq; NP_001166215.1; NM_001172744.1.
DR   AlphaFoldDB; Q9QZY5; -.
DR   SMR; Q9QZY5; -.
DR   STRING; 10141.ENSCPOP00000007364; -.
DR   GeneID; 100379271; -.
DR   KEGG; cpoc:100379271; -.
DR   CTD; 913; -.
DR   eggNOG; ENOG502SJH6; Eukaryota.
DR   InParanoid; Q9QZY5; -.
DR   OrthoDB; 827472at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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; Disulfide bond; Endosome; Glycoprotein; Golgi apparatus;
KW   Immunity; Immunoglobulin domain; Lipid-binding; Lysosome; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..390
FT                   /note="T-cell surface glycoprotein CD1e, membrane-
FT                   associated"
FT                   /id="PRO_0000014590"
FT   PROPEP          15..33
FT                   /note="Removed in sCD1e"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000379896"
FT   CHAIN           34..390
FT                   /note="T-cell surface glycoprotein CD1e, soluble"
FT                   /id="PRO_0000379897"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          215..306
FT                   /note="Ig-like"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        131..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        234..288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   390 AA;  44292 MW;  16FD28EFEB74D853 CRC64;
     MLLLILLFFK GLVCHEKSIV GPQPLGWHHP AEAEEPLIFR LLHIASFKNH SWSHSQASAW
     IGDLQTHGWN STMGTIQFLK PWSQGDFSKE ELKNFEALFR LYFHDFPREV HAFAHQFQFE
     YPFELQISGG CKNVGKTSEN FLNGAYQGSD LLSFQRSSWE PSPGAGSRAQ KVCEVLSYYK
     DITEIVQSLL SSVCPRFLSG LIAAGKSELE RQVKPEVWLS RGPSPGRGRL QLVCHVSGFH
     PKPVWVMWMK GQQEQKGTKT GDIPNADETW YLQATLDVAE REATGLSCRV KHSSLGGHDI
     IIHWGGYSIL LILMYVAVIV TLVTLIVMGS WHRKQSSNRN VLSSYISNPT FPLENDTQCP
     RSSALQLHSA QESWIKNRIL KWKRSLNQFW