ID   CD1B_AOTNA              Reviewed;         333 AA.
AC   Q5YB65;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=T-cell surface glycoprotein CD1b;
DE   AltName: CD_antigen=CD1b;
DE   Flags: Precursor;
GN   Name=CD1B;
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Monocyte;
RX   PubMed=15365647; DOI=10.1007/s00251-004-0716-8;
RA   Castillo F., Guerrero C., Trujillo E., Delgado G., Martinez P.,
RA   Salazar L.M., Barato P., Patarroyo M.E., Parra-Lopez C.;
RT   "Identifying and structurally characterizing CD1b in Aotus nancymaae owl
RT   monkeys.";
RL   Immunogenetics 56:480-489(2004).
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|UniProtKB:P29016};
CC       Single-pass type I membrane protein {ECO:0000255}. Endosome membrane
CC       {ECO:0000250|UniProtKB:P29016}; Single-pass type I membrane protein
CC       {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P29016};
CC       Single-pass type I membrane protein {ECO:0000255}. Note=Subject to
CC       intracellular trafficking between the cell membrane, endosomes and
CC       lysosomes. {ECO:0000250|UniProtKB:P29016}.
CC   -!- TISSUE SPECIFICITY: Expressed in lymphocytes, spleen, lung, liver,
CC       kidney and heart. {ECO:0000269|PubMed:15365647}.
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; AY605931; AAT37499.1; -; mRNA.
DR   AlphaFoldDB; Q5YB65; -.
DR   SMR; Q5YB65; -.
DR   STRING; 37293.ENSANAP00000022297; -.
DR   Proteomes; UP000233020; Whole Genome Shotgun Assembly.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..333
FT                   /note="T-cell surface glycoprotein CD1b"
FT                   /id="PRO_0000045408"
FT   TOPO_DOM        19..303
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..333
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          185..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   CARBOHYD        258
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;  36500 MW;  B7C7D455B60819C4 CRC64;
     MLLLPFQLLA VLFPGGNSEH AFQGPTSFHV IQTSSFTNST WAQTQGSGWL DDLQIHGWDS
     DSGTAIFLKP WSKGNFSDKE VAELEEIFRV YILGFAREVQ DFAGDFQMKY PFEIQGIAGC
     GLHSGGAIVS FLRGALGGLD FLSVKNASCV PSPEGGSRAQ KVCALIMQYQ GIMEIVRLLL
     YKTCPRYLLG VLNAGKADLQ GKMKPEAWLS SGPSPGPGRL LLVCHVSGFC PKPVWVMWMP
     GEQEQQGTQL GDILPNANWT WYLRATLDVA AGEAAGLSCR VKHSSLEGQD IILYWSNPTS
     IGSIVLAIIV PSLLLLLCLA LWYMRRRSYQ NIP