CD1A_PIG
ID CD1A_PIG Reviewed; 339 AA.
AC Q9XS72;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=T-cell surface glycoprotein CD1a;
DE AltName: CD_antigen=CD1a;
DE Flags: Precursor;
GN Name=CD1A; Synonyms=CD1.1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Chun T., Wang K., Gaskins H.R.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
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 CD74 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P06126};
CC Single-pass type I membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000250|UniProtKB:P06126}; Single-pass type I membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P06126};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Subject to
CC intracellular trafficking between the cell membrane and endosomes.
CC Localizes to cell surface lipid rafts. {ECO:0000250|UniProtKB:P06126}.
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 before trafficking back to the cell surface. {ECO:0000250}.
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DR EMBL; AF059492; AAD26983.1; -; mRNA.
DR EMBL; AF056045; AAF28737.1; -; Genomic_DNA.
DR RefSeq; NP_998996.1; NM_213831.1.
DR AlphaFoldDB; Q9XS72; -.
DR SMR; Q9XS72; -.
DR STRING; 9823.ENSSSCP00000027437; -.
DR PaxDb; Q9XS72; -.
DR PRIDE; Q9XS72; -.
DR GeneID; 396785; -.
DR KEGG; ssc:396785; -.
DR CTD; 396785; -.
DR eggNOG; ENOG502SJH6; Eukaryota.
DR InParanoid; Q9XS72; -.
DR OrthoDB; 827472at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0030883; F:endogenous lipid antigen binding; IBA:GO_Central.
DR GO; GO:0030884; F:exogenous lipid antigen binding; IBA:GO_Central.
DR GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0048006; P:antigen processing and presentation, endogenous lipid antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:GO_Central.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..339
FT /note="T-cell surface glycoprotein CD1a"
FT /id="PRO_0000014593"
FT TOPO_DOM 19..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 185..295
FT /note="Ig-like"
FT BINDING 91..95
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000250|UniProtKB:P06126"
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 339 AA; 38631 MW; E6B2DD14E515D818 CRC64;
MLFLQLPLLL VLLPGGDSEE GFQEPISFQI IWISSFYNRS WEEEVCSAWL GELQTHRREG
KSDIVIYRQP WSKGNFSRED LMESEHILRM FFVRFVQAFF NHASQWKLEY PFDVQIAGGC
DLYHGETSVG FVRIAYQGSD FASFQNNSWL PSPKGGTRAQ LVCKLFNLYQ GTLEIIHKLL
SDTCPRFVLG LLDAGKADLQ RQVRPEAWLS SGPNPSPGHL MLVCHVSGFY PKPIWVMWMR
DEQEQPGTQQ GDILPNADGT WYLRVTLDVA AGEASGLSCR VKHSSLGGQD IILYWEQHSS
VGWILLAVIV PLVLLTGLAF WHRKHWKHCD PSSALHRLE
