CD1A_HUMAN
ID CD1A_HUMAN Reviewed; 327 AA.
AC P06126; D3DVD7; Q13962; Q5TDJ8; Q9UMM4; Q9Y5M5;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 4.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=T-cell surface glycoprotein CD1a;
DE AltName: Full=T-cell surface antigen T6/Leu-6;
DE Short=hTa1 thymocyte antigen;
DE AltName: CD_antigen=CD1a;
DE Flags: Precursor;
GN Name=CD1A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-30 AND TRP-68.
RX PubMed=2701945;
RA Aruffo A., Seed B.;
RT "Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c
RT demonstrates a hierarchy of exclusion in fibroblasts.";
RL J. Immunol. 143:1723-1730(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2447586; DOI=10.1073/pnas.84.24.9189;
RA Martin L.H., Calabi F., Lefebvre F.-A., Bilsland C.A.G., Milstein C.;
RT "Structure and expression of the human thymocyte antigens CD1a, CD1b, and
RT CD1c.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:9189-9193(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-108.
RX PubMed=10488738; DOI=10.1034/j.1399-0039.1999.540202.x;
RA Han M., Hannick L.I., DiBrino M., Robinson M.A.;
RT "Polymorphism of human CD1 genes.";
RL Tissue Antigens 54:122-127(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-327.
RX PubMed=2784820; DOI=10.1111/1523-1747.ep12712175;
RA Longley J., Kraus J., Alonso M., Edelson R.;
RT "Molecular cloning of CD1a (T6), a human epidermal dendritic cell marker
RT related to class I MHC molecules.";
RL J. Invest. Dermatol. 92:628-631(1989).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-327.
RC TISSUE=T-cell;
RX PubMed=3093894; DOI=10.1038/323540a0;
RA Calabi F., Milstein C.;
RT "A novel family of human major histocompatibility complex-related genes not
RT mapping to chromosome 6.";
RL Nature 323:540-543(1986).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-294.
RX PubMed=3097645; DOI=10.1073/pnas.83.23.9154;
RA Martin L.H., Calabi F., Milstein C.;
RT "Isolation of CD1 genes: a family of major histocompatibility complex-
RT related differentiation antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9154-9158(1986).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11231314; DOI=10.1046/j.1523-1747.2001.01264.x;
RA Salamero J., Bausinger H., Mommaas A.M., Lipsker D., Proamer F.,
RA Cazenave J.-P., Goud B., de la Salle H., Hanau D.;
RT "CD1a molecules traffic through the early recycling endosomal pathway in
RT human Langerhans cells.";
RL J. Invest. Dermatol. 116:401-408(2001).
RN [11]
RP FUNCTION.
RX PubMed=16272286; DOI=10.4049/jimmunol.175.10.6344;
RA Vincent M.S., Xiong X., Grant E.P., Peng W., Brenner M.B.;
RT "CD1a-, b-, and c-restricted TCRs recognize both self and foreign
RT antigens.";
RL J. Immunol. 175:6344-6351(2005).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CD47, AND TISSUE
RP SPECIFICITY.
RX PubMed=18178838; DOI=10.4049/jimmunol.180.2.980;
RA Sloma I., Zilber M.-T., Vasselon T., Setterblad N., Cavallari M., Mori L.,
RA De Libero G., Charron D., Mooney N., Gelin C.;
RT "Regulation of CD1a surface expression and antigen presentation by
RT invariant chain and lipid rafts.";
RL J. Immunol. 180:980-987(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 18-300 IN COMPLEX WITH B2M AND
RP SULFATIDE SELF-ANTIGEN, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION
RP AT ASN-37; ASN-74 AND ASN-145, AND DISULFIDE BOND.
RX PubMed=12833155; DOI=10.1038/ni948;
RA Zajonc D.M., Elsliger M.-A., Teyton L., Wilson I.A.;
RT "Crystal structure of CD1a in complex with a sulfatide self antigen at a
RT resolution of 2.15 A.";
RL Nat. Immunol. 4:808-815(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-294 IN COMPLEX WITH B2M AND
RP LIPOPEPTIDE, GLYCOSYLATION AT ASN-37; ASN-74 AND ASN-145, AND DISULFIDE
RP BOND.
RX PubMed=15723809; DOI=10.1016/j.immuni.2004.12.009;
RA Zajonc D.M., Crispin M.D., Bowden T.A., Young D.C., Cheng T.-Y., Hu J.,
RA Costello C.E., Rudd P.M., Dwek R.A., Miller M.J., Brenner M.B., Moody D.B.,
RA Wilson I.A.;
RT "Molecular mechanism of lipopeptide presentation by CD1a.";
RL Immunity 22:209-219(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 21-295, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-74 AND ASN-145.
RX PubMed=25642819; DOI=10.1038/ni.3098;
RA Birkinshaw R.W., Pellicci D.G., Cheng T.Y., Keller A.N.,
RA Sandoval-Romero M., Gras S., de Jong A., Uldrich A.P., Moody D.B.,
RA Godfrey D.I., Rossjohn J.;
RT "alphabeta T cell antigen receptor recognition of CD1a presenting self
RT lipid ligands.";
RL Nat. Immunol. 16:258-266(2015).
RN [16]
RP VARIANTS ILE-30 AND TRP-68, AND SUBCELLULAR LOCATION.
RX PubMed=11600221; DOI=10.1016/s0198-8859(01)00314-7;
RA Oteo M., Arribas P., Setien F., Parra J.F., Mirones I., Gomez del Moral M.,
RA Martinez-Naves E.;
RT "Structural characterization of two CD1A allelic variants.";
RL Hum. Immunol. 62:1137-1141(2001).
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:0000269|PubMed:11231314,
CC ECO:0000269|PubMed:16272286, ECO:0000269|PubMed:18178838}.
CC -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with
CC CD74. {ECO:0000269|PubMed:12833155, ECO:0000269|PubMed:15723809,
CC ECO:0000269|PubMed:18178838}.
CC -!- INTERACTION:
CC P06126; P61769: B2M; NbExp=2; IntAct=EBI-1036766, EBI-714718;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11231314,
CC ECO:0000269|PubMed:11600221, ECO:0000269|PubMed:18178838}; Single-pass
CC type I membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000269|PubMed:18178838}; Single-pass type I membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:11231314}; Single-
CC pass type I membrane protein {ECO:0000255}. Note=Subject to
CC intracellular trafficking between the cell membrane and endosomes
CC (PubMed:11231314). Localizes to cell surface lipid rafts
CC (PubMed:18178838). {ECO:0000269|PubMed:11231314,
CC ECO:0000269|PubMed:18178838}.
CC -!- TISSUE SPECIFICITY: Expressed on cortical thymocytes, epidermal
CC Langerhans cells, dendritic cells, on certain T-cell leukemias, and in
CC various other tissues. {ECO:0000269|PubMed:11231314,
CC ECO:0000269|PubMed:18178838}.
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.
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DR EMBL; M28825; AAA51931.1; -; mRNA.
DR EMBL; M22167; AAA51932.1; -; Genomic_DNA.
DR EMBL; M22080; AAA51932.1; JOINED; Genomic_DNA.
DR EMBL; M22163; AAA51932.1; JOINED; Genomic_DNA.
DR EMBL; M22164; AAA51932.1; JOINED; Genomic_DNA.
DR EMBL; M22165; AAA51932.1; JOINED; Genomic_DNA.
DR EMBL; M22166; AAA51932.1; JOINED; Genomic_DNA.
DR EMBL; AK312945; BAG35786.1; -; mRNA.
DR EMBL; AL121986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52843.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52844.1; -; Genomic_DNA.
DR EMBL; AF142665; AAD37578.1; -; Genomic_DNA.
DR EMBL; M27735; AAA51933.1; -; mRNA.
DR EMBL; X04450; CAA28049.1; -; mRNA.
DR EMBL; M14663; AAA51934.1; -; Genomic_DNA.
DR CCDS; CCDS1174.1; -.
DR PIR; A39957; HLHUCD.
DR RefSeq; NP_001307581.1; NM_001320652.1.
DR RefSeq; NP_001754.2; NM_001763.2.
DR PDB; 1ONQ; X-ray; 2.15 A; A/C=18-294.
DR PDB; 1XZ0; X-ray; 2.80 A; A/C=18-294.
DR PDB; 4X6C; X-ray; 2.80 A; A/C=21-295.
DR PDB; 4X6D; X-ray; 2.98 A; A/C=21-295.
DR PDB; 4X6E; X-ray; 2.10 A; A=21-295.
DR PDB; 4X6F; X-ray; 1.91 A; A=21-295.
DR PDB; 5J1A; X-ray; 1.86 A; A=1-295.
DR PDB; 6NUX; X-ray; 2.20 A; A=21-295.
DR PDB; 7KOZ; X-ray; 2.25 A; A=18-295.
DR PDB; 7KP0; X-ray; 2.40 A; A=18-295.
DR PDB; 7KP1; X-ray; 2.02 A; A=18-295.
DR PDBsum; 1ONQ; -.
DR PDBsum; 1XZ0; -.
DR PDBsum; 4X6C; -.
DR PDBsum; 4X6D; -.
DR PDBsum; 4X6E; -.
DR PDBsum; 4X6F; -.
DR PDBsum; 5J1A; -.
DR PDBsum; 6NUX; -.
DR PDBsum; 7KOZ; -.
DR PDBsum; 7KP0; -.
DR PDBsum; 7KP1; -.
DR AlphaFoldDB; P06126; -.
DR SMR; P06126; -.
DR BioGRID; 107347; 83.
DR IntAct; P06126; 4.
DR STRING; 9606.ENSP00000289429; -.
DR DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit).
DR GlyGen; P06126; 5 sites.
DR iPTMnet; P06126; -.
DR PhosphoSitePlus; P06126; -.
DR SwissPalm; P06126; -.
DR BioMuta; CD1A; -.
DR DMDM; 288558852; -.
DR jPOST; P06126; -.
DR MassIVE; P06126; -.
DR MaxQB; P06126; -.
DR PaxDb; P06126; -.
DR PeptideAtlas; P06126; -.
DR PRIDE; P06126; -.
DR ProteomicsDB; 51868; -.
DR ABCD; P06126; 1 sequenced antibody.
DR Antibodypedia; 2533; 2030 antibodies from 49 providers.
DR DNASU; 909; -.
DR Ensembl; ENST00000289429.6; ENSP00000289429.5; ENSG00000158477.7.
DR GeneID; 909; -.
DR KEGG; hsa:909; -.
DR MANE-Select; ENST00000289429.6; ENSP00000289429.5; NM_001763.3; NP_001754.2.
DR UCSC; uc001frt.4; human.
DR CTD; 909; -.
DR DisGeNET; 909; -.
DR GeneCards; CD1A; -.
DR HGNC; HGNC:1634; CD1A.
DR HPA; ENSG00000158477; Tissue enriched (lymphoid).
DR MIM; 188370; gene.
DR neXtProt; NX_P06126; -.
DR OpenTargets; ENSG00000158477; -.
DR PharmGKB; PA26193; -.
DR VEuPathDB; HostDB:ENSG00000158477; -.
DR eggNOG; ENOG502SJH6; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_9_2_1; -.
DR InParanoid; P06126; -.
DR OMA; QVAGGCE; -.
DR OrthoDB; 827472at2759; -.
DR PhylomeDB; P06126; -.
DR TreeFam; TF336723; -.
DR PathwayCommons; P06126; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; P06126; -.
DR BioGRID-ORCS; 909; 8 hits in 1073 CRISPR screens.
DR EvolutionaryTrace; P06126; -.
DR GeneWiki; CD1A; -.
DR GenomeRNAi; 909; -.
DR Pharos; P06126; Tbio.
DR PRO; PR:P06126; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P06126; protein.
DR Bgee; ENSG00000158477; Expressed in thymus and 67 other tissues.
DR Genevisible; P06126; HS.
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:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0006955; P:immune response; NAS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond; Endosome;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT CHAIN 17..327
FT /note="T-cell surface glycoprotein CD1a"
FT /id="PRO_0000014578"
FT TOPO_DOM 17..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 184..291
FT /note="Ig-like"
FT BINDING 90..94
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000269|PubMed:12833155,
FT ECO:0007744|PDB:1ONQ"
FT BINDING 171
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000269|PubMed:12833155,
FT ECO:0007744|PDB:1ONQ"
FT BINDING 175
FT /ligand="a D-galactosylceramide"
FT /ligand_id="ChEBI:CHEBI:36498"
FT /evidence="ECO:0000269|PubMed:12833155,
FT ECO:0007744|PDB:1ONQ"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12833155,
FT ECO:0000269|PubMed:15723809"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12833155,
FT ECO:0000269|PubMed:15723809, ECO:0000269|PubMed:25642819"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12833155,
FT ECO:0000269|PubMed:15723809, ECO:0000269|PubMed:25642819"
FT DISULFID 119..183
FT /evidence="ECO:0000269|PubMed:25642819,
FT ECO:0007744|PDB:4X6C"
FT DISULFID 223..278
FT /evidence="ECO:0000269|PubMed:12833155,
FT ECO:0000269|PubMed:15723809, ECO:0000269|PubMed:25642819,
FT ECO:0007744|PDB:1ONQ, ECO:0007744|PDB:1XZ0,
FT ECO:0007744|PDB:4X6C"
FT VARIANT 22
FT /note="K -> N (in dbSNP:rs3087217)"
FT /id="VAR_062522"
FT VARIANT 30
FT /note="T -> I (in dbSNP:rs2269714)"
FT /evidence="ECO:0000269|PubMed:11600221,
FT ECO:0000269|PubMed:2701945"
FT /id="VAR_010209"
FT VARIANT 68
FT /note="C -> W (in dbSNP:rs2269715)"
FT /evidence="ECO:0000269|PubMed:11600221,
FT ECO:0000269|PubMed:2701945"
FT /id="VAR_010210"
FT CONFLICT 70..71
FT /note="WS -> V (in Ref. 7; AAA51933)"
FT /evidence="ECO:0000305"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:5J1A"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:5J1A"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:5J1A"
FT HELIX 77..101
FT /evidence="ECO:0007829|PDB:5J1A"
FT TURN 102..106
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 109..119
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:5J1A"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5J1A"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:5J1A"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:5J1A"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:5J1A"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:5J1A"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 218..231
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:4X6C"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:5J1A"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:5J1A"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5J1A"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5J1A"
SQ SEQUENCE 327 AA; 37077 MW; C575C3C538F0AA29 CRC64;
MLFLLLPLLA VLPGDGNADG LKEPLSFHVT WIASFYNHSW KQNLVSGWLS DLQTHTWDSN
SSTIVFLCPW SRGNFSNEEW KELETLFRIR TIRSFEGIRR YAHELQFEYP FEIQVTGGCE
LHSGKVSGSF LQLAYQGSDF VSFQNNSWLP YPVAGNMAKH FCKVLNQNQH ENDITHNLLS
DTCPRFILGL LDAGKAHLQR QVKPEAWLSH GPSPGPGHLQ LVCHVSGFYP KPVWVMWMRG
EQEQQGTQRG DILPSADGTW YLRATLEVAA GEAADLSCRV KHSSLEGQDI VLYWEHHSSV
GFIILAVIVP LLLLIGLALW FRKRCFC
