ID CD1B_HUMAN Reviewed; 333 AA. AC P29016; Q5TDK9; Q5TDL0; Q9UMM2; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 09-DEC-2015, entry version 149. DE RecName: Full=T-cell surface glycoprotein CD1b; DE AltName: CD_antigen=CD1b; DE Flags: Precursor; GN Name=CD1B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] 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, RT and CD1c."; RL Proc. Natl. Acad. Sci. U.S.A. 84:9189-9193(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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 [3] 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-295. 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 [6] RP FUNCTION, MUTAGENESIS OF 329-TYR-GLN-330, AND SUBCELLULAR LOCATION. RX PubMed=10981968; DOI=10.1016/S1074-7613(00)00025-X; RA Shamshiev A., Donda A., Prigozy T.I., Mori L., Chigorno V., RA Benedict C.A., Kappos L., Sonnino S., Kronenberg M., De Libero G.; RT "The alphabeta T cell response to self-glycolipids shows a novel RT mechanism of CD1b loading and a requirement for complex RT oligosaccharides."; RL Immunity 13:255-264(2000). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=10899914; DOI=10.1084/jem.192.2.281; RA Briken V., Jackman R.M., Watts G.F.M., Rogers R.A., Porcelli S.A.; RT "Human CD1b and CD1c isoforms survey different intracellular RT compartments for the presentation of microbial lipid antigens."; RL J. Exp. Med. 192:281-288(2000). RN [8] RP FUNCTION, INTERACTION WITH SAPOSIN C, AND SUBCELLULAR LOCATION. RX PubMed=14716313; DOI=10.1038/ni1035; RA Winau F., Schwierzeck V., Hurwitz R., Remmel N., Sieling P.A., RA Modlin R.L., Porcelli S.A., Brinkmann V., Sugita M., Sandhoff K., RA Kaufmann S.H.E., Schaible U.E.; RT "Saposin C is required for lipid presentation by human CD1b."; RL Nat. Immunol. 5:169-174(2004). RN [9] RP ERRATUM. RA Winau F., Schwierzeck V., Hurwitz R., Remmel N., Sieling P.A., RA Modlin R.L., Porcelli S.A., Brinkmann V., Sugita M., Sandhoff K., RA Kaufmann S.H.E., Schaible U.E.; RL Nat. Immunol. 5:344-344(2004). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-75. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 18-295 IN COMPLEXES WITH B2M; RP GANGLIOSIDE GM2 AND PHOSPHATIDYLINOSITOL, AND DISULFIDE BONDS. RX PubMed=12118248; DOI=10.1038/ni821; RA Gadola S.D., Zaccai N.R., Harlos K., Shepherd D., RA Castro-Palomino J.C., Ritter G., Schmidt R.R., Jones E.Y., RA Cerundolo V.; RT "Structure of human CD1b with bound ligands at 2.3 A, a maze for alkyl RT chains."; RL Nat. Immunol. 3:721-726(2002). RN [12] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 18-295 IN COMPLEX WITH B2M RP AND GLUCOSE MONOMYCOLATE, AND DISULFIDE BONDS. RX PubMed=14764708; DOI=10.4049/jimmunol.172.4.2382; RA Batuwangala T., Shepherd D., Gadola S.D., Gibson K.J.C., Zaccai N.R., RA Fersht A.R., Besra G.S., Cerundolo V., Jones E.Y.; RT "The crystal structure of human CD1b with a bound bacterial RT glycolipid."; RL J. Immunol. 172:2382-2388(2004). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-298 IN COMPLEX WITH B2M; RP PHOSPHATIDYLCHOLINE AND SPACER LIGAND, GLYCOSYLATION AT ASN-38 AND RP ASN-75, IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE BONDS. RX PubMed=16874306; DOI=10.1038/sj.emboj.7601244; RA Garcia-Alles L.F., Versluis K., Maveyraud L., Vallina A.T., RA Sansano S., Bello N.F., Gober H.-J., Guillet V., de la Salle H., RA Puzo G., Mori L., Heck A.J.R., De Libero G., Mourey L.; RT "Endogenous phosphatidylcholine and a long spacer ligand stabilize the RT lipid-binding groove of CD1b."; RL EMBO J. 25:3684-3692(2006). CC -!- FUNCTION: Antigen-presenting protein that binds self and non-self CC lipid and glycolipid antigens and presents them to T-cell CC receptors on natural killer T-cells. {ECO:0000269|PubMed:10981968, CC ECO:0000269|PubMed:14716313}. CC -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts CC with saposin C. {ECO:0000269|PubMed:14716313, CC ECO:0000269|PubMed:14764708, ECO:0000269|PubMed:16874306}. CC -!- INTERACTION: CC P61769:B2M; NbExp=3; IntAct=EBI-1033762, EBI-714718; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endosome membrane. Lysosome membrane. Note=Subject to CC intracellular trafficking between the cell membrane, endosomes and CC lysosomes. Localizes to cell surface lipid rafts. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P29016-1; Sequence=Displayed; CC Name=2; CC IsoId=P29016-2; Sequence=VSP_016911; CC -!- TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain CC T-cell leukemias, and in various other tissues. CC -!- MISCELLANEOUS: During protein synthesis and maturation, CD1 family CC members bind endogenous lipids that are replaced by lipid or CC glycolipid antigens when the proteins are internalized and pass CC through endosomes or lysosomes, before trafficking back to the CC cell surface. Interaction with saposin C is required for the CC loading of bacterial lipid antigens onto CD1B in the lysosome. CC -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAI10852.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M22173; AAA51940.1; -; Genomic_DNA. DR EMBL; M22168; AAA51940.1; JOINED; Genomic_DNA. DR EMBL; M22169; AAA51940.1; JOINED; Genomic_DNA. DR EMBL; M22170; AAA51940.1; JOINED; Genomic_DNA. DR EMBL; M22171; AAA51940.1; JOINED; Genomic_DNA. DR EMBL; M22172; AAA51940.1; JOINED; Genomic_DNA. DR EMBL; M28826; AAA51939.1; -; mRNA. DR EMBL; AL121986; CAI10852.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL121986; CAI10853.1; -; Genomic_DNA. DR EMBL; BC069481; AAH69481.1; -; mRNA. DR EMBL; BC074747; AAH74747.1; -; mRNA. DR EMBL; BC104216; AAI04217.1; -; mRNA. DR EMBL; BC104217; AAI04218.1; -; mRNA. DR EMBL; M14665; AAA51936.1; -; Genomic_DNA. DR CCDS; CCDS1176.1; -. [P29016-1] DR PIR; B39957; HLHUCB. DR RefSeq; NP_001755.1; NM_001764.2. [P29016-1] DR RefSeq; XP_011508421.1; XM_011510119.1. [P29016-2] DR UniGene; Hs.1310; -. DR PDB; 1GZP; X-ray; 2.80 A; A=18-295. DR PDB; 1GZQ; X-ray; 2.26 A; A=18-295. DR PDB; 1UQS; X-ray; 3.10 A; A=18-295. DR PDB; 2H26; X-ray; 1.80 A; A=19-298. DR PDB; 3OV6; X-ray; 2.50 A; A=166-295. DR PDB; 3T8X; X-ray; 1.90 A; A/C=19-298. DR PDB; 4ONO; X-ray; 2.70 A; A=201-295. DR PDBsum; 1GZP; -. DR PDBsum; 1GZQ; -. DR PDBsum; 1UQS; -. DR PDBsum; 2H26; -. DR PDBsum; 3OV6; -. DR PDBsum; 3T8X; -. DR PDBsum; 4ONO; -. DR ProteinModelPortal; P29016; -. DR SMR; P29016; 22-298. DR BioGrid; 107348; 51. DR IntAct; P29016; 1. DR MINT; MINT-242013; -. DR STRING; 9606.ENSP00000357150; -. DR PhosphoSite; P29016; -. DR BioMuta; CD1B; -. DR DMDM; 115962; -. DR MaxQB; P29016; -. DR PaxDb; P29016; -. DR PRIDE; P29016; -. DR DNASU; 910; -. DR Ensembl; ENST00000368168; ENSP00000357150; ENSG00000158485. [P29016-1] DR GeneID; 910; -. DR KEGG; hsa:910; -. DR UCSC; uc001frw.3; human. [P29016-2] DR UCSC; uc001frx.3; human. [P29016-1] DR CTD; 910; -. DR GeneCards; CD1B; -. DR HGNC; HGNC:1635; CD1B. DR HPA; HPA021824; -. DR MIM; 188360; gene. DR neXtProt; NX_P29016; -. DR PharmGKB; PA26194; -. DR eggNOG; ENOG410JACG; Eukaryota. DR eggNOG; ENOG41113WA; LUCA. DR GeneTree; ENSGT00480000042665; -. DR HOGENOM; HOG000111666; -. DR HOVERGEN; HBG004453; -. DR InParanoid; P29016; -. DR KO; K06448; -. DR OMA; WAQTQGS; -. DR PhylomeDB; P29016; -. DR TreeFam; TF336723; -. DR EvolutionaryTrace; P29016; -. DR GenomeRNAi; 910; -. DR NextBio; 3754; -. DR PRO; PR:P29016; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; P29016; -. DR CleanEx; HS_CD1B; -. DR ExpressionAtlas; P29016; baseline and differential. DR Genevisible; P29016; HS. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0030881; F:beta-2-microglobulin binding; IBA:GO_Central. 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:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; 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; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. 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; Alternative splicing; Cell membrane; KW Complete proteome; Disulfide bond; Endosome; Glycoprotein; Immunity; KW Immunoglobulin domain; Lysosome; Membrane; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 17 {ECO:0000255}. FT CHAIN 18 333 T-cell surface glycoprotein CD1b. FT /FTId=PRO_0000014579. FT TOPO_DOM 18 303 Extracellular. {ECO:0000255}. FT TRANSMEM 304 324 Helical. {ECO:0000255}. FT TOPO_DOM 325 333 Cytoplasmic. {ECO:0000255}. FT DOMAIN 185 295 Ig-like. FT MOTIF 329 332 Internalization signal. FT CARBOHYD 38 38 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16874306}. FT CARBOHYD 75 75 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16874306, FT ECO:0000269|PubMed:19349973}. FT CARBOHYD 146 146 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 258 258 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 120 184 FT DISULFID 149 163 FT DISULFID 224 279 FT VAR_SEQ 242 296 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_016911. FT MUTAGEN 329 330 YQ->AA: Strongly reduced internalization FT and trafficking to endosomes. FT {ECO:0000269|PubMed:10981968}. FT STRAND 27 38 {ECO:0000244|PDB:2H26}. FT STRAND 41 50 {ECO:0000244|PDB:2H26}. FT STRAND 53 59 {ECO:0000244|PDB:2H26}. FT TURN 60 63 {ECO:0000244|PDB:2H26}. FT STRAND 64 67 {ECO:0000244|PDB:2H26}. FT TURN 70 75 {ECO:0000244|PDB:2H26}. FT HELIX 78 102 {ECO:0000244|PDB:2H26}. FT TURN 103 107 {ECO:0000244|PDB:2H26}. FT STRAND 110 122 {ECO:0000244|PDB:2H26}. FT STRAND 128 136 {ECO:0000244|PDB:2H26}. FT STRAND 139 145 {ECO:0000244|PDB:2H26}. FT STRAND 148 151 {ECO:0000244|PDB:2H26}. FT HELIX 153 155 {ECO:0000244|PDB:2H26}. FT HELIX 156 166 {ECO:0000244|PDB:2H26}. FT HELIX 170 181 {ECO:0000244|PDB:2H26}. FT HELIX 183 194 {ECO:0000244|PDB:2H26}. FT HELIX 196 199 {ECO:0000244|PDB:2H26}. FT STRAND 206 213 {ECO:0000244|PDB:2H26}. FT STRAND 219 232 {ECO:0000244|PDB:2H26}. FT STRAND 234 240 {ECO:0000244|PDB:2H26}. FT STRAND 254 256 {ECO:0000244|PDB:3T8X}. FT TURN 257 259 {ECO:0000244|PDB:3T8X}. FT STRAND 261 270 {ECO:0000244|PDB:2H26}. FT HELIX 271 273 {ECO:0000244|PDB:2H26}. FT STRAND 277 283 {ECO:0000244|PDB:2H26}. FT HELIX 284 286 {ECO:0000244|PDB:2H26}. FT STRAND 291 296 {ECO:0000244|PDB:2H26}. SQ SEQUENCE 333 AA; 36939 MW; 7D02B670D4DE8CC7 CRC64; MLLLPFQLLA VLFPGGNSEH AFQGPTSFHV IQTSSFTNST WAQTQGSGWL DDLQIHGWDS DSGTAIFLKP WSKGNFSDKE VAELEEIFRV YIFGFAREVQ DFAGDFQMKY PFEIQGIAGC ELHSGGAIVS FLRGALGGLD FLSVKNASCV PSPEGGSRAQ KFCALIIQYQ GIMETVRILL YETCPRYLLG VLNAGKADLQ RQVKPEAWLS SGPSPGPGRL QLVCHVSGFY PKPVWVMWMR GEQEQQGTQL GDILPNANWT WYLRATLDVA DGEAAGLSCR VKHSSLEGQD IILYWRNPTS IGSIVLAIIV PSLLLLLCLA LWYMRRRSYQ NIP //