ID CD1D_HUMAN Reviewed; 335 AA. AC P15813; D3DVD5; Q5W0J3; Q9UMM3; Q9Y5M4; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 24-JAN-2024, entry version 214. DE RecName: Full=Antigen-presenting glycoprotein CD1d; DE AltName: Full=R3G1; DE AltName: CD_antigen=CD1d; DE Flags: Precursor; GN Name=CD1D; 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 [GENOMIC DNA]. RX PubMed=2467814; DOI=10.1002/eji.1830190211; RA Calabi F., Jarvis J.M., Martin L., Milstein C.; RT "Two classes of CD1 genes."; RL Eur. J. Immunol. 19:285-292(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=2463622; DOI=10.1073/pnas.86.1.252; RA Balk S.P., Bleicher P.A., Terhorst C.; RT "Isolation and characterization of a cDNA and gene coding for a fourth CD1 RT molecule."; RL Proc. Natl. Acad. Sci. U.S.A. 86:252-256(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., 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-109, AND VARIANT SER-64. 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 [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 [8] RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF TYR-331 AND VAL-334. RX PubMed=9973405; RA Rodionov D.G., Nordeng T.W., Pedersen K., Balk S.P., Bakke O.; RT "A critical tyrosine residue in the cytoplasmic tail is important for CD1d RT internalization but not for its basolateral sorting in MDCK cells."; RL J. Immunol. 162:1488-1495(1999). RN [9] RP SUBCELLULAR LOCATION, AND INTERACTION WITH B2M AND MHC II. RX PubMed=11927549; DOI=10.1093/emboj/21.7.1650; RA Kang S.-J., Cresswell P.; RT "Regulation of intracellular trafficking of human CD1d by association with RT MHC class II molecules."; RL EMBO J. 21:1650-1660(2002). RN [10] RP REVIEW. RX PubMed=16818729; DOI=10.4049/jimmunol.177.2.769; RA Brutkiewicz R.R.; RT "CD1d ligands: the good, the bad, and the ugly."; RL J. Immunol. 177:769-775(2006). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17475845; DOI=10.4049/jimmunol.178.10.6181; RA Chen X., Wang X., Keaton J.M., Reddington F., Illarionov P.A., Besra G.S., RA Gumperz J.E.; RT "Distinct endosomal trafficking requirements for presentation of RT autoantigens and exogenous lipids by human CD1d molecules."; RL J. Immunol. 178:6181-6190(2007). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-60. 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-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [13] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-299 IN COMPLEX WITH B2M AND RP GALACTOSYLCERAMIDE, AND DISULFIDE BONDS. RX PubMed=16007090; DOI=10.1038/ni1225; RA Koch M., Stronge V.S., Shepherd D., Gadola S.D., Mathew B., Ritter G., RA Fersht A.R., Besra G.S., Schmidt R.R., Jones E.Y., Cerundolo V.; RT "The crystal structure of human CD1d with and without alpha- RT galactosylceramide."; RL Nat. Immunol. 6:819-826(2005). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 24-295 IN COMPLEX WITH B2M AND RP T-CELL RECEPTOR, AND GLYCOSYLATION AT ASN-38 AND ASN-60. RX PubMed=17581592; DOI=10.1038/nature05907; RA Borg N.A., Wun K.S., Kjer-Nielsen L., Wilce M.C.J., Pellicci D.G., Koh R., RA Besra G.S., Bharadwaj M., Godfrey D.I., McCluskey J., Rossjohn J.; RT "CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell RT receptor."; RL Nature 448:44-49(2007). CC -!- FUNCTION: Antigen-presenting protein that binds self and non-self CC glycolipids and presents them to T-cell receptors on natural killer T- CC cells. {ECO:0000269|PubMed:17475845}. CC -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with CC MHC II. {ECO:0000269|PubMed:11927549, ECO:0000269|PubMed:16007090, CC ECO:0000269|PubMed:17581592}. CC -!- INTERACTION: CC P15813; Q12959: DLG1; NbExp=2; IntAct=EBI-15643544, EBI-357481; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11927549, CC ECO:0000269|PubMed:17475845, ECO:0000269|PubMed:9973405}; Single-pass CC type I membrane protein {ECO:0000305|PubMed:9973405}. Basolateral cell CC membrane {ECO:0000269|PubMed:9973405}; Single-pass type I membrane CC protein {ECO:0000305|PubMed:9973405}. Endosome membrane CC {ECO:0000269|PubMed:11927549, ECO:0000269|PubMed:9973405}; Single-pass CC type I membrane protein {ECO:0000305|PubMed:9973405}. Lysosome membrane CC {ECO:0000269|PubMed:17475845, ECO:0000269|PubMed:9973405}; Single-pass CC type I membrane protein {ECO:0000269|PubMed:9973405}. Endoplasmic CC reticulum membrane {ECO:0000269|PubMed:11927549}; Single-pass type I CC membrane protein {ECO:0000269|PubMed:11927549}. Note=Subject to CC intracellular trafficking between the cell membrane, endosomes and CC lysosomes. {ECO:0000269|PubMed:9973405}. CC -!- TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain T-cell CC 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 glycolipid CC antigens when the proteins are internalized and pass through endosomes, CC before trafficking back to the cell surface. {ECO:0000250}. 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; L38820; AAA59672.1; -; Genomic_DNA. DR EMBL; L38815; AAA59672.1; JOINED; Genomic_DNA. DR EMBL; L38817; AAA59672.1; JOINED; Genomic_DNA. DR EMBL; L38816; AAA59672.1; JOINED; Genomic_DNA. DR EMBL; L38818; AAA59672.1; JOINED; Genomic_DNA. DR EMBL; L38819; AAA59672.1; JOINED; Genomic_DNA. DR EMBL; X14974; CAA33099.1; -; Genomic_DNA. DR EMBL; J04142; AAA59673.1; -; mRNA. DR EMBL; AL138899; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW52847.1; -; Genomic_DNA. DR EMBL; CH471121; EAW52848.1; -; Genomic_DNA. DR EMBL; CH471121; EAW52849.1; -; Genomic_DNA. DR EMBL; BC027926; AAH27926.1; -; mRNA. DR EMBL; AF142668; AAD37581.1; -; Genomic_DNA. DR EMBL; M14664; AAA51935.1; -; Genomic_DNA. DR CCDS; CCDS1173.1; -. DR PIR; S07715; HLHUR3. DR RefSeq; NP_001306074.1; NM_001319145.1. DR RefSeq; NP_001757.1; NM_001766.3. DR RefSeq; XP_011508427.1; XM_011510125.1. DR PDB; 1ZT4; X-ray; 3.00 A; A/C=19-299. DR PDB; 2PO6; X-ray; 3.20 A; A/E=24-295. DR PDB; 3HUJ; X-ray; 2.50 A; A/C=21-295. DR PDB; 3SDX; X-ray; 3.12 A; A/C=24-295. DR PDB; 3TZV; X-ray; 3.06 A; C=21-295. DR PDB; 3U0P; X-ray; 2.80 A; A/C/E=21-295. DR PDB; 3VWJ; X-ray; 3.09 A; A=21-295. DR PDB; 3VWK; X-ray; 2.94 A; A=21-295. DR PDB; 4EN3; X-ray; 2.57 A; C=21-295. DR PDB; 4LHU; X-ray; 2.87 A; A=24-295. DR PDB; 4MNG; X-ray; 3.01 A; A/C=21-201. DR PDB; 4MQ7; X-ray; 2.60 A; A=21-202. DR PDB; 4WO4; X-ray; 2.50 A; A=24-295. DR PDB; 4WW2; X-ray; 2.48 A; C=21-295. DR PDB; 4WWK; X-ray; 3.10 A; C=21-295. DR PDB; 6V7Y; X-ray; 2.40 A; A=23-296. DR PDB; 6V7Z; X-ray; 2.75 A; A/C=23-296. DR PDB; 6V80; X-ray; 3.53 A; A/F=23-296. DR PDBsum; 1ZT4; -. DR PDBsum; 2PO6; -. DR PDBsum; 3HUJ; -. DR PDBsum; 3SDX; -. DR PDBsum; 3TZV; -. DR PDBsum; 3U0P; -. DR PDBsum; 3VWJ; -. DR PDBsum; 3VWK; -. DR PDBsum; 4EN3; -. DR PDBsum; 4LHU; -. DR PDBsum; 4MNG; -. DR PDBsum; 4MQ7; -. DR PDBsum; 4WO4; -. DR PDBsum; 4WW2; -. DR PDBsum; 4WWK; -. DR PDBsum; 6V7Y; -. DR PDBsum; 6V7Z; -. DR PDBsum; 6V80; -. DR AlphaFoldDB; P15813; -. DR SMR; P15813; -. DR BioGRID; 107350; 6. DR DIP; DIP-60257N; -. DR IntAct; P15813; 2. DR STRING; 9606.ENSP00000501245; -. DR ChEMBL; CHEMBL1649053; -. DR DrugBank; DB04661; cis-tetracosenoyl sulfatide. DR GlyCosmos; P15813; 4 sites, No reported glycans. DR GlyGen; P15813; 4 sites. DR iPTMnet; P15813; -. DR PhosphoSitePlus; P15813; -. DR BioMuta; CD1D; -. DR DMDM; 115964; -. DR MassIVE; P15813; -. DR MaxQB; P15813; -. DR PaxDb; 9606-ENSP00000357153; -. DR PeptideAtlas; P15813; -. DR ProteomicsDB; 53222; -. DR Antibodypedia; 4236; 605 antibodies from 39 providers. DR DNASU; 912; -. DR Ensembl; ENST00000368171.5; ENSP00000357153.3; ENSG00000158473.8. DR Ensembl; ENST00000673723.4; ENSP00000501245.3; ENSG00000158473.8. DR Ensembl; ENST00000674085.2; ENSP00000501100.1; ENSG00000158473.8. DR GeneID; 912; -. DR KEGG; hsa:912; -. DR MANE-Select; ENST00000674085.2; ENSP00000501100.1; NM_001371762.2; NP_001358691.1. DR UCSC; uc001frr.4; human. DR AGR; HGNC:1637; -. DR CTD; 912; -. DR DisGeNET; 912; -. DR GeneCards; CD1D; -. DR HGNC; HGNC:1637; CD1D. DR HPA; ENSG00000158473; Group enriched (intestine, liver, lymphoid tissue). DR MIM; 188410; gene. DR neXtProt; NX_P15813; -. DR OpenTargets; ENSG00000158473; -. DR PharmGKB; PA26196; -. DR VEuPathDB; HostDB:ENSG00000158473; -. DR eggNOG; ENOG502SJH6; Eukaryota. DR GeneTree; ENSGT01100000263475; -. DR HOGENOM; CLU_047501_9_2_1; -. DR InParanoid; P15813; -. DR OMA; NDICPQF; -. DR OrthoDB; 4632172at2759; -. DR PhylomeDB; P15813; -. DR TreeFam; TF336723; -. DR PathwayCommons; P15813; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR SignaLink; P15813; -. DR BioGRID-ORCS; 912; 27 hits in 1149 CRISPR screens. DR EvolutionaryTrace; P15813; -. DR GeneWiki; CD1D; -. DR GenomeRNAi; 912; -. DR Pharos; P15813; Tbio. DR PRO; PR:P15813; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P15813; Protein. DR Bgee; ENSG00000158473; Expressed in monocyte and 105 other cell types or tissues. DR ExpressionAtlas; P15813; baseline and differential. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. 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:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB. DR GO; GO:0030881; F:beta-2-microglobulin binding; TAS:UniProtKB. DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL. DR GO; GO:0030883; F:endogenous lipid antigen binding; IBA:GO_Central. DR GO; GO:0030884; F:exogenous lipid antigen binding; IDA:UniProtKB. DR GO; GO:0042393; F:histone binding; IPI:UniProtKB. DR GO; GO:0030882; F:lipid antigen binding; IDA:UniProtKB. DR GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central. DR GO; GO:0048006; P:antigen processing and presentation, endogenous lipid antigen via MHC class Ib; IDA:UniProtKB. DR GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IBA:GO_Central. DR GO; GO:0016045; P:detection of bacterium; TAS:UniProtKB. DR GO; GO:0034113; P:heterotypic cell-cell adhesion; TAS:BHF-UCL. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0045089; P:positive regulation of innate immune response; TAS:UniProtKB. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:GO_Central. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL. DR GO; GO:0045058; P:T cell selection; TAS:UniProtKB. DR CDD; cd21029; IgC1_CD1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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 PANTHER; PTHR16675:SF175; ANTIGEN-PRESENTING GLYCOPROTEIN CD1D; 1. DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF16497; MHC_I_3; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; P15813; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Disulfide bond; Endoplasmic reticulum; KW Endosome; Glycoprotein; Immunity; Immunoglobulin domain; Innate immunity; KW Lysosome; Membrane; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..335 FT /note="Antigen-presenting glycoprotein CD1d" FT /id="PRO_0000014581" FT TOPO_DOM 20..301 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 302..322 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 323..335 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 185..292 FT /note="Ig-like" FT MOTIF 331..334 FT /note="Internalization signal" FT BINDING 98 FT /ligand="a D-galactosylceramide" FT /ligand_id="ChEBI:CHEBI:36498" FT /evidence="ECO:0000269|PubMed:16007090, FT ECO:0000269|PubMed:17581592, ECO:0007744|PDB:1ZT4, FT ECO:0007744|PDB:2PO6" FT BINDING 169..172 FT /ligand="a D-galactosylceramide" FT /ligand_id="ChEBI:CHEBI:36498" FT /evidence="ECO:0000269|PubMed:16007090, FT ECO:0000269|PubMed:17581592, ECO:0007744|PDB:1ZT4, FT ECO:0007744|PDB:2PO6" FT CARBOHYD 38 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:17581592" FT CARBOHYD 60 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:17581592, FT ECO:0000269|PubMed:19349973" FT CARBOHYD 126 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 181 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 120..184 FT /evidence="ECO:0000269|PubMed:16007090, FT ECO:0000269|PubMed:17581592, ECO:0007744|PDB:1ZT4, FT ECO:0007744|PDB:2PO6" FT DISULFID 224..279 FT /evidence="ECO:0000269|PubMed:16007090, FT ECO:0000269|PubMed:17581592, ECO:0007744|PDB:1ZT4, FT ECO:0007744|PDB:2PO6" FT VARIANT 64 FT /note="T -> S (in dbSNP:rs62621276)" FT /evidence="ECO:0000269|PubMed:10488738" FT /id="VAR_010211" FT MUTAGEN 331 FT /note="Y->A: Strongly reduced internalization." FT /evidence="ECO:0000269|PubMed:9973405" FT MUTAGEN 334 FT /note="V->A: Strongly reduced internalization." FT /evidence="ECO:0000269|PubMed:9973405" FT HELIX 23..25 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 28..40 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 43..50 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 53..58 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 63..67 FT /evidence="ECO:0007829|PDB:3U0P" FT TURN 70..75 FT /evidence="ECO:0007829|PDB:6V7Y" FT HELIX 78..106 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 112..123 FT /evidence="ECO:0007829|PDB:6V7Y" FT TURN 124..126 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 127..136 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 139..145 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:6V7Y" FT HELIX 157..166 FT /evidence="ECO:0007829|PDB:6V7Y" FT HELIX 170..181 FT /evidence="ECO:0007829|PDB:6V7Y" FT HELIX 183..194 FT /evidence="ECO:0007829|PDB:6V7Y" FT HELIX 196..199 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 206..212 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:4LHU" FT STRAND 219..232 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 235..239 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:1ZT4" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:3VWK" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:3VWJ" FT STRAND 261..270 FT /evidence="ECO:0007829|PDB:6V7Y" FT TURN 271..276 FT /evidence="ECO:0007829|PDB:4WW2" FT STRAND 278..282 FT /evidence="ECO:0007829|PDB:6V7Y" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:6V7Y" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:6V7Y" SQ SEQUENCE 335 AA; 37717 MW; EA041C1C45A5777F CRC64; MGCLLFLLLW ALLQAWGSAE VPQRLFPLRC LQISSFANSS WTRTDGLAWL GELQTHSWSN DSDTVRSLKP WSQGTFSDQQ WETLQHIFRV YRSSFTRDVK EFAKMLRLSY PLELQVSAGC EVHPGNASNN FFHVAFQGKD ILSFQGTSWE PTQEAPLWVN LAIQVLNQDK WTRETVQWLL NGTCPQFVSG LLESGKSELK KQVKPKAWLS RGPSPGPGRL LLVCHVSGFY PKPVWVKWMR GEQEQQGTQP GDILPNADET WYLRATLDVV AGEAAGLSCR VKHSSLEGQD IVLYWGGSYT SMGLIALAVL ACLLFLLIVG FTSRFKRQTS YQGVL //