CD1D_HUMAN
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 03-AUG-2022, entry version 206.
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}.
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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.ENSP00000357153; -.
DR ChEMBL; CHEMBL1649053; -.
DR DrugBank; DB04661; cis-tetracosenoyl sulfatide.
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; P15813; -.
DR PeptideAtlas; P15813; -.
DR PRIDE; P15813; -.
DR ProteomicsDB; 53222; -.
DR Antibodypedia; 4236; 546 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 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; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_9_2_1; -.
DR InParanoid; P15813; -.
DR OMA; NDICPQF; -.
DR OrthoDB; 827472at2759; -.
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; 25 hits in 1069 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 104 other tissues.
DR ExpressionAtlas; P15813; baseline and differential.
DR Genevisible; P15813; HS.
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:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
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:Reactome.
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: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 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; 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
