ID   CD83_HUMAN              Reviewed;         205 AA.
AC   Q01151; Q5THX9;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   24-JAN-2024, entry version 200.
DE   RecName: Full=CD83 antigen;
DE            Short=hCD83;
DE   AltName: Full=B-cell activation protein;
DE   AltName: Full=Cell surface protein HB15;
DE   AltName: CD_antigen=CD83;
DE   Flags: Precursor;
GN   Name=CD83;
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].
RC   TISSUE=Tonsil;
RX   PubMed=1378080;
RA   Zhou L.-J., Schwarting R., Smith H.M., Tedder T.F.;
RT   "A novel cell-surface molecule expressed by human interdigitating reticulum
RT   cells, Langerhans cells, and activated lymphocytes is a new member of the
RT   Ig superfamily.";
RL   J. Immunol. 149:735-742(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=B-cell;
RX   PubMed=8422464;
RA   Kozlow E.J., Wilson G.L., Fox C.H., Kehrl J.H.;
RT   "Subtractive cDNA cloning of a novel member of the Ig gene superfamily
RT   expressed at high levels in activated B lymphocytes.";
RL   Blood 81:454-461(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   PROTEIN SEQUENCE OF 20-34.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79.
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).
CC   -!- FUNCTION: May play a significant role in antigen presentation or the
CC       cellular interactions that follow lymphocyte activation.
CC   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       Q01151; Q969F0: FATE1; NbExp=3; IntAct=EBI-2873723, EBI-743099;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed by activated lymphocytes, Langerhans
CC       cells and interdigitating reticulum cells.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=CD83 antigen;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Other_00148";
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DR   EMBL; Z11697; CAA77755.1; -; mRNA.
DR   EMBL; S53354; AAB25085.1; -; mRNA.
DR   EMBL; CR457019; CAG33300.1; -; mRNA.
DR   EMBL; AL133259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL022396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC030830; AAH30830.1; -; mRNA.
DR   CCDS; CCDS4532.1; -.
DR   PIR; A48929; A48929.
DR   RefSeq; NP_001035370.1; NM_001040280.1.
DR   RefSeq; NP_001238830.1; NM_001251901.1.
DR   RefSeq; NP_004224.1; NM_004233.3.
DR   PDB; 5MIX; X-ray; 1.70 A; A=20-131.
DR   PDB; 5MJ0; X-ray; 3.20 A; A/B=20-131.
DR   PDB; 5MJ1; X-ray; 1.80 A; A=20-131.
DR   PDB; 5MJ2; X-ray; 1.98 A; A=20-131.
DR   PDBsum; 5MIX; -.
DR   PDBsum; 5MJ0; -.
DR   PDBsum; 5MJ1; -.
DR   PDBsum; 5MJ2; -.
DR   AlphaFoldDB; Q01151; -.
DR   SMR; Q01151; -.
DR   BioGRID; 114721; 70.
DR   IntAct; Q01151; 45.
DR   STRING; 9606.ENSP00000368450; -.
DR   UniLectin; Q01151; -.
DR   GlyCosmos; Q01151; 3 sites, No reported glycans.
DR   GlyGen; Q01151; 3 sites.
DR   iPTMnet; Q01151; -.
DR   PhosphoSitePlus; Q01151; -.
DR   SwissPalm; Q01151; -.
DR   BioMuta; CD83; -.
DR   DMDM; 232223; -.
DR   jPOST; Q01151; -.
DR   MassIVE; Q01151; -.
DR   MaxQB; Q01151; -.
DR   PaxDb; 9606-ENSP00000368450; -.
DR   PeptideAtlas; Q01151; -.
DR   ProteomicsDB; 57923; -.
DR   Pumba; Q01151; -.
DR   ABCD; Q01151; 22 sequenced antibodies.
DR   Antibodypedia; 3744; 1102 antibodies from 42 providers.
DR   DNASU; 9308; -.
DR   Ensembl; ENST00000379153.4; ENSP00000368450.3; ENSG00000112149.10.
DR   GeneID; 9308; -.
DR   KEGG; hsa:9308; -.
DR   MANE-Select; ENST00000379153.4; ENSP00000368450.3; NM_004233.4; NP_004224.1.
DR   UCSC; uc003nbi.4; human.
DR   AGR; HGNC:1703; -.
DR   CTD; 9308; -.
DR   DisGeNET; 9308; -.
DR   GeneCards; CD83; -.
DR   HGNC; HGNC:1703; CD83.
DR   HPA; ENSG00000112149; Tissue enhanced (bone).
DR   MIM; 604534; gene.
DR   neXtProt; NX_Q01151; -.
DR   OpenTargets; ENSG00000112149; -.
DR   PharmGKB; PA26241; -.
DR   VEuPathDB; HostDB:ENSG00000112149; -.
DR   eggNOG; ENOG502S7FP; Eukaryota.
DR   GeneTree; ENSGT00390000007302; -.
DR   HOGENOM; CLU_099481_0_0_1; -.
DR   InParanoid; Q01151; -.
DR   OMA; SKPGMER; -.
DR   OrthoDB; 4309716at2759; -.
DR   PhylomeDB; Q01151; -.
DR   TreeFam; TF337861; -.
DR   PathwayCommons; Q01151; -.
DR   SignaLink; Q01151; -.
DR   SIGNOR; Q01151; -.
DR   BioGRID-ORCS; 9308; 12 hits in 1155 CRISPR screens.
DR   ChiTaRS; CD83; human.
DR   GeneWiki; CD83; -.
DR   GenomeRNAi; 9308; -.
DR   Pharos; Q01151; Tbio.
DR   PRO; PR:Q01151; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q01151; Protein.
DR   Bgee; ENSG00000112149; Expressed in adrenal tissue and 192 other cell types or tissues.
DR   ExpressionAtlas; Q01151; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR   GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IEA:Ensembl.
DR   GO; GO:0006952; P:defense response; TAS:ProtInc.
DR   GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR   GO; GO:0032713; P:negative regulation of interleukin-4 production; IEA:Ensembl.
DR   GO; GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; IEA:Ensembl.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   PANTHER; PTHR15193; CD83 ANTIGEN; 1.
DR   PANTHER; PTHR15193:SF1; CD83 ANTIGEN; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   Genevisible; Q01151; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           20..205
FT                   /note="CD83 antigen"
FT                   /id="PRO_0000014657"
FT   TOPO_DOM        20..144
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..205
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          20..114
FT                   /note="Ig-like V-type"
FT   REGION          60..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VARIANT         182
FT                   /note="R -> Q (in dbSNP:rs2230193)"
FT                   /id="VAR_033609"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:5MIX"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:5MIX"
FT   STRAND          46..52
FT                   /evidence="ECO:0007829|PDB:5MIX"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:5MIX"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:5MIX"
FT   STRAND          103..110
FT                   /evidence="ECO:0007829|PDB:5MIX"
FT   STRAND          112..115
FT                   /evidence="ECO:0007829|PDB:5MJ0"
FT   STRAND          117..126
FT                   /evidence="ECO:0007829|PDB:5MIX"
SQ   SEQUENCE   205 AA;  23042 MW;  1D77133595F2B852 CRC64;
     MSRGLQLLLL SCAYSLAPAT PEVKVACSED VDLPCTAPWD PQVPYTVSWV KLLEGGEERM
     ETPQEDHLRG QHYHQKGQNG SFDAPNERPY SLKIRNTTSC NSGTYRCTLQ DPDGQRNLSG
     KVILRVTGCP AQRKEETFKK YRAEIVLLLA LVIFYLTLII FTCKFARLQS IFPDFSKAGM
     ERAFLPVTSP NKHLGLVTPH KTELV
//