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CD205; lymphocyte antigen 75; DEC-205; gp200-MR6 (LY75)
Function:
- antigen endocytic receptor
- directs movement from the extracellular space to specialized antigen processing compartment
- decreases B cell proliferation
Structure:
- N-glycosylated
- contains 10 C-type lectin domains
- contains 1 fibronectin F2 module
- contains 1 ricin B-type lectin domain
Compartment: membrane
Alternative splicing: named isoforms=4 Produced by intergenic splicing of LY75 & CD302
Expression:
- expressed in spleen, thymus, colon & peripheral blood lymphocytes
- detected in myeloid & B lymphoid cell lines
Pathology:
- isoforms 2 & 3 are expressed in Reed-sternberg cells of Hodgkin's lymphoma by a transcriptional control mechanism which cotranscribed an mRNA containing LY75 & CD302 prior to generating the intergenically spliced mRNA to produce LY75/CD302 fusion proteins
General
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
glycoprotein
phosphoprotein
receptor
Properties
SIZE: entity length = 1722 aa
MW = 198 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-27}
Ricin B-type lectin {33-156}
MOTIF: N-glycosylation site {N135}
fibronectin type II domain or F2 module
SITE: 164-211
FOR-BINDING-OF: collagen
MOTIF: cysteine residue {*1}
MODIFICATION: cysteine residue {*3}
cysteine residue {*2}
MODIFICATION: cysteine residue {*4}
cysteine residue {*3}
MODIFICATION: cysteine residue {*1}
cysteine residue {*4}
MODIFICATION: cysteine residue {*2}
cysteine residue {C169}
MODIFICATION: cysteine residue {C194}
cysteine residue {C183}
MODIFICATION: cysteine residue {C209}
cysteine residue {C194}
MODIFICATION: cysteine residue {C169}
cysteine residue {C209}
MODIFICATION: cysteine residue {C183}
C-type lectin 1 {225-341}
MOTIF: cysteine residue {C247}
MODIFICATION: cysteine residue {C340}
cysteine residue {C317}
MODIFICATION: cysteine residue {C332}
cysteine residue {C332}
MODIFICATION: cysteine residue {C317}
cysteine residue {C340}
MODIFICATION: cysteine residue {C247}
N-glycosylation site {N345}
C-type lectin 2 {368-486}
MOTIF: N-glycosylation site {N377}
cysteine residue {C389}
MODIFICATION: cysteine residue {C485}
cysteine residue {C462}
MODIFICATION: cysteine residue {C477}
cysteine residue {C477}
MODIFICATION: cysteine residue {C462}
cysteine residue {C485}
MODIFICATION: cysteine residue {C389}
C-type lectin 3 {493-625}
MOTIF: N-glycosylation site {N529}
cysteine residue {C597}
MODIFICATION: cysteine residue {C614}
cysteine residue {C614}
MODIFICATION: cysteine residue {C597}
C-type lectin 4 {652-778}
C-type lectin 5 {818-931}
MOTIF: cysteine residue {C840}
MODIFICATION: cysteine residue {C930}
N-glycosylation site {N843}
N-glycosylation site {N865}
cysteine residue {C904}
MODIFICATION: cysteine residue {C922}
cysteine residue {C922}
MODIFICATION: cysteine residue {C904}
cysteine residue {C930}
MODIFICATION: cysteine residue {C840}
N-glycosylation site {N934}
C-type lectin 6 {958-1091}
MOTIF: cysteine residue {C1060}
MODIFICATION: cysteine residue {C1080}
N-glycosylation site {N1076}
cysteine residue {C1080}
MODIFICATION: cysteine residue {C1060}
N-glycosylation site {N1103}
C-type lectin 7 {1110-1222}
MOTIF: cysteine residue {C1197}
MODIFICATION: cysteine residue {C1211}
cysteine residue {C1211}
MODIFICATION: cysteine residue {C1197}
N-glycosylation site {N1225}
C-type lectin 8 {1251-1374}
MOTIF: N-glycosylation site {N1320}
N-glycosylation site {N1392}
C-type lectin 9 {1401-1513}
MOTIF: cysteine residue {C1488}
MODIFICATION: cysteine residue {C1502}
cysteine residue {C1502}
MODIFICATION: cysteine residue {C1488}
C-type lectin 10 {1542-1661}
MOTIF: N-glycosylation site {N1593}
N-glycosylation site {N1626}
cysteine residue {C1635}
MODIFICATION: cysteine residue {C1650}
cysteine residue {C1650}
MODIFICATION: cysteine residue {C1635}
transmembrane domain {1667-1691}
Ser phosphorylation site {S1703}
Database Correlations
OMIM 604524
UniProt O60449
PFAM correlations
Entrez Gene 4065
Kegg hsa:4065
References
- UniProt :accession O60449
- http://www.pathologyoutlines.com/cd100247.html
21 June 2005
- Functional glycomics gateway - glycan binding Note: DEC-205
http://www.functionalglycomics.org/glycomics/GBPServlet?&operationtype=view&cbpId=cbp_hum_Ctlect_250