CD276 (costimulatory molecule, B7 homolog 3, B7-H3, 4Ig-B7-H3, B7H3, PSEC0249, UNQ309/PRO352)

Function: 1) regulation of T-cell-mediated immune response (putative) 2) inhibits natural-killer mediated cell lysis 3) role in acute & chronic transplant rejection 4) regulation of lymphocytic activity at mucosal surfaces 5) role in placental & fetal immunity Structure: 1) belongs to the immunoglobulin superfamily, BTN/MOG family 2) contains 2 Ig-like C2-type domains (immunoglobulin-like) - contains 2 Ig-like V-type domains (immunoglobulin-like) Compartment: membrane Alternative splicing: named isoforms=4 Expression: - not detected in peripheral blood lymphocytes or granulocytes - weakly expressed in resting monocytes - expressed in dentritic cells derived from monocytes - expressed in epithelial cells of sinonasal tissue - expressed in extravillous trophoblast cells & Hofbauer cells 1st trimester & term placenta - induced by LPS in monocytes & by ionomycin in T-cells & B-cells Pathology: - marker for detection of neuroblastoma cells

General

cluster-of-differentiation antigen; cluster designation antigen; CD antigen glycoprotein immunoglobulin superfamily protein

Properties

SIZE: MW = 57 kD entity length = 534 aa COMPARTMENT: plasma membrane MOTIF: signal sequence {1-28} immunoglobulin superfamily domain {29-139} MOTIF: cysteine residue {C50} MODIFICATION: cysteine residue {C122} N-glycosylation site {N104} cysteine residue {C122} MODIFICATION: cysteine residue {C50} immunoglobulin superfamily domain {145-238} MOTIF: cysteine residue {C165} MODIFICATION: cysteine residue {C220} N-glycosylation site {N189} N-glycosylation site {N215} cysteine residue {C220} MODIFICATION: cysteine residue {C165} immunoglobulin superfamily domain {243-357} MOTIF: cysteine residue {C268} MODIFICATION: cysteine residue {C340} cysteine residue {C340} MODIFICATION: cysteine residue {C268} immunoglobulin superfamily domain {363-456} MOTIF: cysteine residue {C383} MODIFICATION: cysteine residue {C438} N-glycosylation site {N407} cysteine residue {C438} MODIFICATION: cysteine residue {C383} transmembrane domain {467-487}

Database Correlations

OMIM 605715 UniProt Q5ZPR3 PFAM correlations

References

UniProt :accession Q5ZPR3