NATIVE HUMAN C4c

C4c

Phosphate buffered saline

C4 plays a central role in the activation of the classical pathway of the complement system. It is processed by activated C1 which removes from the alpha chain the C4a anaphylatoxin. The remaining alpha chain fragment C4b is the major activation product and is an essential subunit of the C3 convertase (C4b2a) and the C5 convertase (C3bC4b2a) enzymes of the classical complement pathway. Derived from proteolytic degradation of complement C4 C4a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. Subunit structureCirculates in blood as a disulfide-linked trimer of an alpha beta and gamma chain. Subcellular locationSecreted. Post-translational modificationPrior to secretion the single-chain precursor is enzymatically cleaved to yield the non-identical chains (alpha beta and gamma). During activation the alpha chain is cleaved by C1 into C4a and C4b and C4b stays linked to the beta and gamma chains. Further degradation of C4b by C1 into the inactive fragments C4c and C4d blocks the generation of C3 convertase.

C4A allotypes react more rapidly with the amino group of peptide antigens while C4B allotypes react more rapidly with the hydroxyl group of carbohydrate antigens. Sequence similaritiesContains 1 anaphylatoxin-like domain. Contains 1 NTR domain. Sequence cautionThe sequence AAA99717. 1 differs from that shown. Reason: Erroneous gene model prediction. 1. Rosendahl. M. S. et al. (1997) Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases. J. Biol. Chem. 272: 24588-24593. [1] \" Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases. \" Rosendahl M. S. Ko S. C. Long D. L. Brewer M. T. Rosenzweig B. Hedl E. Anderson L. Pyle S. M. Moreland J. Meyers M. A. Kohno T. Lyons D. Lichenstein H. S. J. Biol. Chem. 272:24588-24593(1997) [PubMed: 9305925] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] PROTEIN SEQUENCE OF 216-237. [2] \" Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. \" Howard L. Mitchell S. Lu X. Griffiths S. Glynn P. Biochem. J. 317:45-50(1996) [PubMed: 8694785] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-748. [3] \" Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes. \" McKie N. Edwards T. Dallas D. J. Houghton A. Stringer B. Graham R. Russell G. Croucher P. I. Biochem. Biophys. Res. Commun. 230:335-339(1997) [PubMed: 9016778] [Abstract]Cited for: TISSUE SPECIFICITY. [4] \" ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles. \" Gutwein P. Mechtersheimer S. Riedle S. Stoeck A. Gast D. Joumaa S. Zentgraf H. Fogel M. Altevogt P. FASEB J. 17:292-294(2003) [PubMed: 12475894] [Abstract]Cited for: FUNCTION. [5] \" The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. \" Vincent B. Paitel E. Saftig P. Frobert Y. Hartmann D. De Strooper B. Grassi J. Lopez-Perez E. Checler F. J. Biol. Chem. 276:37743-37746(2001) [PubMed: 11477090] [Abstract]Cited for: FUNCTION. [6] \" ADAM-10 protein is present in human articular cartilage primarily in the membrane-bound form and is upregulated in osteoarthritis and in response to IL-1alpha in bovine nasal cartilage. \" Chubinskaya S. Mikhail R. Deutsch A. Tindal M. H. J. Histochem. Cytochem. 49:1165-1176(2001) [PubMed: 11511685] [Abstract]Cited for: TISSUE SPECIFICITY. [7] \" Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells. \" Lemjabbar H. Basbaum C. Nat. Med. 8:41-46(2002) [PubMed: 11786905] [Abstract]Cited for: FUNCTION. [8] \" Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. \" Lewandrowski U. Moebius J. Walter U. Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed: 16263699] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278 MASS SPECTROMETRY. Tissue: Platelet. [9] \" Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. \" Chen R. Jiang X. Sun D. Han G. Wang F. Ye M. Wang L. Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278 MASS SPECTROMETRY. Tissue: Liver. [10] \" Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. \" Wollscheid B. Bausch-Fluck D. Henderson C. O\' Brien R. Bibel M. Schiess R. Aebersold R. Watts J. D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278 MASS SPECTROMETRY. Tissue: Leukemic T-cell.