Decay-accelerating factor
CD55 molecule, decay accelerating factor for complement (Cromer blood group) |
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PDB rendering based on 1h03. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1H03, 1H04, 1H2P, 1H2Q, 1M11, 1NWV, 1OJV, 1OJW, 1OJY, 1OK1, 1OK2, 1OK3, 1OK9, 1UOT, 1UPN, 2C8I, 2QZD, 2QZF, 2QZH, 3IYP, 3J24
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Identifiers |
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Symbols |
CD55 ; CR; CROM; DAF; TC |
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External IDs |
OMIM: 125240 MGI: 104850 HomoloGene: 479 GeneCards: CD55 Gene |
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RNA expression pattern |
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More reference expression data |
Orthologs |
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Species |
Human |
Mouse |
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Entrez |
1604 |
13136 |
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Ensembl |
ENSG00000196352 |
ENSMUSG00000026399 |
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UniProt |
P08174 |
Q61475 |
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RefSeq (mRNA) |
NM_000574 |
NM_010016 |
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RefSeq (protein) |
NP_000565 |
NP_034146 |
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Location (UCSC) |
Chr 1: 207.32 – 207.36 Mb |
Chr 1: 130.44 – 130.46 Mb |
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PubMed search |
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Complement decay-accelerating factor, also known as CD55 or DAF, is a protein that, in humans, is encoded by the CD55 gene.[1]
Decay accelerating factor is a 70 kDa membrane protein that regulates the complement system on the cell surface. DAF recognizes C4b and C3b fragments that are created during C4 (classical complement pathway and lectin pathway) and C3 (alternate complement pathway) activation. Interaction of DAF with cell-associated C4b of the classical and lectin pathways interferes with the conversion of C2 to C2a, thereby preventing formation of the C4b2a C3 convertase, and interaction of DAF with C3b of the alternative pathway interferes with the conversion of factor B to Bb by factor D, thereby preventing formation of the C3bBb C3 convertase of the alternative pathway. Thus, by limiting the amplification convertases of the complement
cascade, DAF indirectly blocks the formation of the membrane attack complex.[2]
This glycoprotein is broadly distributed among hematopoietic and non-hematopoietic cells. It is a determinant for the Cromer blood group system.
Pathology
Paroxysmal nocturnal hemoglobinuria
Because DAF is a GPI-anchored protein, its expression is reduced in persons with mutations that reduce GPI levels such as those with paroxysmal nocturnal hemoglobinuria; in that disorder, red blood cells with very low levels of DAF and CD59 undergo complement-mediated hemolysis.[3]
Infectious diseases
DAF is used as a receptor by some coxsackieviruses and other enteroviruses.[4] Recombinant soluble DAF-Fc has been tested in mice as an anti-enterovirus therapy for heart damage;[5] however, the human enterovirus that was tested binds much more strongly to human DAF than to mouse or rat DAF. Echoviruses and coxsackie B viruses that use human decay-accelerating factor (DAF) as a receptor do not bind the rodent analogues of DAF.[6] and DAF-Fc has yet to be tested in humans.
See also
References
- ↑ Medof ME, Lublin DM, Holers VM, Ayers DJ, Getty RR, Leykam JF, Atkinson JP, Tykocinski ML (April 1987). "Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement". Proc. Natl. Acad. Sci. U.S.A. 84 (7): 2007–11. doi:10.1073/pnas.84.7.2007. PMC 304572. PMID 2436222.
- ↑ http://www.genecards.org/cgi-bin/carddisp.pl?gene=CD55#function.
- ↑ Parker C, Omine M, Richards S, et al. (2005). "Diagnosis and management of paroxysmal nocturnal hemoglobinuria". Blood 106 (12): 3699–709. doi:10.1182/blood-2005-04-1717. PMC 1895106. PMID 16051736.
- ↑ Karnauchow TM, Tolson DL, Harrison BA, Altman E, Lublin DM, Dimock K (August 1996). "The HeLa cell receptor for enterovirus 70 is decay-accelerating factor (CD55)". J. Virol. 70 (8): 5143–52. PMC 190469. PMID 8764022.
- ↑ Yanagawa B, Spiller OB, Choy J, Luo H, Cheung P, Zhang HM, Goodfellow IG, Evans DJ, Suarez A, Yang D, McManus BM (January 2003). "Coxsackievirus B3-associated myocardial pathology and viral load reduced by recombinant soluble human decay-accelerating factor in mice". Lab. Invest. 83 (1): 75–85. doi:10.1097/01.lab.0000049349.56211.09. PMID 12533688.
- ↑ Spiller OB, Goodfellow IG, Evans DJ, Almond JW, Morgan BP (January 2000). "Echoviruses and coxsackie B viruses that use human decay-accelerating factor (DAF) as a receptor do not bind the rodent analogues of DAF". J. Infect. Dis. 181 (1): 340–3. doi:10.1086/315210. PMID 10608785.
Further reading
- Selinka HC, Wolde A, Sauter M, et al. (2004). "Virus-receptor interactions of coxsackie B viruses and their putative influence on cardiotropism.". Med. Microbiol. Immunol. 193 (2-3): 127–31. doi:10.1007/s00430-003-0193-y. PMID 12920584.
- Mikesch JH, Schier K, Roetger A, et al. (2007). "The expression and action of decay-accelerating factor (CD55) in human malignancies and cancer therapy.". Cell. Oncol. 28 (5-6): 223–32. PMID 17167176.
External links
PDB gallery |
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| | 1h03: HUMAN CD55 DOMAINS 3 & 4 |
| 1h04: HUMAN CD55 DOMAINS 3 & 4 |
| 1h2p: HUMAN CD55 DOMAINS 3 & 4 |
| 1h2q: HUMAN CD55 DOMAINS 3 & 4 |
| 1nwv: SOLUTION STRUCTURE OF A FUNCTIONALLY ACTIVE COMPONENT OF DECAY ACCELERATING FACTOR |
| 1ojv: DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR. |
| 1ojw: DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR. |
| 1ojy: DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR. |
| 1ok1: DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR. |
| 1ok2: DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR. |
| 1ok3: DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR. |
| 1ok9: DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR. |
| 1uot: HUMAN CD55 DOMAINS 3 & 4 |
| 1upn: COMPLEX OF ECHOVIRUS TYPE 12 WITH DOMAINS 3 AND 4 OF ITS RECEPTOR DECAY ACCELERATING FACTOR (CD55) BY CRYO ELECTRON MICROSCOPY AT 16 A |
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