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Reviewed, UniProtKB/Swiss-Prot P08174 (DAF_HUMAN)

Last modified July 22, 2008. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (9) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Complement decay-accelerating factor
Alternative name(s):
    CD_antigen=CD55
Gene names
Name: CD55
Synonyms: CR, DAF
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade.

Subunit structure

Monomer (major form) and non-disulfide-linked, covalent homodimer (minor form). Binds to coxsackievirus A21, coxsackieviruses B1, B3 and B5, human enterovirus 70, human echoviruses 6, 7, 11, 12, 20 and 21 capsid proteins and acts as a receptor for these viruses.

Subcellular location

Isoform 1: Membrane; Single-pass type I membrane protein.

Isoform 2: Cell membrane; Lipid-anchor › GPI-anchor.

Tissue specificity

Expressed on the plasma membranes of all cell types that are in intimate contact with plasma complement proteins. It is also found on the surfaces of epithelial cells lining extracellular compartments, and variants of the molecule are present in body fluids and in extracellular matrix.

Domain

The first Sushi domain (SCR1) is not necessary for function. SCR2 and SCR4 provide the proper conformation for the active site on SCR3 By similarity.

Post-translational modification

The Ser/Thr-rich domain is heavily O-glycosylated.

Polymorphism

Responsible for the Cromer blood group system. It consists of at least 8 high-incidence (Cr(a), Tc(a), Dr(a), Es(a), WES(b), UMC, IFC and GUTI) and three low-incidence (Tc(b), Tc(c) and WES(a)) antigens that reside on DAF. In the Cromer phenotypes Dr(a-) and Inab there is reduced or absent expression of DAF, respectively. In the case of the Dr(a-) phenotype, a single nucleotide substitution within exon 5 accounts for two changes: a simple amino acid substitution, Leu-199 that is the basis of the antigenic variation, and an alternative splicing event that underlies the decreased expression of DAF in this phenotype. The Inab phenotype is a very rare one in which the red blood cells lack all Cromer system antigens. The red blood cells of individuals with Inab phenotype have a deficiency of DAF, but these individuals are not known to have any associated hematologic or other abnormalities.

Sequence similarities

Belongs to the receptors of complement activation (RCA) family.

Contains 4 Sushi (CCP/SCR) domains.

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P08174-1)

Also known as: DAF-2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Notes: GPI-anchored form.
Isoform 1 (identifier: P08174-2)

Also known as: DAF-1;

The sequence of this isoform differs from the canonical sequence as follows:
     362-381: HTCFTLTGLLGTLVTMGLLT → SRPVTQAGMR...TQVYRLFLVS

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 3434
Chain35 – 353319Complement decay-accelerating factor
Propeptide354 – 38128Removed in mature form

Regions

Domain35 – 9662Sushi 1
Domain96 – 16065Sushi 2
Domain161 – 22262Sushi 3
Domain223 – 28563Sushi 4
Compositional bias287 – 35670Ser/Thr-rich

Amino acid modifications

Modified residue1401Phosphoserine
Lipidation3531GPI-anchor amidated serine
Glycosylation951N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 81
Disulfide bond65 ↔ 94
Disulfide bond98 ↔ 145
Disulfide bond129 ↔ 158
Disulfide bond163 ↔ 204
Disulfide bond190 ↔ 220
Disulfide bond225 ↔ 267
Disulfide bond253 ↔ 283

Natural variations

Alternative sequence362 – 38120HTCFT…MGLLT → SRPVTQAGMRWCDRSSLQSR TPGFKRSFHFSLPSSWYYRA HVFHVDRFAWDASNHGLADL AKEELRRKYTQVYRLFLVS in isoform 1.
Natural variant521R → L in Tc(b) antigen. dbSNP rs28371588.
Natural variant521R → P in Tc(c) antigen.
Natural variant821L → R in WES(a) antigen.
Natural variant1991S → L in Dr(a-) antigen.
Natural variant2271A → P in Cr(a-) antigen.
Natural variant2401R → H in GUTI(-) antigen.

Experimental info

Sequence conflict381L → G Ref.7
Sequence conflict801I → T Ref.5 Ref.7
Sequence conflict851S → M in AAA52167. Ref.4
Sequence conflict1871S → T in AAB48622. Ref.5
Sequence conflict2971Q → H in AAB48622. Ref.5

Secondary structure

1 .......................................... 381
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (DAF-2) [UniParc].

Last modified March 1, 2005. Version 4.
Checksum: C1CBE5300F60C176

FASTA38141,400
        10         20         30         40         50         60 
MTVARPSVPA ALPLLGELPR LLLLVLLCLP AVWGDCGLPP DVPNAQPALE GRTSFPEDTV 

        70         80         90        100        110        120 
ITYKCEESFV KIPGEKDSVI CLKGSQWSDI EEFCNRSCEV PTRLNSASLK QPYITQNYFP 

       130        140        150        160        170        180 
VGTVVEYECR PGYRREPSLS PKLTCLQNLK WSTAVEFCKK KSCPNPGEIR NGQIDVPGGI 

       190        200        210        220        230        240 
LFGATISFSC NTGYKLFGST SSFCLISGSS VQWSDPLPEC REIYCPAPPQ IDNGIIQGER 

       250        260        270        280        290        300 
DHYGYRQSVT YACNKGFTMI GEHSIYCTVN NDEGEWSGPP PECRGKSLTS KVPPTVQKPT 

       310        320        330        340        350        360 
TVNVPTTEVS PTSQKTTTKT TTPNAQATRS TPVSRTTKHF HETTPNKGSG TTSGTTRLLS 

       370        380 
GHTCFTLTGL LGTLVTMGLL T

« Hide

Isoform 1 (DAF-1) [UniParc].

Checksum: CF6154031FAC5D58
Show »

44048,717

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References

« Hide 'large scale' references
[1]"Cloning of decay-accelerating factor suggests novel use of splicing to generate two proteins."
Caras I.W., Davitz M.A., Rhee L., Weddell G., Martin D.W. Jr., Nussenzweig V.
Nature 325:545-549(1987) [PubMed: 2433596] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]SeattleSNPs program for genomic applications
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-52.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cervix.
[5]"Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement."
Medof M.E., Lublin D.M., Holers V.M., Ayers D.J., Getty R.R., Leykam J.F., Atkinson J.P., Tykocinski M.L.
Proc. Natl. Acad. Sci. U.S.A. 84:2007-2011(1987) [PubMed: 2436222] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-381 (ISOFORM 2).
[6]"Decay-acceleration factor (DAF; CD 55) in the brain of Alzheimer's disease patients."
Kumar V.B., Hyung C., Nakra R., Walters M., Sasser T., Bernardo A.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 35-381 (ISOFORM 2).
Tissue: Hippocampus.
[7]"Characterization of the decay-accelerating factor gene promoter region."
Ewulonu U.K., Ravi L., Medof M.E.
Proc. Natl. Acad. Sci. U.S.A. 88:4675-4679(1991) [PubMed: 1711208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
[8]"Improved method for the isolation and preliminary characterization of human DAF (decay-accelerating factor)."
Sugita Y., Negoro T., Matsuda T., Sakamoto T., Tomita M.
J. Biochem. 100:143-150(1986) [PubMed: 2428813] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-63.
[9]"Isolation of two forms of decay-accelerating factor (DAF) from human urine."
Nakano Y., Sugita Y., Ishikawa Y., Choi N.-H., Tobe T., Tomita M.
Biochim. Biophys. Acta 1074:326-330(1991) [PubMed: 1712233] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-46.
Tissue: Urine.
[10]"Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site."
Moran P., Raab H., Kohr W.J., Caras I.W.
J. Biol. Chem. 266:1250-1257(1991) [PubMed: 1824699] [Abstract]
Cited for: GPI-ANCHOR AT SER-353.
[11]"Complete determination of disulfide bonds localized within the short consensus repeat units of decay accelerating factor (CD55 antigen)."
Nakano Y., Sumida K., Kikuta N., Miura N.-H., Tobe T., Tomita M.
Biochim. Biophys. Acta 1116:235-240(1992) [PubMed: 1377029] [Abstract]
Cited for: DISULFIDE BONDS IN SUSHI DOMAINS.
[12]"Decay-accelerating factor CD55 is identified as the receptor for echovirus 7 using CELICS, a rapid immuno-focal cloning method."
Ward T., Pipkin P.A., Clarkson N.A., Stone D.M., Minor P.D., Almond J.W.
EMBO J. 13:5070-5074(1994) [PubMed: 7525274] [Abstract]
Cited for: FUNCTION AS A ECHOVIRUS RECEPTOR.
[13]"Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses."
Bergelson J.M., Chan M., Solomon K.R., St John N.F., Lin H., Finberg R.W.
Proc. Natl. Acad. Sci. U.S.A. 91:6245-6248(1994) [PubMed: 7517044] [Abstract]
Cited for: INTERACTION WITH HUMAN ECHOVIRUS 6, HUMAN ECHOVIRUS 7, HUMAN ECHOVIRUS 11, HUMAN ECHOVIRUS 12, HUMAN ECHOVIRUS 20, HUMAN ECHOVIRUS 21 CAPSID PROTEINS.
[14]"Coxsackieviruses B1, B3, and B5 use decay aCCelerating factor as a receptor for cell attachment."
Shafren D.R., Bates R.C., Agrez M.V., Herd R.L., Burns G.F., Barry R.D.
J. Virol. 69:3873-3877(1995) [PubMed: 7538177] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUS B1, B3, B5 CAPSID PROTEINS.
[15]"The HeLa cell receptor for enterovirus 70 is decay-accelerating factor (CD55)."
Karnauchow T.M., Tolson D.L., Harrison B.A., Altman E., Lublin D.M., Dimock K.
J. Virol. 70:5143-5152(1996) [PubMed: 8764022] [Abstract]
Cited for: INTERACTION WITH HUMAN ENTEROVIRUS 70 CAPSID PROTEINS.
[16]"Coxsackievirus A21 binds to decay-aCCelerating factor but requires intercellular adhesion molecule 1 for cell entry."
Shafren D.R., Dorahy D.J., Ingham R.A., Burns G.F., Barry R.D.
J. Virol. 71:4736-4743(1997) [PubMed: 9151867] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUS A21 CAPSID PROTEINS.
[17]"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed: 14517339] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[18]"Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
J. Proteome Res. 5:935-943(2006) [PubMed: 16602701] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, MASS SPECTROMETRY.
Tissue: Epithelium.
[20]"Interaction of decay-aCCelerating factor with coxsackievirus B3."
Hafenstein S., Bowman V.D., Chipman P.R., Bator Kelly C.M., Lin F., Medof M.E., Rossmann M.G.
J. Virol. 81:12927-12935(2007) [PubMed: 17804498] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUS B3 CAPSID PROTEINS.
[21]"Molecular basis of reduced or absent expression of decay-accelerating factor in Cromer blood group phenotypes."
Lublin D.M., Mallinson G., Poole J., Reid M.E., Thompson E.S., Ferdman B.R., Telen M.J., Anstee D.J., Tanner M.J.A.
Blood 84:1276-1282(1994) [PubMed: 7519480] [Abstract]
Cited for: VARIANT BLOOD GROUP DR(A-) LEU-199.
[22]"GUTI: a new antigen in the Cromer blood group system."
Storry J.R., Sausais L., Hue-Roye K., Mudiwa F., Ferrer Z., Blajchman M.A., Lublin D.M., Ma B.W., Miquel J.F., Nervi F., Pereira J., Reid M.E.
Transfusion 43:340-344(2003) [PubMed: 12675719] [Abstract]
Cited for: VARIANT BLOOD GROUP GUTI(-) HIS-240.
[23]"Biochemical studies on red blood cells from a patient with the Inab phenotype (decay-accelerating factor deficiency)."
Reid M.E., Mallinson G., Sim R.B., Poole J., Pausch V., Merry A.H., Liew Y.W., Tanner M.J.A.
Blood 78:3291-3297(1991) [PubMed: 1720702] [Abstract]
Cited for: INVOLVEMENT IN BLOOD GROUP INAB.
[24]"Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A."
Williams P., Chaudhry Y., Goodfellow I.G.,