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P08174 (DAF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

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. Ref.15

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. Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.2.

Isoform 2: Cell membrane; Lipid-anchorGPI-anchor Ref.2.

Isoform 3: Secreted Ref.2.

Isoform 4: Secreted Ref.2.

Isoform 5: Secreted Ref.2.

Isoform 6: Cell membrane; Lipid-anchorGPI-anchor Probable Ref.2.

Isoform 7: Cell membrane; Lipid-anchorGPI-anchor Probable Ref.2.

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. Ref.14

Post-translational modification

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

Polymorphism

Responsible for the Cromer blood group system (CROM) [MIM:613793]. 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.

Ontologies

Keywords
   Biological processComplement pathway
Immunity
Innate immunity
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Sushi
   Molecular functionBlood group antigen
Host cell receptor for virus entry
Receptor
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCD4-positive, alpha-beta T cell cytokine production

Inferred from direct assay PubMed 16818763. Source: UniProt

complement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement. Source: Reactome

maternal process involved in parturition

Inferred from electronic annotation. Source: Ensembl

negative regulation of complement activation

Inferred from direct assay PubMed 6211481. Source: UniProt

positive regulation of CD4-positive, alpha-beta T cell activation

Inferred from direct assay PubMed 16818763. Source: UniProt

positive regulation of CD4-positive, alpha-beta T cell proliferation

Inferred from direct assay PubMed 16818763. Source: UniProt

positive regulation of cytosolic calcium ion concentration

Inferred from direct assay PubMed 8223854. Source: UniProtKB

regulation of complement activation

Traceable author statement. Source: Reactome

regulation of lipopolysaccharide-mediated signaling pathway

Inferred from direct assay PubMed 12731067. Source: UniProt

respiratory burst

Non-traceable author statement PubMed 8223854. Source: UniProtKB

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from direct assay Ref.15. Source: GOC

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 15907827. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 20458337PubMed 23376485. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

membrane raft

Inferred from direct assay PubMed 11313396. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 6211481. Source: UniProt

   Molecular_functionenzyme inhibitor activity

Inferred from electronic annotation. Source: Ensembl

lipid binding

Inferred from direct assay PubMed 12731067. Source: UniProt

protein binding

Inferred from physical interaction PubMed 9064337. Source: UniProt

virus receptor activity

Inferred from direct assay Ref.15. Source: UniProt

Complete GO annotation...

Alternative products

This entry describes 7 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.
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
Isoform 3 (identifier: P08174-3)

Also known as: VDAF3;

The sequence of this isoform differs from the canonical sequence as follows:
     361-381: GHTCFTLTGLLGTLVTMGLLT → ALQVRPFEVSGSSHISSKKMMCIL
Isoform 4 (identifier: P08174-4)

Also known as: VDAF2;

The sequence of this isoform differs from the canonical sequence as follows:
     361-381: GHTCFTLTGLLGTLVTMGLLT → VLFM
Isoform 5 (identifier: P08174-5)

Also known as: VDAF1;

The sequence of this isoform differs from the canonical sequence as follows:
     361-381: GHTCFTLTGLLGTLVTMGLLT → ETVFHRVIQD...TQVYRLFLVS
Isoform 6 (identifier: P08174-6)

Also known as: VDAF4;

The sequence of this isoform differs from the canonical sequence as follows:
     327-327: A → GTETPSVLQK...AFTQSPSAAP
Note: Includes partial sequence of the intron 7.
Isoform 7 (identifier: P08174-7)

Also known as: VDAF5;

The sequence of this isoform differs from the canonical sequence as follows:
     326-326: Q → QGTETPSVLQ...TQRFPSAHIT
Note: Includes full sequence of the intron 7.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Ref.11 Ref.12
Chain35 – 353319Complement decay-accelerating factor
PRO_0000006000
Propeptide354 – 38128Removed in mature form
PRO_0000006001

Regions

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

Amino acid modifications

Lipidation3531GPI-anchor amidated serine Ref.13 Ref.20 Ref.21
Glycosylation951N-linked (GlcNAc...) Ref.23
Disulfide bond36 ↔ 81 Ref.14
Disulfide bond65 ↔ 94 Ref.14
Disulfide bond98 ↔ 145 Ref.14
Disulfide bond129 ↔ 158 Ref.14
Disulfide bond163 ↔ 204 Ref.14
Disulfide bond190 ↔ 220 Ref.14
Disulfide bond225 ↔ 267 Ref.14
Disulfide bond253 ↔ 283 Ref.14

Natural variations

Alternative sequence3261Q → QGTETPSVLQKHTTENVSAT RTPPTPQKPTTVNVPATIVT PTPQKPTTINVPATGVSSTP QRHTIVNVSATGTLPTLQKP TRANDSATKSPAAAQTSFIS KTLSTKTPSAAQNPMMTNAS ATQATLTAQKFTTAKVAFTQ SPSAARKSTNVHSPVTNGLK STQRFPSAHIT in isoform 7.
VSP_047634
Alternative sequence3271A → GTETPSVLQKHTTENVSATR TPPTPQKPTTVNVPATIVTP TPQKPTTINVPATGVSSTPQ RHTIVNVSATGTLPTLQKPT RANDSATKSPAAAQTSFISK TLSTKTPSAAQNPMMTNASA TQATLTAQKFTTAKVAFTQS PSAAP in isoform 6.
VSP_047635
Alternative sequence361 – 38121GHTCF…MGLLT → ALQVRPFEVSGSSHISSKKM MCIL in isoform 3.
VSP_047636
Alternative sequence361 – 38121GHTCF…MGLLT → VLFM in isoform 4.
VSP_047637
Alternative sequence361 – 38121GHTCF…MGLLT → ETVFHRVIQDGLDLLASRSA CLGLPKCWDYRREPPHLARA HVFHVDRFAWDASNHGLADL AKEELRRKYTQVYRLFLVS in isoform 5.
VSP_047638
Alternative sequence362 – 38120HTCFT…MGLLT → SRPVTQAGMRWCDRSSLQSR TPGFKRSFHFSLPSSWYYRA HVFHVDRFAWDASNHGLADL AKEELRRKYTQVYRLFLVS in isoform 1.
VSP_001200
Natural variant521R → L in Tc(b) antigen. Ref.4
Corresponds to variant rs28371588 [ dbSNP | Ensembl ].
VAR_001997
Natural variant521R → P in Tc(c) antigen.
Corresponds to variant rs28371588 [ dbSNP | Ensembl ].
VAR_001998
Natural variant821L → R in WES(a) antigen.
Corresponds to variant rs147474393 [ dbSNP | Ensembl ].
VAR_001999
Natural variant1991S → L in Dr(a-) antigen. Ref.25
Corresponds to variant rs56283594 [ dbSNP | Ensembl ].
VAR_002000
Natural variant2271A → P in Cr(a-) antigen.
Corresponds to variant rs60822373 [ dbSNP | Ensembl ].
VAR_002001
Natural variant2401R → H in GUTI(-) antigen. Ref.26
VAR_015884

Experimental info

Sequence conflict801I → T in AAA52170. Ref.8
Sequence conflict801I → T in AAA52167. Ref.9
Sequence conflict851S → M in AAA52167. Ref.9
Sequence conflict1871S → T in AAB48622. Ref.10
Sequence conflict2971Q → H in AAB48622. Ref.10

Secondary structure

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

Details...

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 »

FASTA44048,717
Isoform 3 (VDAF3) [UniParc].

Checksum: 192116A331DBD533
Show »

FASTA38441,900
Isoform 4 (VDAF2) [UniParc].

Checksum: BFDE9FD6B7C10A07
Show »

FASTA36439,759
Isoform 5 (VDAF1) [UniParc].

Checksum: 256086EFD8CDBDBA
Show »

FASTA43948,513
Isoform 6 (VDAF4) [UniParc].

Checksum: 1AAFC1E5FD7DCE4C
Show »

FASTA52556,218
Isoform 7 (VDAF5) [UniParc].

Checksum: 505AEC29D919AF48
Show »

FASTA55159,038

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"Molecular cloning and characterization of novel splicing variants of human decay-accelerating factor."
Osuka F., Endo Y., Higuchi M., Suzuki H., Shio Y., Fujiu K., Kanno R., Oishi A., Terashima M., Fujita T., Gotoh M.
Genomics 88:316-322(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), SUBCELLULAR LOCATION (ISOFORMS 3; 4; 5; 6 AND 7).
Tissue: Lung.
[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]SeattleSNPs variation discovery resource
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-52.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cervix.
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-381 (ISOFORM 2).
[10]"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 [MRNA] OF 35-381 (ISOFORM 2).
Tissue: Hippocampus.
[11]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-63.
[12]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-46.
Tissue: Urine.
[13]"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] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR AT SER-353.
[14]"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] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS IN SUSHI DOMAINS.
[15]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN ECHOVIRUS RECEPTOR.
[16]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ECHOVIRUSES 6/7/11/12/20/21 CAPSID PROTEINS.
[17]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUSES B1/B3/B5 CAPSID PROTEINS.
[18]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ENTEROVIRUS 70 CAPSID PROTEINS.
[19]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUS A21 CAPSID PROTEINS.
[20]"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] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUS B3 CAPSID PROTEINS.
[23]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95.
Tissue: Liver.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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] [Europe PMC] [Abstract]
Cited for: VARIANT BLOOD GROUP DR(A-) LEU-199.
[26]"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] [Europe PMC] [Abstract]
Cited for: VARIANT BLOOD GROUP GUTI(-) HIS-240.
[27]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BLOOD GROUP INAB.
[28]"Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A."
Williams P., Chaudhry Y., Goodfellow I.G., Billington J., Powell R., Spiller O.B., Evans D.J., Lea S.
J. Biol. Chem. 278:10691-10696(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 161-285.
[29]"Complement regulation at the molecular level: the structure of decay-accelerating factor."
Lukacik P., Roversi P., White J., Esser D., Smith G.P., Billington J., Williams P.A., Rudd P.M., Wormald M.R., Harvey D.J., Crispin M.D., Radcliffe C.M., Dwek R.A., Evans D.J., Morgan B.P., Smith R.A., Lea S.M.
Proc. Natl. Acad. Sci. U.S.A. 101:1279-1284(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF OF 35-286.
[30]"Solution structure of a functionally active fragment of decay-accelerating factor."
Uhrinova S., Lin F., Ball G., Bromek K., Uhrin D., Medof M.E., Barlow P.N.
Proc. Natl. Acad. Sci. U.S.A. 100:4718-4723(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 95-223.
+Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

CD55base

CD55 mutation db

Wikipedia

Decay-accelerating factor entry

SeattleSNPs
Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31516 mRNA. Translation: AAA52169.1.
M30142 mRNA. Translation: AAA52168.1.
AB240566 mRNA. Translation: BAE97422.1.
AB240567 mRNA. Translation: BAE97423.1.
AB240568 mRNA. Translation: BAE97424.1.
AB240569 mRNA. Translation: BAE97425.1.
AB240570 mRNA. Translation: BAE97426.1.
BT007159 mRNA. Translation: AAP35823.1.
AY851161 Genomic DNA. Translation: AAW29942.1.
AL391597, AL596218 Genomic DNA. Translation: CAH72946.1.
AL596218, AL391597 Genomic DNA. Translation: CAI16463.1.
CH471100 Genomic DNA. Translation: EAW93485.1.
CH471100 Genomic DNA. Translation: EAW93487.1.
CH471100 Genomic DNA. Translation: EAW93488.1.
CH471100 Genomic DNA. Translation: EAW93491.1.
BC001288 mRNA. Translation: AAH01288.1.
M64653, M64356 Genomic DNA. Translation: AAA52170.1.
M15799 mRNA. Translation: AAA52167.1.
U88576 mRNA. Translation: AAB48622.1.
S72858 Genomic DNA. Translation: AAC60633.1.
CCDSCCDS31006.1. [P08174-1]
CCDS44307.1. [P08174-2]
PIRA26359.
B26359.
RefSeqNP_000565.1. NM_000574.3. [P08174-1]
NP_001108224.1. NM_001114752.1. [P08174-2]
UniGeneHs.126517.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H03X-ray1.70P/Q161-285[»]
1H04X-ray2.00P161-285[»]
1H2PX-ray2.80P161-285[»]
1H2QX-ray3.00P161-285[»]
1M11electron microscopy16.00R35-277[»]
1NWVNMR-A96-222[»]
1OJVX-ray2.30A/B35-285[»]
1OJWX-ray2.30A/B35-285[»]
1OJYX-ray2.60A/B/C/D35-285[»]
1OK1X-ray2.60A/B35-285[»]
1OK2X-ray2.50A/B35-285[»]
1OK3X-ray2.20A/B35-285[»]
1OK9X-ray3.00A/B35-285[»]
1UOTX-ray3.00P161-285[»]
1UPNelectron microscopy16.00E157-285[»]
2C8Ielectron microscopy14.00E35-285[»]
2QZDelectron microscopy-A222-285[»]
2QZFelectron microscopy-A35-94[»]
2QZHelectron microscopy14.00A96-222[»]
3IYPelectron microscopy-F1-381[»]
3J24electron microscopy9.00B35-285[»]
ProteinModelPortalP08174.
SMRP08174. Positions 35-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107974. 21 interactions.
IntActP08174. 5 interactions.
STRING9606.ENSP00000316333.

Chemistry

DrugBankDB00446. Chloramphenicol.

PTM databases

PhosphoSiteP08174.

Polymorphism databases

DMDM60416353.

Proteomic databases

MaxQBP08174.
PaxDbP08174.
PRIDEP08174.

Protocols and materials databases

DNASU1604.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314754; ENSP00000316333; ENSG00000196352. [P08174-2]
ENST00000367062; ENSP00000356029; ENSG00000196352. [P08174-4]
ENST00000367064; ENSP00000356031; ENSG00000196352. [P08174-1]
ENST00000367065; ENSP00000356032; ENSG00000196352. [P08174-5]
ENST00000391920; ENSP00000375787; ENSG00000196352. [P08174-3]
GeneID1604.
KEGGhsa:1604.
UCSCuc001hfq.4. human. [P08174-1]
uc001hfr.4. human. [P08174-2]

Organism-specific databases

CTD1604.
GeneCardsGC01P207494.
HGNCHGNC:2665. CD55.
HPACAB010454.
HPA002190.
HPA024386.
MIM125240. gene.
613793. phenotype.
neXtProtNX_P08174.
PharmGKBPA27137.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG150769.
HOGENOMHOG000237360.
HOVERGENHBG001406.
KOK04006.
OMAGHTCLIT.
OrthoDBEOG78WKS7.
PhylomeDBP08174.
TreeFamTF334137.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP08174.
BgeeP08174.
CleanExHS_CD55.
GenevestigatorP08174.

Family and domain databases

InterProIPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00084. Sushi. 4 hits.
[Graphical view]
SMARTSM00032. CCP. 4 hits.
[Graphical view]
SUPFAMSSF57535. SSF57535. 4 hits.
PROSITEPS50923. SUSHI. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD55. human.
EvolutionaryTraceP08174.
GeneWikiDecay-accelerating_factor.
GenomeRNAi1604.
NextBio6582.
PROP08174.
SOURCESearch...

Entry information

Entry nameDAF_HUMAN
AccessionPrimary (citable) accession number: P08174
Secondary accession number(s): B1AP14 expand/collapse secondary AC list , D3DT83, D3DT84, E7ER69, P09679, P78361, Q14UF2, Q14UF3, Q14UF4, Q14UF5, Q14UF6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: March 1, 2005
Last modified: July 9, 2014
This is version 170 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries