P08174 (DAF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Complement decay-accelerating factor

Alternative name(s):
CD_antigen=CD55

Gene names

Name:	CD55
Synonyms:	CR, DAF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.14
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.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.21
Subcellular location	Isoform 1: Cell 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. Ref.13
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 process	Complement pathway Immunity Innate immunity
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Sushi
Molecular function	Blood group antigen Host cell receptor for virus entry Receptor
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW elevation of cytosolic calcium ion concentration Inferred from direct assay PubMed 8223854. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome maternal process involved in parturition Inferred from electronic annotation. Source: Compara negative regulation of complement activation Inferred from electronic annotation. Source: Compara regulation of complement activation Traceable author statement. Source: Reactome respiratory burst Non-traceable author statement PubMed 8223854. Source: UniProtKB response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW apical plasma membrane Inferred from electronic annotation. Source: Compara cell surface Inferred from direct assay PubMed 15907827. Source: UniProtKB extracellular region Traceable author statement. Source: Reactome integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc membrane raft Inferred from direct assay PubMed 11313396. Source: UniProtKB
Molecular_function	enzyme inhibitor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

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.

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 34

34

Ref.10 Ref.11

Chain

35 – 353

319

Complement decay-accelerating factor

PRO_0000006000

Propeptide

354 – 381

28

Removed in mature form

PRO_0000006001

Regions

Domain

35 – 96

62

Sushi 1

Domain

96 – 160

65

Sushi 2

Domain

161 – 222

62

Sushi 3

Domain

223 – 285

63

Sushi 4

Compositional bias

287 – 356

70

Ser/Thr-rich

Amino acid modifications

Lipidation

353

1

GPI-anchor amidated serine Ref.12 Ref.19 Ref.20

Glycosylation

95

1

N-linked (GlcNAc...) Ref.22

Disulfide bond

36 ↔ 81

Ref.13

Disulfide bond

65 ↔ 94

Ref.13

Disulfide bond

98 ↔ 145

Ref.13

Disulfide bond

129 ↔ 158

Ref.13

Disulfide bond

163 ↔ 204

Ref.13

Disulfide bond

190 ↔ 220

Ref.13

Disulfide bond

225 ↔ 267

Ref.13

Disulfide bond

253 ↔ 283

Ref.13

Natural variations

Alternative sequence

362 – 381

20

HTCFT…MGLLT → SRPVTQAGMRWCDRSSLQSR TPGFKRSFHFSLPSSWYYRA HVFHVDRFAWDASNHGLADL AKEELRRKYTQVYRLFLVS in isoform 1.

VSP_001200

Natural variant

52

1

R → L in Tc(b) antigen. Ref.3
Corresponds to variant rs28371588 [ dbSNP | Ensembl ].

VAR_001997

Natural variant

52

1

R → P in Tc(c) antigen.

VAR_001998

Natural variant

82

1

L → R in WES(a) antigen.

VAR_001999

Natural variant

199

1

S → L in Dr(a-) antigen. Ref.24
Corresponds to variant rs56283594 [ dbSNP | Ensembl ].

VAR_002000

Natural variant

227

1

A → P in Cr(a-) antigen.
Corresponds to variant rs60822373 [ dbSNP | Ensembl ].

VAR_002001

Natural variant

240

1

R → H in GUTI(-) antigen. Ref.25

VAR_015884

Experimental info

Sequence conflict

80

1

I → T in AAA52170. Ref.7

Sequence conflict

80

1

I → T in AAA52167. Ref.8

Sequence conflict

85

1

S → M in AAA52167. Ref.8

Sequence conflict

187

1

S → T in AAB48622. Ref.9

Sequence conflict

297

1

Q → H in AAB48622. Ref.9

Secondary structure

1

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381

Helix Strand Turn

Details...

Beta strand

45 – 47

3

Beta strand

60 – 65

6

Beta strand

69 – 71

3

Beta strand

78 – 82

5

Turn

83 – 85

3

Beta strand

94 – 98

5

Beta strand

105 – 109

5

Helix

113 – 115

3

Beta strand

124 – 129

6

Beta strand

133 – 135

3

Beta strand

136 – 138

3

Beta strand

142 – 145

4

Beta strand

149 – 151

3

Beta strand

157 – 160

4

Beta strand

172 – 175

4

Turn

177 – 180

4

Beta strand

185 – 190

6

Beta strand

194 – 198

5

Beta strand

200 – 207

8

Beta strand

210 – 215

6

Beta strand

219 – 222

4

Beta strand

234 – 236

3

Beta strand

241 – 244

4

Beta strand

248 – 253

6

Beta strand

258 – 261

4

Beta strand

263 – 270

8

Beta strand

273 – 278

6

Beta strand

282 – 284

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (DAF-2) [UniParc]. Last modified March 1, 2005. Version 4. Checksum: C1CBE5300F60C176	FASTA	381	41,400
	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
	Isoform 1 (DAF-1) [UniParc]. Checksum: CF6154031FAC5D58	FASTA	440	48,717
	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 370 380 390 400 410 420 GSRPVTQAGM RWCDRSSLQS RTPGFKRSFH FSLPSSWYYR AHVFHVDRFA WDASNHGLAD 430 440 LAKEELRRKY TQVYRLFLVS

References

	« Hide 'large scale' referencesShow '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]	"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).
[3]	SeattleSNPs variation discovery resource Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-52.
[4]	"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. , 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].
[5]	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. , 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].
[6]	"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.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
[8]	"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).
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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.
[22]	"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, MASS SPECTROMETRY. Tissue: Liver.
[23]	"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].
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
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.

IPI

IPI00216550.
IPI00292069.

PIR

A26359.
B26359.

RefSeq

NP_000565.1. NM_000574.3.
NP_001108224.1. NM_001114752.1.

UniGene

Hs.126517.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H03	X-ray	1.70	P/Q	161-285	[»]
1H04	X-ray	2.00	P	161-285	[»]
1H2P	X-ray	2.80	P	161-285	[»]
1H2Q	X-ray	3.00	P	161-285	[»]
1M11	electron microscopy	16.00	R	35-277	[»]
1NWV	NMR	-	A	96-222	[»]
1OJV	X-ray	2.30	A/B	35-285	[»]
1OJW	X-ray	2.30	A/B	35-285	[»]
1OJY	X-ray	2.60	A/B/C/D	35-285	[»]
1OK1	X-ray	2.60	A/B	35-285	[»]
1OK2	X-ray	2.50	A/B	35-285	[»]
1OK3	X-ray	2.20	A/B	35-285	[»]
1OK9	X-ray	3.00	A/B	35-285	[»]
1UOT	X-ray	3.00	P	161-285	[»]
1UPN	electron microscopy	16.00	E	157-285	[»]
2C8I	electron microscopy	14.00	E	35-285	[»]
2QZD	electron microscopy	-	A	222-285	[»]
2QZF	electron microscopy	-	A	35-94	[»]
2QZH	electron microscopy	14.00	A	96-222	[»]
3IYP	electron microscopy	-	F	1-381	[»]
3J24	electron microscopy	9.00	B	35-285	[»]

ProteinModelPortal

P08174.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08174. 5 interactions.

STRING

9606.ENSP00000316333.

PTM databases

PhosphoSite

P08174.

Polymorphism databases

DMDM

60416353.

Proteomic databases

PaxDb

P08174.

PRIDE

P08174.

Protocols and materials databases

DNASU

1604.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000314754; ENSP00000316333; ENSG00000196352.
ENST00000367064; ENSP00000356031; ENSG00000196352.

GeneID

1604.

KEGG

hsa:1604.

UCSC

uc001hfq.4. human.
uc001hfr.4. human.

Organism-specific databases

CTD

1604.

GeneCards

GC01P207494.

HGNC

HGNC:2665. CD55.

HPA

CAB010454.
HPA002190.
HPA024386.

MIM

125240. gene.
613793. phenotype.

neXtProt

NX_P08174.

PharmGKB

PA27137.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG150769.

HOGENOM

HOG000237360.

HOVERGEN

HBG001406.

KO

K04006.

OrthoDB

EOG4WSWB0.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P08174.

Bgee

P08174.

CleanEx

HS_CD55.

Genevestigator

P08174.

GermOnline

ENSG00000196352. Homo sapiens.

Family and domain databases

InterPro

IPR000436. Sushi_SCR_CCP.
[Graphical view]

Pfam

PF00084. Sushi. 4 hits.
[Graphical view]

SMART

SM00032. CCP. 4 hits.
[Graphical view]

SUPFAM

SSF57535. Complement_control_module. 4 hits.

PROSITE

PS50923. SUSHI. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CD55. human.

DrugBank

DB00446. Chloramphenicol.

EvolutionaryTrace

P08174.

GenomeRNAi

1604.

NextBio

6582.

SOURCE

Search...

Entry information

Entry name

DAF_HUMAN

Accession

Primary (citable) accession number: P08174
Secondary accession number(s): B1AP14 , D3DT83, D3DT84, P09679, P78361

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	March 1, 2005
Last modified:	May 1, 2013
This is version 158 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.