Complement decay-accelerating factor precursor

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Web resources

Cross-references

Entry information

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.

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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.22
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. Ref.23
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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Keywords
Biological process	Complement pathway Immune response Innate immunity
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Sushi
Molecular function	Blood group antigen
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
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. Source: UniProtKB innate immune response Inferred from electronic annotation. Source: UniProtKB-KW respiratory burst Non-traceable author statement. Source: UniProtKB
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc membrane raft Inferred from direct assay. Source: UniProtKB soluble fraction Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

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

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

Modified residue

140

1

Phosphoserine Ref.21

Lipidation

353

1

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

Glycosylation

95

1

N-linked (GlcNAc...) Ref.23

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

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. dbSNP rs28371588. Ref.3

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. dbSNP rs56283594. Ref.24

VAR_002000

Natural variant

227

1

A → P in Cr(a-) antigen. dbSNP rs60822373.

VAR_002001

Natural variant

240

1

R → H in GUTI(-) antigen. Ref.25

VAR_015884

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

1

.

381

Helix Strand Turn

Details...

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Sequence		Length	Mass (Da)
Isoform 2 (DAF-2) [UniParc]. Last modified March 1, 2005. Version 4. Checksum: C1CBE5300F60C176 Show »	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 « Hide
Isoform 1 (DAF-1). Checksum: CF6154031FAC5D58 Show »	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 « Hide

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	« 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: 2433596] [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. Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [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. 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: 15489334] [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: 1711208] [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: 2436222] [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: 2428813] [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: 1712233] [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: 1824699] [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: 1377029] [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: 7525274] [Abstract] Cited for: FUNCTION AS A 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: 7517044] [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: 7538177] [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: 8764022] [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: 9151867] [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: 14517339] [Abstract] Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 16602701] [Abstract] Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]	"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.
[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: 17804498] [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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95, MASS SPECTROMETRY. Tissue: Liver.
[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: 7519480] [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: 12675719] [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: 1720702] [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: 12499389] [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: 14734808] [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: 12672958] [Abstract] Cited for: STRUCTURE BY NMR OF 95-223.
+	Additional computationally mapped references.

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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

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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: EAW93488.1.
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.
NP_001108224.1.

UniGene

Hs.126517

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	[»]

ModBase

Search...

STRING

P08174.

PRIDE

P08174.

Ensembl

ENST00000367064; ENSP00000356031; ENSG00000196352; Homo sapiens. [Genome view]

GeneID

1604.

KEGG

hsa:1604.

UCSC

uc001hfq.2. human.
uc001hfr.2. human.

CTD

1604.

GeneCards

GC01P205561.

H-InvDB

HIX0001538.

HGNC

HGNC:2665. CD55.

HPA

CAB010454.
HPA002190.
HPA024386.

MIM

125240. gene+phenotype.

GenAtlas

Search...

eggNOG

prNOG14672.

HOVERGEN

P08174.

OrthoDB

EOG95HVH1.

ArrayExpress

P08174.

Bgee

P08174.

CleanEx

HS_CD55.

Genevestigator

P08174.

GermOnline

ENSG00000196352. Homo sapiens.

InterPro

IPR016060. Complement_control_module.
IPR000436. Sushi_SCR_CCP.
[Graphical view]

Gene3D

G3DSA:2.10.70.10. Complement_control_module. 4 hits.

Pfam

PF00084. Sushi. 4 hits.
[Graphical view]

SMART

SM00032. CCP. 4 hits.
[Graphical view]

PROSITE

PS50923. SUSHI. 4 hits.
[Graphical view]

ProtoNet

Search...

DrugBank

DB00446. Chloramphenicol.

NextBio

6582.

SOURCE

Search...

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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.

Note: 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

Entry name

DAF_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	March 1, 2005
Last modified:	February 9, 2010
This is version 128 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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