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P08174

- DAF_HUMAN

UniProt

P08174 - DAF_HUMAN

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Protein

Complement decay-accelerating factor

Gene

CD55

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. enzyme inhibitor activity Source: Ensembl
  2. lipid binding Source: UniProt
  3. virus receptor activity Source: UniProt

GO - Biological processi

  1. CD4-positive, alpha-beta T cell cytokine production Source: UniProt
  2. complement activation, classical pathway Source: UniProtKB-KW
  3. innate immune response Source: Reactome
  4. maternal process involved in parturition Source: Ensembl
  5. negative regulation of complement activation Source: UniProt
  6. positive regulation of CD4-positive, alpha-beta T cell activation Source: UniProt
  7. positive regulation of CD4-positive, alpha-beta T cell proliferation Source: UniProt
  8. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  9. regulation of complement activation Source: Reactome
  10. regulation of lipopolysaccharide-mediated signaling pathway Source: UniProt
  11. respiratory burst Source: UniProtKB
  12. response to peptide hormone Source: Ensembl
  13. response to virus Source: GOC
  14. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Blood group antigen, Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_118707. Regulation of Complement cascade.
REACT_18372. Class B/2 (Secretin family receptors).

Names & Taxonomyi

Protein namesi
Recommended name:
Complement decay-accelerating factor
Alternative name(s):
CD_antigen: CD55
Gene namesi
Name:CD55
Synonyms:CR, DAF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2665. CD55.

Subcellular locationi

Isoform 3 : Secreted 1 Publication
Isoform 4 : Secreted 1 Publication
Isoform 5 : Secreted 1 Publication
Isoform 6 : Cell membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication
Isoform 7 : Cell membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. apical plasma membrane Source: Ensembl
  3. cell surface Source: UniProtKB
  4. extracellular region Source: Reactome
  5. extracellular vesicular exosome Source: UniProtKB
  6. integral component of plasma membrane Source: ProtInc
  7. membrane raft Source: UniProtKB
  8. plasma membrane Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

MIMi613793. phenotype.
PharmGKBiPA27137.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 34342 PublicationsAdd
BLAST
Chaini35 – 353319Complement decay-accelerating factorPRO_0000006000Add
BLAST
Propeptidei354 – 38128Removed in mature formPRO_0000006001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 811 PublicationPROSITE-ProRule annotation
Disulfide bondi65 ↔ 941 PublicationPROSITE-ProRule annotation
Glycosylationi95 – 951N-linked (GlcNAc...)1 Publication
Disulfide bondi98 ↔ 1451 PublicationPROSITE-ProRule annotation
Disulfide bondi129 ↔ 1581 PublicationPROSITE-ProRule annotation
Disulfide bondi163 ↔ 2041 PublicationPROSITE-ProRule annotation
Disulfide bondi190 ↔ 2201 PublicationPROSITE-ProRule annotation
Disulfide bondi225 ↔ 2671 PublicationPROSITE-ProRule annotation
Disulfide bondi253 ↔ 2831 PublicationPROSITE-ProRule annotation
Lipidationi353 – 3531GPI-anchor amidated serine1 Publication

Post-translational modificationi

The Ser/Thr-rich domain is heavily O-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP08174.
PaxDbiP08174.
PRIDEiP08174.

PTM databases

PhosphoSiteiP08174.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiP08174.
CleanExiHS_CD55.
ExpressionAtlasiP08174. baseline and differential.
GenevestigatoriP08174.

Organism-specific databases

HPAiCAB010454.
HPA002190.
HPA024386.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi107974. 23 interactions.
IntActiP08174. 6 interactions.
STRINGi9606.ENSP00000316333.

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 473
Beta strandi60 – 656
Beta strandi69 – 713
Beta strandi78 – 825
Turni83 – 853
Beta strandi94 – 985
Beta strandi105 – 1095
Helixi113 – 1153
Beta strandi124 – 1296
Beta strandi133 – 1353
Beta strandi136 – 1383
Beta strandi142 – 1454
Beta strandi149 – 1513
Beta strandi157 – 1604
Beta strandi172 – 1754
Turni177 – 1804
Beta strandi185 – 1906
Beta strandi194 – 1985
Beta strandi200 – 2078
Beta strandi210 – 2156
Beta strandi219 – 2224
Beta strandi234 – 2363
Beta strandi241 – 2444
Beta strandi248 – 2536
Beta strandi258 – 2614
Beta strandi263 – 2708
Beta strandi273 – 2786
Beta strandi282 – 2843

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP08174.
SMRiP08174. Positions 35-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08174.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 9662Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini96 – 16065Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini161 – 22262Sushi 3PROSITE-ProRule annotationAdd
BLAST
Domaini223 – 28563Sushi 4PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi287 – 35670Ser/Thr-richAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Contains 4 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiNOG150769.
GeneTreeiENSGT00760000118803.
HOGENOMiHOG000237360.
HOVERGENiHBG001406.
InParanoidiP08174.
KOiK04006.
OMAiGHTCLIT.
OrthoDBiEOG78WKS7.
PhylomeDBiP08174.
TreeFamiTF334137.

Family and domain databases

InterProiIPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamiPF00084. Sushi. 4 hits.
[Graphical view]
SMARTiSM00032. CCP. 4 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 4 hits.
PROSITEiPS50923. SUSHI. 4 hits.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: P08174) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTVARPSVPA ALPLLGELPR LLLLVLLCLP AVWGDCGLPP DVPNAQPALE
60 70 80 90 100
GRTSFPEDTV ITYKCEESFV KIPGEKDSVI CLKGSQWSDI EEFCNRSCEV
110 120 130 140 150
PTRLNSASLK QPYITQNYFP VGTVVEYECR PGYRREPSLS PKLTCLQNLK
160 170 180 190 200
WSTAVEFCKK KSCPNPGEIR NGQIDVPGGI LFGATISFSC NTGYKLFGST
210 220 230 240 250
SSFCLISGSS VQWSDPLPEC REIYCPAPPQ IDNGIIQGER DHYGYRQSVT
260 270 280 290 300
YACNKGFTMI GEHSIYCTVN NDEGEWSGPP PECRGKSLTS KVPPTVQKPT
310 320 330 340 350
TVNVPTTEVS PTSQKTTTKT TTPNAQATRS TPVSRTTKHF HETTPNKGSG
360 370 380
TTSGTTRLLS GHTCFTLTGL LGTLVTMGLL T
Length:381
Mass (Da):41,400
Last modified:March 1, 2005 - v4
Checksum:iC1CBE5300F60C176
GO
Isoform 1 (identifier: P08174-2) [UniParc]FASTAAdd to Basket

Also known as: DAF-1

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

Show »
Length:440
Mass (Da):48,717
Checksum:iCF6154031FAC5D58
GO
Isoform 3 (identifier: P08174-3) [UniParc]FASTAAdd to Basket

Also known as: VDAF3

The sequence of this isoform differs from the canonical sequence as follows:
     361-381: GHTCFTLTGLLGTLVTMGLLT → ALQVRPFEVSGSSHISSKKMMCIL

Show »
Length:384
Mass (Da):41,900
Checksum:i192116A331DBD533
GO
Isoform 4 (identifier: P08174-4) [UniParc]FASTAAdd to Basket

Also known as: VDAF2

The sequence of this isoform differs from the canonical sequence as follows:
     361-381: GHTCFTLTGLLGTLVTMGLLT → VLFM

Show »
Length:364
Mass (Da):39,759
Checksum:iBFDE9FD6B7C10A07
GO
Isoform 5 (identifier: P08174-5) [UniParc]FASTAAdd to Basket

Also known as: VDAF1

The sequence of this isoform differs from the canonical sequence as follows:
     361-381: GHTCFTLTGLLGTLVTMGLLT → ETVFHRVIQD...TQVYRLFLVS

Show »
Length:439
Mass (Da):48,513
Checksum:i256086EFD8CDBDBA
GO
Isoform 6 (identifier: P08174-6) [UniParc]FASTAAdd to Basket

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.

Show »
Length:525
Mass (Da):56,218
Checksum:i1AAFC1E5FD7DCE4C
GO
Isoform 7 (identifier: P08174-7) [UniParc]FASTAAdd to Basket

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.

Show »
Length:551
Mass (Da):59,038
Checksum:i505AEC29D919AF48
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801I → T in AAA52170. (PubMed:1711208)Curated
Sequence conflicti80 – 801I → T in AAA52167. (PubMed:2436222)Curated
Sequence conflicti85 – 851S → M in AAA52167. (PubMed:2436222)Curated
Sequence conflicti187 – 1871S → T in AAB48622. 1 PublicationCurated
Sequence conflicti297 – 2971Q → H in AAB48622. 1 PublicationCurated

Polymorphismi

Responsible for the Cromer blood group system (CROM) [MIMi: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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521R → L in Tc(b) antigen. 1 Publication
Corresponds to variant rs28371588 [ dbSNP | Ensembl ].
VAR_001997
Natural varianti52 – 521R → P in Tc(c) antigen.
Corresponds to variant rs28371588 [ dbSNP | Ensembl ].
VAR_001998
Natural varianti82 – 821L → R in WES(a) antigen.
Corresponds to variant rs147474393 [ dbSNP | Ensembl ].
VAR_001999
Natural varianti199 – 1991S → L in Dr(a-) antigen. 1 Publication
Corresponds to variant rs56283594 [ dbSNP | Ensembl ].
VAR_002000
Natural varianti227 – 2271A → P in Cr(a-) antigen.
Corresponds to variant rs60822373 [ dbSNP | Ensembl ].
VAR_002001
Natural varianti240 – 2401R → H in GUTI(-) antigen. 1 Publication
VAR_015884

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei326 – 3261Q → QGTETPSVLQKHTTENVSAT RTPPTPQKPTTVNVPATIVT PTPQKPTTINVPATGVSSTP QRHTIVNVSATGTLPTLQKP TRANDSATKSPAAAQTSFIS KTLSTKTPSAAQNPMMTNAS ATQATLTAQKFTTAKVAFTQ SPSAARKSTNVHSPVTNGLK STQRFPSAHIT in isoform 7. 1 PublicationVSP_047634
Alternative sequencei327 – 3271A → GTETPSVLQKHTTENVSATR TPPTPQKPTTVNVPATIVTP TPQKPTTINVPATGVSSTPQ RHTIVNVSATGTLPTLQKPT RANDSATKSPAAAQTSFISK TLSTKTPSAAQNPMMTNASA TQATLTAQKFTTAKVAFTQS PSAAP in isoform 6. 1 PublicationVSP_047635
Alternative sequencei361 – 38121GHTCF…MGLLT → ALQVRPFEVSGSSHISSKKM MCIL in isoform 3. 1 PublicationVSP_047636Add
BLAST
Alternative sequencei361 – 38121GHTCF…MGLLT → VLFM in isoform 4. 1 PublicationVSP_047637Add
BLAST
Alternative sequencei361 – 38121GHTCF…MGLLT → ETVFHRVIQDGLDLLASRSA CLGLPKCWDYRREPPHLARA HVFHVDRFAWDASNHGLADL AKEELRRKYTQVYRLFLVS in isoform 5. 1 PublicationVSP_047638Add
BLAST
Alternative sequencei362 – 38120HTCFT…MGLLT → SRPVTQAGMRWCDRSSLQSR TPGFKRSFHFSLPSSWYYRA HVFHVDRFAWDASNHGLADL AKEELRRKYTQVYRLFLVS in isoform 1. 2 PublicationsVSP_001200Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31006.1. [P08174-1]
CCDS44307.1. [P08174-2]
PIRiA26359.
B26359.
RefSeqiNP_000565.1. NM_000574.4. [P08174-1]
NP_001108224.1. NM_001114752.2. [P08174-2]
UniGeneiHs.126517.
Hs.609950.

Genome annotation databases

EnsembliENST00000314754; ENSP00000316333; ENSG00000196352. [P08174-2]
ENST00000367064; ENSP00000356031; ENSG00000196352. [P08174-1]
GeneIDi1604.
KEGGihsa:1604.
UCSCiuc001hfq.4. human. [P08174-1]
uc001hfr.4. human. [P08174-2]
uc009xce.3. human.

Polymorphism databases

DMDMi60416353.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31006.1. [P08174-1 ]
CCDS44307.1. [P08174-2 ]
PIRi A26359.
B26359.
RefSeqi NP_000565.1. NM_000574.4. [P08174-1 ]
NP_001108224.1. NM_001114752.2. [P08174-2 ]
UniGenei Hs.126517.
Hs.609950.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P08174.
SMRi P08174. Positions 35-285.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107974. 23 interactions.
IntActi P08174. 6 interactions.
STRINGi 9606.ENSP00000316333.

Chemistry

DrugBanki DB00446. Chloramphenicol.

PTM databases

PhosphoSitei P08174.

Polymorphism databases

DMDMi 60416353.

Proteomic databases

MaxQBi P08174.
PaxDbi P08174.
PRIDEi P08174.

Protocols and materials databases

DNASUi 1604.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314754 ; ENSP00000316333 ; ENSG00000196352 . [P08174-2 ]
ENST00000367064 ; ENSP00000356031 ; ENSG00000196352 . [P08174-1 ]
GeneIDi 1604.
KEGGi hsa:1604.
UCSCi uc001hfq.4. human. [P08174-1 ]
uc001hfr.4. human. [P08174-2 ]
uc009xce.3. human.

Organism-specific databases

CTDi 1604.
GeneCardsi GC01P207494.
HGNCi HGNC:2665. CD55.
HPAi CAB010454.
HPA002190.
HPA024386.
MIMi 125240. gene.
613793. phenotype.
neXtProti NX_P08174.
PharmGKBi PA27137.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG150769.
GeneTreei ENSGT00760000118803.
HOGENOMi HOG000237360.
HOVERGENi HBG001406.
InParanoidi P08174.
KOi K04006.
OMAi GHTCLIT.
OrthoDBi EOG78WKS7.
PhylomeDBi P08174.
TreeFami TF334137.

Enzyme and pathway databases

Reactomei REACT_118707. Regulation of Complement cascade.
REACT_18372. Class B/2 (Secretin family receptors).

Miscellaneous databases

ChiTaRSi CD55. human.
EvolutionaryTracei P08174.
GeneWikii Decay-accelerating_factor.
GenomeRNAii 1604.
NextBioi 6582.
PROi P08174.
SOURCEi Search...

Gene expression databases

Bgeei P08174.
CleanExi HS_CD55.
ExpressionAtlasi P08174. baseline and differential.
Genevestigatori P08174.

Family and domain databases

InterProi IPR000436. Sushi_SCR_CCP.
[Graphical view ]
Pfami PF00084. Sushi. 4 hits.
[Graphical view ]
SMARTi SM00032. CCP. 4 hits.
[Graphical view ]
SUPFAMi SSF57535. SSF57535. 4 hits.
PROSITEi PS50923. SUSHI. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiDAF_HUMAN
AccessioniPrimary (citable) accession number: P08174
Secondary accession number(s): B1AP14
, D3DT83, D3DT84, E7ER69, P09679, P78361, Q14UF2, Q14UF3, Q14UF4, Q14UF5, Q14UF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: March 1, 2005
Last modified: October 29, 2014
This is version 173 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Blood group antigen proteins
    Nomenclature of blood group antigens and list of entries
  2. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  3. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. SIMILARITY comments
    Index of protein domains and families

External Data

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