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Protein

Complement decay-accelerating factor

Gene

CD55

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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
(Microbial infection) Acts as a receptor for coxsackievirus A21, coxsackieviruses B1, B3 and B5 (PubMed:9151867). Acts as a receptor for human enterovirus 70 and D68 (Probable) (PubMed:8764022). Acts as a receptor for human echoviruses 6, 7, 11, 12, 20 and 21 (PubMed:7525274).1 Publication3 Publications

GO - Molecular functioni

  • lipid binding Source: UniProtKB
  • virus receptor activity Source: UniProtKB

GO - Biological processi

  • CD4-positive, alpha-beta T cell cytokine production Source: UniProtKB
  • complement activation, classical pathway Source: UniProtKB-KW
  • ER to Golgi vesicle-mediated transport Source: Reactome
  • innate immune response Source: UniProtKB-KW
  • negative regulation of complement activation Source: UniProtKB
  • positive regulation of CD4-positive, alpha-beta T cell activation Source: UniProtKB
  • positive regulation of CD4-positive, alpha-beta T cell proliferation Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  • regulation of complement activation Source: Reactome
  • regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • respiratory burst Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Complement pathway, Host-virus interaction, Immunity, Innate immunity

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143463-MONOMER.
ReactomeiR-HSA-373080. Class B/2 (Secretin family receptors).
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-977606. Regulation of Complement cascade.
SIGNORiP08174.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2665. CD55.

Subcellular locationi

Isoform 3 :
Isoform 4 :
Isoform 5 :
Isoform 6 :
Isoform 7 :

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • cell surface Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • Golgi membrane Source: Reactome
  • integral component of plasma membrane Source: ProtInc
  • membrane raft Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • transport vesicle Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi1604.
MIMi613793. phenotype.
OpenTargetsiENSG00000196352.
PharmGKBiPA27137.

Chemistry databases

DrugBankiDB00446. Chloramphenicol.

Polymorphism and mutation databases

BioMutaiCD55.
DMDMi60416353.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 342 PublicationsAdd BLAST34
ChainiPRO_000000600035 – 353Complement decay-accelerating factorAdd BLAST319
PropeptideiPRO_0000006001354 – 381Removed in mature formAdd BLAST28

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi36 ↔ 81PROSITE-ProRule annotation1 Publication
Disulfide bondi65 ↔ 94PROSITE-ProRule annotation1 Publication
Glycosylationi95N-linked (GlcNAc...)1 Publication1
Disulfide bondi98 ↔ 145PROSITE-ProRule annotation1 Publication
Disulfide bondi129 ↔ 158PROSITE-ProRule annotation1 Publication
Disulfide bondi163 ↔ 204PROSITE-ProRule annotation1 Publication
Disulfide bondi190 ↔ 220PROSITE-ProRule annotation1 Publication
Disulfide bondi225 ↔ 267PROSITE-ProRule annotation1 Publication
Disulfide bondi253 ↔ 283PROSITE-ProRule annotation1 Publication
Lipidationi353GPI-anchor amidated serine1 Publication1

Post-translational modificationi

The Ser/Thr-rich domain is heavily O-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP08174.
PaxDbiP08174.
PeptideAtlasiP08174.
PRIDEiP08174.

PTM databases

iPTMnetiP08174.
PhosphoSitePlusiP08174.
SwissPalmiP08174.

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

BgeeiENSG00000196352.
CleanExiHS_CD55.
ExpressionAtlasiP08174. baseline and differential.
GenevisibleiP08174. HS.

Organism-specific databases

HPAiCAB010454.
HPA002190.
HPA024386.

Interactioni

Subunit structurei

Monomer (major form) and non-disulfide-linked, covalent homodimer (minor form).1 Publication1 Publication
(Microbial infection) Interacts with coxsackievirus A21, coxsackieviruses B1, B3 and B5 capsid proteins.1 Publication
(Microbial infection) Interacts with human enterovirus 70 and D68 capsid proteins (Probable).1 Publication
(Microbial infection) Interacts with human echoviruses 6, 7, 11, 12, 20 and 21 capsid proteins.1 Publication

Protein-protein interaction databases

BioGridi107974. 24 interactors.
IntActiP08174. 6 interactors.
STRINGi9606.ENSP00000316333.

Structurei

Secondary structure

1381
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi45 – 47Combined sources3
Beta strandi60 – 65Combined sources6
Beta strandi69 – 71Combined sources3
Beta strandi78 – 82Combined sources5
Turni83 – 85Combined sources3
Beta strandi94 – 98Combined sources5
Beta strandi105 – 109Combined sources5
Helixi113 – 115Combined sources3
Beta strandi124 – 129Combined sources6
Beta strandi133 – 135Combined sources3
Beta strandi136 – 138Combined sources3
Beta strandi142 – 145Combined sources4
Beta strandi149 – 151Combined sources3
Beta strandi157 – 160Combined sources4
Beta strandi172 – 175Combined sources4
Turni177 – 180Combined sources4
Beta strandi185 – 190Combined sources6
Beta strandi194 – 198Combined sources5
Beta strandi200 – 207Combined sources8
Beta strandi210 – 215Combined sources6
Beta strandi219 – 222Combined sources4
Beta strandi234 – 236Combined sources3
Beta strandi241 – 244Combined sources4
Beta strandi248 – 253Combined sources6
Beta strandi258 – 261Combined sources4
Beta strandi263 – 270Combined sources8
Beta strandi273 – 278Combined sources6
Beta strandi282 – 284Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FOAX-ray4.19E/F97-285[»]
ProteinModelPortaliP08174.
SMRiP08174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08174.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 96Sushi 1PROSITE-ProRule annotationAdd BLAST62
Domaini96 – 160Sushi 2PROSITE-ProRule annotationAdd BLAST65
Domaini161 – 222Sushi 3PROSITE-ProRule annotationAdd BLAST62
Domaini223 – 285Sushi 4PROSITE-ProRule annotationAdd BLAST63

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi287 – 356Ser/Thr-richAdd BLAST70

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

eggNOGiENOG410IEGQ. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00860000133887.
HOGENOMiHOG000237360.
HOVERGENiHBG001406.
InParanoidiP08174.
KOiK04006.
PhylomeDBiP08174.
TreeFamiTF334137.

Family and domain databases

CDDicd00033. CCP. 4 hits.
InterProiIPR000436. Sushi_SCR_CCP_dom.
[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. AlignAdd to basket

Isoform 2 (identifier: P08174-1) [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)DescriptionActionsGraphical viewLength
Sequence conflicti80I → T in AAA52170 (PubMed:1711208).Curated1
Sequence conflicti80I → T in AAA52167 (PubMed:2436222).Curated1
Sequence conflicti85S → M in AAA52167 (PubMed:2436222).Curated1
Sequence conflicti187S → T in AAB48622 (Ref. 10) Curated1
Sequence conflicti297Q → H in AAB48622 (Ref. 10) Curated1

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 (PubMed:12675719).1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00199752R → L in Tc(b) antigen. 1 PublicationCorresponds to variant rs28371588dbSNPEnsembl.1
Natural variantiVAR_00199852R → P in Tc(c) antigen. Corresponds to variant rs28371588dbSNPEnsembl.1
Natural variantiVAR_00199982L → R in WES(a) antigen. Corresponds to variant rs147474393dbSNPEnsembl.1
Natural variantiVAR_002000199S → L in Dr(a-) antigen. 1 PublicationCorresponds to variant rs56283594dbSNPEnsembl.1
Natural variantiVAR_002001227A → P in Cr(a-) antigen. Corresponds to variant rs60822373dbSNPEnsembl.1
Natural variantiVAR_015884240R → H in GUTI(-) antigen. 1 PublicationCorresponds to variant rs199705465dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_047634326Q → QGTETPSVLQKHTTENVSAT RTPPTPQKPTTVNVPATIVT PTPQKPTTINVPATGVSSTP QRHTIVNVSATGTLPTLQKP TRANDSATKSPAAAQTSFIS KTLSTKTPSAAQNPMMTNAS ATQATLTAQKFTTAKVAFTQ SPSAARKSTNVHSPVTNGLK STQRFPSAHIT in isoform 7. 1 Publication1
Alternative sequenceiVSP_047635327A → GTETPSVLQKHTTENVSATR TPPTPQKPTTVNVPATIVTP TPQKPTTINVPATGVSSTPQ RHTIVNVSATGTLPTLQKPT RANDSATKSPAAAQTSFISK TLSTKTPSAAQNPMMTNASA TQATLTAQKFTTAKVAFTQS PSAAP in isoform 6. 1 Publication1
Alternative sequenceiVSP_047636361 – 381GHTCF…MGLLT → ALQVRPFEVSGSSHISSKKM MCIL in isoform 3. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_047637361 – 381GHTCF…MGLLT → VLFM in isoform 4. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_047638361 – 381GHTCF…MGLLT → ETVFHRVIQDGLDLLASRSA CLGLPKCWDYRREPPHLARA HVFHVDRFAWDASNHGLADL AKEELRRKYTQVYRLFLVS in isoform 5. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_001200362 – 381HTCFT…MGLLT → SRPVTQAGMRWCDRSSLQSR TPGFKRSFHFSLPSSWYYRA HVFHVDRFAWDASNHGLADL AKEELRRKYTQVYRLFLVS in isoform 1. 2 PublicationsAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
NP_001287832.1. NM_001300903.1. [P08174-5]
NP_001287833.1. NM_001300904.1. [P08174-3]
UniGeneiHs.126517.
Hs.609950.

Genome annotation databases

EnsembliENST00000314754; ENSP00000316333; ENSG00000196352. [P08174-2]
ENST00000367064; ENSP00000356031; ENSG00000196352. [P08174-1]
GeneIDi1604.
KEGGihsa:1604.
UCSCiuc001hfq.5. human. [P08174-1]

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:
EMBLi
GenBanki
DDBJi
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]
NP_001287832.1. NM_001300903.1. [P08174-5]
NP_001287833.1. NM_001300904.1. [P08174-3]
UniGeneiHs.126517.
Hs.609950.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FOAX-ray4.19E/F97-285[»]
ProteinModelPortaliP08174.
SMRiP08174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107974. 24 interactors.
IntActiP08174. 6 interactors.
STRINGi9606.ENSP00000316333.

Chemistry databases

DrugBankiDB00446. Chloramphenicol.

PTM databases

iPTMnetiP08174.
PhosphoSitePlusiP08174.
SwissPalmiP08174.

Polymorphism and mutation databases

BioMutaiCD55.
DMDMi60416353.

Proteomic databases

MaxQBiP08174.
PaxDbiP08174.
PeptideAtlasiP08174.
PRIDEiP08174.

Protocols and materials databases

DNASUi1604.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314754; ENSP00000316333; ENSG00000196352. [P08174-2]
ENST00000367064; ENSP00000356031; ENSG00000196352. [P08174-1]
GeneIDi1604.
KEGGihsa:1604.
UCSCiuc001hfq.5. human. [P08174-1]

Organism-specific databases

CTDi1604.
DisGeNETi1604.
GeneCardsiCD55.
HGNCiHGNC:2665. CD55.
HPAiCAB010454.
HPA002190.
HPA024386.
MIMi125240. gene.
613793. phenotype.
neXtProtiNX_P08174.
OpenTargetsiENSG00000196352.
PharmGKBiPA27137.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEGQ. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00860000133887.
HOGENOMiHOG000237360.
HOVERGENiHBG001406.
InParanoidiP08174.
KOiK04006.
PhylomeDBiP08174.
TreeFamiTF334137.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143463-MONOMER.
ReactomeiR-HSA-373080. Class B/2 (Secretin family receptors).
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-977606. Regulation of Complement cascade.
SIGNORiP08174.

Miscellaneous databases

ChiTaRSiCD55. human.
EvolutionaryTraceiP08174.
GeneWikiiDecay-accelerating_factor.
GenomeRNAii1604.
PROiP08174.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196352.
CleanExiHS_CD55.
ExpressionAtlasiP08174. baseline and differential.
GenevisibleiP08174. HS.

Family and domain databases

CDDicd00033. CCP. 4 hits.
InterProiIPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00084. Sushi. 4 hits.
[Graphical view]
SMARTiSM00032. CCP. 4 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 4 hits.
PROSITEiPS50923. SUSHI. 4 hits.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 196 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.