Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0000535
UniProt IDP08174
Primary gene name(s)CD55
Synonym gene name(s)CR, DAF
Protein nameComplement decay-accelerating factor
Protein functionThis 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. {ECO:0000269|PubMed:7525274}.; FUNCTION:, 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. {ECO:0000269|PubMed:7525274, ECO:0000269|PubMed:8764022, ECO:0000269|PubMed:9151867, ECO:0000305|PubMed:12409401}.
Subcellular locationIsoform 1: Cell membrane;
Single-pass type I membrane protein.;
SUBCELLULAR LOCATION: Isoform 2: Cell membrane;
Lipid-anchor, GPI-anchor.;
SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000269|PubMed:16503113}.;
SUBCELLULAR LOCATION: Isoform 4: Secreted {ECO:0000269|PubMed:16503113}.;
SUBCELLULAR LOCATION: Isoform 5: Secreted {ECO:0000269|PubMed:16503113}.;
SUBCELLULAR LOCATION: Isoform 6: Cell membrane {ECO:0000305|PubMed:16503113};
Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:16503113}.;
SUBCELLULAR LOCATION: Isoform 7: Cell membrane {ECO:0000305|PubMed:16503113};
Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:16503113}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P08174
Gene Ontology
(Biological Process)
Complete annatation
CD4-positive, alpha-beta T cell cytokine production [GO:0035743];
complement activation, classical pathway [GO:0006958];
ER to Golgi vesicle-mediated transport [GO:0006888];
innate immune response [GO:0045087];
negative regulation of complement activation [GO:0045916];
positive regulation of CD4-positive, alpha-beta T cell activation [GO:2000516];
positive regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000563];
positive regulation of cytosolic calcium ion concentration [GO:0007204];
regulation of complement activation [GO:0030449];
regulation of lipopolysaccharide-mediated signaling pathway [GO:0031664];
respiratory burst [GO:0045730]
Gene Ontology
(Molecular Function)
Complete annatation
lipid binding [GO:0008289];
virus receptor activity [GO:0001618]
Gene Ontology
(Cellular Component)
Complete annatation
anchored component of membrane [GO:0031225];
cell surface [GO:0009986];
endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116];
extracellular exosome [GO:0070062];
extracellular region [GO:0005576];
Golgi membrane [GO:0000139];
integral component of plasma membrane [GO:0005887];
membrane raft [GO:0045121];
plasma membrane [GO:0005886];
transport vesicle [GO:0030133]
Protein-protein interaction107974
Phylogenetic treeP08174
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
      unknown
Brass et al., Science, 2008
      unknown
Smith et al., J. Immunol, 2010
      unknown
Interferon-stimulated
gene status
Lu et al., J. Virol., 2011
      Folds changes 8h: unknown; Folds changes 16h: unknown; Tested: unknown;
Schoggins JW and Rice CM, Curr. Opin. Virol., 2011
      Targeted viruses: unknown
      Viral life cycle: unknown
      Mechanism related to antiviral activity: unknown
Anti-viral restriction factor Liu et al., Retrovirology, 2011
      unknown (Triplicates)

Gene Expression Profile       top

            Up-regulated;            Down-regulated

For brief introduction to each study, please go to the help page.

Gene expression during HIV latency

(1). Mohammadi et al., PLoS Pathog., 2014

Differentially expressed transcripts (Pairwise) during latency and subsequent viral reactivation using several agents - Primary CD4+ T-cell based model


DMSO: Dimethyl suloxyde (negative control) - 0.0033% final
SAHA: Vorinostat (Histone deacetylase inhibitor) - 0.5 μM
CD3: TCR Stimulation by IL-2+ antiCD3/anti-CD28 antibodies
IL7: Interleukin-7 based stimulation
DISU: Disulfiram (alcohol dehydrogenase inhibitor) - 0.5 μM
AZA: 5-azacytidine (AZA; DNA methylation inhibitor) - 1 μM
Experimental Condition Log2 Fold Change P value Adjusted P value
AZA vs. CD30.2470222347835920.4548855707568490.575943827490526
AZA vs. DISU0.4251702272103660.09320110657572240.627754012744611
AZA vs. IL70.5397798372850340.005218939861295510.2228472536241
AZA vs. SAHA-0.413009314114230.09194232488790810.381485991015779
DISU vs. CD30.1658058539734570.6490448559649110.750226375187108
DISU vs. IL70.1055890805997150.6751215025689520.911468444494621
DISU vs. SAHA-0.8372633996272150.004335552580251980.0581844282608883
DMSO vs. AZA-0.05795275817520530.7878644614798241
DMSO vs. CD3-0.3170531402059360.3262662374268840.4396029753006
DMSO vs. DISU-0.4852676721861080.04712116744111030.432781736946112
DMSO vs. IL70.6050126234033060.0008246172281182180.0499503688848944
DMSO vs. SAHA-0.3618387620450890.1264519836426970.424539506678345
HIV vs. Mock in Activation-0.2387771156856410.7016207583282270.999983755607037
HIV vs. Mock in Latency-0.01480358940673710.9285856072104820.999834320637052
IL7 vs. CD30.3013158820533090.3488920069257930.486046479021758
SAHA vs. CD3-0.6849291631758660.05393434302768610.10552980387266
SAHA vs. IL7-0.9564903644644289.82424770503698e-050.0019327964587168
(2). Iglesias-Ussel et al., J. Virol., 2013

Up and Downregulated transcripts during Latency (Latently infected CD4+ T cells vs Uninfected)- Primary CD4+Tcell based model
Log2 Fold Change P Value
unknown unknown

Gene expression during HIV infection and replication

(1). Imbeault et al., PloS Pathog., 2012

Transcriptomic profiling of HIV-1 infected CD4+ T cells - Primary CD4+ T cells
Experiment type Log2 Fold Change P Value Adjusted P Value
Infected vs. Mock unknown unknown unknown
Infected vs. Bystander unknown unknown unknown
(2). Lefebvre et al., J. Virol., 2011

Transcriptome analysis of T-cell line (Sup T1)
Log2 Fold Change unknown
(3). Li et al., J. Immunol., 2013

Lymphatic tissue
Acute Fold Change Acute P Value Asymt Fold Change Asypt P Value AIDS Fold Change AIDS P Value
unknown unknown unknown unknown unknown unknown
(4). Chang et al., MBio., 2011

Transcriptome analysis of T-cell line (Sup T1)

Derived from Sherrill-Mix et al., BMC Retrovirol., 2015 cross validation
Up-regulated (True) TRUE
(5). Sherrill-Mix et al., BMC Retrovirol., 2015

Deep RNA-seq analysis of primary human T cell infected with low passage HIV isolate HIV89.6 - Primary CD4+ T cell based
Test Status Log2 Fold Change P Value
OK 0.0201867 0.922953
(6). Rotger et al., PLoS Pathog., 2010

Genome-wide mRNA expression of CD4+ T cells from HIV-infected patient
(Genes differentially expressed (at adjusted p<0.01) according to the empirical Bayes approach)
Log2 Fold Change P Value
unknown unknown

Proteomic/Transcriptomics studies indicating differentially expressed genes mediated by HIV

(1). Greenwood et al., Elife, 2016

Activated (CD3/CD28) Primary human CD4+ T cells infected with pNL4-3-dE-EGFP. The table shows the complete (unfiltered) TMT (tandem mass tag)-based proteomic time course dataset
6 h 24 h 48 h 72 h RTi
0.994 1.128 0.676 0.576 1.13
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
unknown unknown unknown unknown unknown unknown unknown
(3). Hyrcza et al., J. Virolo., 2007

Primary human CD4+ and CD8+ T Cells
Affymetrix Prob ID Fold Change In CD8? Category
201925_s_at 1.69 No downregulated in CD8+ cells

Protein Overview       top

Drug-protein Interaction       (annotations from DrugBank)      top

Drugbank ID Drug Name Drug Status Pharmacological Action Drug Action
DB00446 Chloramphenicol approved, vet_approved unknown other

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1H03 X-ray 1.7Å P/Q=161-285.
1H04 X-ray 2.0Å P=161-285.
1H2P X-ray 2.8Å P=161-285.
1H2Q X-ray 3.0Å P=161-285.
1M11 EM 16.0Å R=35-277.
1NWV NMR - A=96-222.
1OJV X-ray 2.3Å A/B=35-285.
1OJW X-ray 2.3Å A/B=35-285.
1OJY X-ray 2.6Å A/B/C/D=35-285.
1OK1 X-ray 2.6Å A/B=35-285.
1OK2 X-ray 2.5Å A/B=35-285.
1OK3 X-ray 2.2Å A/B=35-285.
1OK9 X-ray 3.0Å A/B=35-285.
1UOT X-ray 3.0Å P=161-285.
1UPN EM 16.0Å E=157-285.
2C8I EM 14.0Å E=35-285.
2QZD EM - A=222-285.
2QZF EM - A=35-94.
2QZH EM 14.0Å A=96-222.
3IYP EM - F=1-381.
3J24 EM 9.0Å B=35-285.
5FOA X-ray 4.1Å E/F=97-285.

HIV-1 Interaction       (annotations from NCBI HIV-1 Interaction Database)      top

HIV Partner Interaction Type PubMed
Pr55(Gag) recruits 20727121
22830021
Envelope surface glycoprotein gp160; precursor co-localizes with 25759385
Envelope surface glycoprotein gp120 interacts with 7535292
8887350
24639397
Pr55(Gag) co-localizes with 25759385

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa04610 Complement and coagulation cascades - Homo sapiens (human)
hsa04640 Hematopoietic cell lineage - Homo sapiens (human)
hsa05416 Viral myocarditis - Homo sapiens (human)
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