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P08174

- DAF_HUMAN

UniProt

P08174 - DAF_HUMAN

Protein

Complement decay-accelerating factor

Gene

CD55

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 4 (01 Mar 2005)
      Previous versions | rss
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    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. protein binding Source: UniProt
    4. 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

    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: UniProt
    6. integral component of plasma membrane Source: ProtInc
    7. membrane raft Source: UniProtKB
    8. plasma membrane Source: UniProt

    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

    ArrayExpressiP08174.
    BgeeiP08174.
    CleanExiHS_CD55.
    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. 21 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.
    HOGENOMiHOG000237360.
    HOVERGENiHBG001406.
    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: P08174-1) [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

    MTVARPSVPA ALPLLGELPR LLLLVLLCLP AVWGDCGLPP DVPNAQPALE    50
    GRTSFPEDTV ITYKCEESFV KIPGEKDSVI CLKGSQWSDI EEFCNRSCEV 100
    PTRLNSASLK QPYITQNYFP VGTVVEYECR PGYRREPSLS PKLTCLQNLK 150
    WSTAVEFCKK KSCPNPGEIR NGQIDVPGGI LFGATISFSC NTGYKLFGST 200
    SSFCLISGSS VQWSDPLPEC REIYCPAPPQ IDNGIIQGER DHYGYRQSVT 250
    YACNKGFTMI GEHSIYCTVN NDEGEWSGPP PECRGKSLTS KVPPTVQKPT 300
    TVNVPTTEVS PTSQKTTTKT TTPNAQATRS TPVSRTTKHF HETTPNKGSG 350
    TTSGTTRLLS GHTCFTLTGL LGTLVTMGLL T 381
    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_000574.3. [P08174-1]
    NP_001108224.1. NM_001114752.1. [P08174-2]
    UniGeneiHs.126517.

    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]

    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_000574.3. [P08174-1 ]
    NP_001108224.1. NM_001114752.1. [P08174-2 ]
    UniGenei Hs.126517.

    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. 21 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 ]

    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.
    HOGENOMi HOG000237360.
    HOVERGENi HBG001406.
    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

    ArrayExpressi P08174.
    Bgeei P08174.
    CleanExi HS_CD55.
    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

    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 1, 2014
    This is version 172 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

    Dasty 3