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Complement decay-accelerating factor (CD antigen CD55)

 DAF_HUMAN               Reviewed;         381 AA.
P08174; B1AP14; D3DT83; D3DT84; E7ER69; P09679; P78361; Q14UF2;
Q14UF3; Q14UF4; Q14UF5; Q14UF6;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 4.
25-OCT-2017, entry version 203.
RecName: Full=Complement decay-accelerating factor;
AltName: CD_antigen=CD55;
Flags: Precursor;
Name=CD55; Synonyms=CR, DAF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=2433596; DOI=10.1038/325545a0;
Caras I.W., Davitz M.A., Rhee L., Weddell G., Martin D.W. Jr.,
Nussenzweig V.;
"Cloning of decay-accelerating factor suggests novel use of splicing
to generate two proteins.";
Nature 325:545-549(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), AND
SUBCELLULAR LOCATION (ISOFORMS 3; 4; 5; 6 AND 7).
TISSUE=Lung;
PubMed=16503113; DOI=10.1016/j.ygeno.2006.01.006;
Osuka F., Endo Y., Higuchi M., Suzuki H., Shio Y., Fujiu K., Kanno R.,
Oishi A., Terashima M., Fujita T., Gotoh M.;
"Molecular cloning and characterization of novel splicing variants of
human decay-accelerating factor.";
Genomics 88:316-322(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-52.
SeattleSNPs variation discovery resource;
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
PubMed=1711208; DOI=10.1073/pnas.88.11.4675;
Ewulonu U.K., Ravi L., Medof M.E.;
"Characterization of the decay-accelerating factor gene promoter
region.";
Proc. Natl. Acad. Sci. U.S.A. 88:4675-4679(1991).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-381 (ISOFORM 2).
PubMed=2436222; DOI=10.1073/pnas.84.7.2007;
Medof M.E., Lublin D.M., Holers V.M., Ayers D.J., Getty R.R.,
Leykam J.F., Atkinson J.P., Tykocinski M.L.;
"Cloning and characterization of cDNAs encoding the complete sequence
of decay-accelerating factor of human complement.";
Proc. Natl. Acad. Sci. U.S.A. 84:2007-2011(1987).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 35-381 (ISOFORM 2).
TISSUE=Hippocampus;
Kumar V.B., Hyung C., Nakra R., Walters M., Sasser T., Bernardo A.;
"Decay-acceleration factor (DAF; CD 55) in the brain of Alzheimer's
disease patients.";
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 35-63.
PubMed=2428813; DOI=10.1093/oxfordjournals.jbchem.a121686;
Sugita Y., Negoro T., Matsuda T., Sakamoto T., Tomita M.;
"Improved method for the isolation and preliminary characterization of
human DAF (decay-accelerating factor).";
J. Biochem. 100:143-150(1986).
[12]
PROTEIN SEQUENCE OF 35-46.
TISSUE=Urine;
PubMed=1712233; DOI=10.1016/0304-4165(91)90171-C;
Nakano Y., Sugita Y., Ishikawa Y., Choi N.-H., Tobe T., Tomita M.;
"Isolation of two forms of decay-accelerating factor (DAF) from human
urine.";
Biochim. Biophys. Acta 1074:326-330(1991).
[13]
GPI-ANCHOR AT SER-353.
PubMed=1824699;
Moran P., Raab H., Kohr W.J., Caras I.W.;
"Glycophospholipid membrane anchor attachment. Molecular analysis of
the cleavage/attachment site.";
J. Biol. Chem. 266:1250-1257(1991).
[14]
DISULFIDE BONDS IN SUSHI DOMAINS.
PubMed=1377029; DOI=10.1016/0304-4165(92)90016-N;
Nakano Y., Sumida K., Kikuta N., Miura N.-H., Tobe T., Tomita M.;
"Complete determination of disulfide bonds localized within the short
consensus repeat units of decay accelerating factor (CD55 antigen).";
Biochim. Biophys. Acta 1116:235-240(1992).
[15]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ECHOVIRUS CAPSID
PROTEINS.
PubMed=7525274;
Ward T., Pipkin P.A., Clarkson N.A., Stone D.M., Minor P.D.,
Almond J.W.;
"Decay-accelerating factor CD55 is identified as the receptor for
echovirus 7 using CELICS, a rapid immuno-focal cloning method.";
EMBO J. 13:5070-5074(1994).
[16]
INTERACTION WITH HUMAN ECHOVIRUSES 6/7/11/12/20/21 CAPSID PROTEINS.
PubMed=7517044; DOI=10.1073/pnas.91.13.6245;
Bergelson J.M., Chan M., Solomon K.R., St John N.F., Lin H.,
Finberg R.W.;
"Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-
anchored complement regulatory protein, is a receptor for several
echoviruses.";
Proc. Natl. Acad. Sci. U.S.A. 91:6245-6248(1994).
[17]
INTERACTION WITH COXSACKIEVIRUSES B1/B3/B5 CAPSID PROTEINS.
PubMed=7538177;
Shafren D.R., Bates R.C., Agrez M.V., Herd R.L., Burns G.F.,
Barry R.D.;
"Coxsackieviruses B1, B3, and B5 use decay accelerating factor as a
receptor for cell attachment.";
J. Virol. 69:3873-3877(1995).
[18]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ENTEROVIRUS
70 CAPSID PROTEINS.
PubMed=8764022;
Karnauchow T.M., Tolson D.L., Harrison B.A., Altman E., Lublin D.M.,
Dimock K.;
"The HeLa cell receptor for enterovirus 70 is decay-accelerating
factor (CD55).";
J. Virol. 70:5143-5152(1996).
[19]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS
A21 CAPSID PROTEINS.
PubMed=9151867;
Shafren D.R., Dorahy D.J., Ingham R.A., Burns G.F., Barry R.D.;
"Coxsackievirus A21 binds to decay-accelerating factor but requires
intercellular adhesion molecule 1 for cell entry.";
J. Virol. 71:4736-4743(1997).
[20]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ENTEROVIRUS D68
CAPSID PROTEINS.
PubMed=12409401; DOI=10.1128/JCM.40.11.4218-4223.2002;
Blomqvist S., Savolainen C., Raman L., Roivainen M., Hovi T.;
"Human rhinovirus 87 and enterovirus 68 represent a unique serotype
with rhinovirus and enterovirus features.";
J. Clin. Microbiol. 40:4218-4223(2002).
[21]
GPI-ANCHOR [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=14517339; DOI=10.1074/mcp.M300079-MCP200;
Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C.,
Jensen O.N.;
"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane
proteins.";
Mol. Cell. Proteomics 2:1261-1270(2003).
[22]
GPI-ANCHOR [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16602701; DOI=10.1021/pr050419u;
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,
Brodbeck U., Peck S.C., Jensen O.N.;
"Modification-specific proteomics of plasma membrane proteins:
identification and characterization of glycosylphosphatidylinositol-
anchored proteins released upon phospholipase D treatment.";
J. Proteome Res. 5:935-943(2006).
[23]
INTERACTION WITH COXSACKIEVIRUS B3 CAPSID PROTEINS.
PubMed=17804498; DOI=10.1128/JVI.00931-07;
Hafenstein S., Bowman V.D., Chipman P.R., Bator Kelly C.M., Lin F.,
Medof M.E., Rossmann M.G.;
"Interaction of decay-accelerating factor with coxsackievirus B3.";
J. Virol. 81:12927-12935(2007).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
GLYCOSYLATION.
PubMed=26207632; DOI=10.1371/journal.pone.0133704;
Mizuhashi K., Chaya T., Kanamoto T., Omori Y., Furukawa T.;
"Obif, a transmembrane protein, is required for bone mineralization
and spermatogenesis in mice.";
PLoS ONE 10:E0133704-E0133704(2015).
[27]
VARIANT BLOOD GROUP DR(A-) LEU-199.
PubMed=7519480;
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.;
"Molecular basis of reduced or absent expression of decay-accelerating
factor in Cromer blood group phenotypes.";
Blood 84:1276-1282(1994).
[28]
VARIANT BLOOD GROUP GUTI(-) HIS-240, AND POLYMORPHISM.
PubMed=12675719; DOI=10.1046/j.1537-2995.2003.00319.x;
Storry J.R., Sausais L., Hue-Roye K., Mudiwa F., Ferrer Z.,
Blajchman M.A., Lublin D.M., Ma B.W., Miquel J.F., Nervi F.,
Pereira J., Reid M.E.;
"GUTI: a new antigen in the Cromer blood group system.";
Transfusion 43:340-344(2003).
[29]
INVOLVEMENT IN BLOOD GROUP INAB.
PubMed=1720702;
Reid M.E., Mallinson G., Sim R.B., Poole J., Pausch V., Merry A.H.,
Liew Y.W., Tanner M.J.A.;
"Biochemical studies on red blood cells from a patient with the Inab
phenotype (decay-accelerating factor deficiency).";
Blood 78:3291-3297(1991).
[30]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 161-285.
PubMed=12499389; DOI=10.1074/jbc.M212561200;
Williams P., Chaudhry Y., Goodfellow I.G., Billington J., Powell R.,
Spiller O.B., Evans D.J., Lea S.;
"Mapping CD55 function. The structure of two pathogen-binding domains
at 1.7 A.";
J. Biol. Chem. 278:10691-10696(2003).
[31]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF OF 35-286.
PubMed=14734808; DOI=10.1073/pnas.0307200101;
Lukacik P., Roversi P., White J., Esser D., Smith G.P., Billington J.,
Williams P.A., Rudd P.M., Wormald M.R., Harvey D.J., Crispin M.D.,
Radcliffe C.M., Dwek R.A., Evans D.J., Morgan B.P., Smith R.A.,
Lea S.M.;
"Complement regulation at the molecular level: the structure of decay-
accelerating factor.";
Proc. Natl. Acad. Sci. U.S.A. 101:1279-1284(2004).
[32]
STRUCTURE BY NMR OF 95-223.
PubMed=12672958; DOI=10.1073/pnas.0730844100;
Uhrinova S., Lin F., Ball G., Bromek K., Uhrin D., Medof M.E.,
Barlow P.N.;
"Solution structure of a functionally active fragment of decay-
accelerating factor.";
Proc. Natl. Acad. Sci. U.S.A. 100:4718-4723(2003).
-!- FUNCTION: This protein recognizes C4b and C3b fragments that
condense with cell-surface hydroxyl or amino groups when nascent
C4b and C3b are locally generated during C4 and c3 activation.
Interaction of daf with cell-associated C4b and C3b polypeptides
interferes with their ability to catalyze the conversion of C2 and
factor B to enzymatically active C2a and Bb and thereby prevents
the formation of C4b2a and C3bBb, the amplification convertases of
the complement cascade. {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}.
-!- SUBUNIT: Monomer (major form) and non-disulfide-linked, covalent
homodimer (minor form). {ECO:0000269|PubMed:1377029,
ECO:0000305|PubMed:12409401}.
-!- SUBUNIT: (Microbial infection) Interacts with coxsackievirus A21,
coxsackieviruses B1, B3 and B5 capsid proteins.
{ECO:0000269|PubMed:9151867}.
-!- SUBUNIT: (Microbial infection) Interacts with human enterovirus 70
and D68 capsid proteins (Probable). {ECO:0000269|PubMed:8764022}.
-!- SUBUNIT: (Microbial infection) Interacts with human echoviruses 6,
7, 11, 12, 20 and 21 capsid proteins.
{ECO:0000269|PubMed:7525274}.
-!- SUBCELLULAR LOCATION: Isoform 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=2; Synonyms=DAF-2;
IsoId=P08174-1; Sequence=Displayed;
Name=1; Synonyms=DAF-1;
IsoId=P08174-2; Sequence=VSP_001200;
Name=3; Synonyms=VDAF3;
IsoId=P08174-3; Sequence=VSP_047636;
Name=4; Synonyms=VDAF2;
IsoId=P08174-4; Sequence=VSP_047637;
Name=5; Synonyms=VDAF1;
IsoId=P08174-5; Sequence=VSP_047638;
Name=6; Synonyms=VDAF4;
IsoId=P08174-6; Sequence=VSP_047635;
Note=Includes partial sequence of the intron 7.;
Name=7; Synonyms=VDAF5;
IsoId=P08174-7; Sequence=VSP_047634;
Note=Includes full sequence of the intron 7.;
-!- TISSUE SPECIFICITY: Expressed on the plasma membranes of all cell
types that are in intimate contact with plasma complement
proteins. It is also found on the surfaces of epithelial cells
lining extracellular compartments, and variants of the molecule
are present in body fluids and in extracellular matrix.
-!- DOMAIN: The first Sushi domain (SCR1) is not necessary for
function. SCR2 and SCR4 provide the proper conformation for the
active site on SCR3 (By similarity). {ECO:0000250}.
-!- PTM: The Ser/Thr-rich domain is heavily O-glycosylated.
{ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:26207632}.
-!- POLYMORPHISM: Responsible for the Cromer blood group system (CROM)
[MIM: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).
{ECO:0000269|PubMed:12675719}.
-!- SIMILARITY: Belongs to the receptors of complement activation
(RCA) family. {ECO:0000305}.
-!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
mutation database;
URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=cromer";
-!- WEB RESOURCE: Name=CD55base; Note=CD55 mutation db;
URL="http://structure.bmc.lu.se/idbase/CD55base/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Decay-accelerating factor
entry;
URL="https://en.wikipedia.org/wiki/Decay_accelerating_factor";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/daf/";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1upn";
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EMBL; M31516; AAA52169.1; -; mRNA.
EMBL; M30142; AAA52168.1; -; mRNA.
EMBL; AB240566; BAE97422.1; -; mRNA.
EMBL; AB240567; BAE97423.1; -; mRNA.
EMBL; AB240568; BAE97424.1; -; mRNA.
EMBL; AB240569; BAE97425.1; -; mRNA.
EMBL; AB240570; BAE97426.1; -; mRNA.
EMBL; BT007159; AAP35823.1; -; mRNA.
EMBL; AY851161; AAW29942.1; -; Genomic_DNA.
EMBL; AL391597; CAH72946.1; -; Genomic_DNA.
EMBL; AL596218; CAH72946.1; JOINED; Genomic_DNA.
EMBL; AL596218; CAI16463.1; -; Genomic_DNA.
EMBL; AL391597; CAI16463.1; JOINED; Genomic_DNA.
EMBL; CH471100; EAW93485.1; -; Genomic_DNA.
EMBL; CH471100; EAW93487.1; -; Genomic_DNA.
EMBL; CH471100; EAW93488.1; -; Genomic_DNA.
EMBL; CH471100; EAW93491.1; -; Genomic_DNA.
EMBL; BC001288; AAH01288.1; -; mRNA.
EMBL; M64653; AAA52170.1; -; Genomic_DNA.
EMBL; M64356; AAA52170.1; JOINED; Genomic_DNA.
EMBL; M15799; AAA52167.1; -; mRNA.
EMBL; U88576; AAB48622.1; -; mRNA.
EMBL; S72858; AAC60633.1; -; Genomic_DNA.
CCDS; CCDS31006.1; -. [P08174-1]
CCDS; CCDS44307.1; -. [P08174-2]
PIR; A26359; A26359.
PIR; B26359; B26359.
RefSeq; NP_000565.1; NM_000574.4. [P08174-1]
RefSeq; NP_001108224.1; NM_001114752.2. [P08174-2]
RefSeq; NP_001287832.1; NM_001300903.1. [P08174-5]
RefSeq; NP_001287833.1; NM_001300904.1. [P08174-3]
UniGene; Hs.126517; -.
UniGene; Hs.609950; -.
PDB; 1H03; X-ray; 1.70 A; P/Q=161-285.
PDB; 1H04; X-ray; 2.00 A; P=161-285.
PDB; 1H2P; X-ray; 2.80 A; P=161-285.
PDB; 1H2Q; X-ray; 3.00 A; P=161-285.
PDB; 1M11; EM; 16.00 A; R=35-277.
PDB; 1NWV; NMR; -; A=96-222.
PDB; 1OJV; X-ray; 2.30 A; A/B=35-285.
PDB; 1OJW; X-ray; 2.30 A; A/B=35-285.
PDB; 1OJY; X-ray; 2.60 A; A/B/C/D=35-285.
PDB; 1OK1; X-ray; 2.60 A; A/B=35-285.
PDB; 1OK2; X-ray; 2.50 A; A/B=35-285.
PDB; 1OK3; X-ray; 2.20 A; A/B=35-285.
PDB; 1OK9; X-ray; 3.00 A; A/B=35-285.
PDB; 1UOT; X-ray; 3.00 A; P=161-285.
PDB; 1UPN; EM; 16.00 A; E=157-285.
PDB; 2C8I; EM; 14.00 A; E=35-285.
PDB; 2QZD; EM; -; A=222-285.
PDB; 2QZF; EM; -; A=35-94.
PDB; 2QZH; EM; 14.00 A; A=96-222.
PDB; 3IYP; EM; -; F=1-381.
PDB; 3J24; EM; 9.00 A; B=35-285.
PDB; 5FOA; X-ray; 4.19 A; E/F=97-285.
PDBsum; 1H03; -.
PDBsum; 1H04; -.
PDBsum; 1H2P; -.
PDBsum; 1H2Q; -.
PDBsum; 1M11; -.
PDBsum; 1NWV; -.
PDBsum; 1OJV; -.
PDBsum; 1OJW; -.
PDBsum; 1OJY; -.
PDBsum; 1OK1; -.
PDBsum; 1OK2; -.
PDBsum; 1OK3; -.
PDBsum; 1OK9; -.
PDBsum; 1UOT; -.
PDBsum; 1UPN; -.
PDBsum; 2C8I; -.
PDBsum; 2QZD; -.
PDBsum; 2QZF; -.
PDBsum; 2QZH; -.
PDBsum; 3IYP; -.
PDBsum; 3J24; -.
PDBsum; 5FOA; -.
ProteinModelPortal; P08174; -.
SMR; P08174; -.
BioGrid; 107974; 26.
IntAct; P08174; 7.
STRING; 9606.ENSP00000316333; -.
DrugBank; DB00446; Chloramphenicol.
iPTMnet; P08174; -.
PhosphoSitePlus; P08174; -.
SwissPalm; P08174; -.
BioMuta; CD55; -.
DMDM; 60416353; -.
MaxQB; P08174; -.
PaxDb; P08174; -.
PeptideAtlas; P08174; -.
PRIDE; P08174; -.
DNASU; 1604; -.
Ensembl; ENST00000314754; ENSP00000316333; ENSG00000196352. [P08174-2]
Ensembl; ENST00000367064; ENSP00000356031; ENSG00000196352. [P08174-1]
GeneID; 1604; -.
KEGG; hsa:1604; -.
UCSC; uc001hfq.5; human. [P08174-1]
CTD; 1604; -.
DisGeNET; 1604; -.
EuPathDB; HostDB:ENSG00000196352.14; -.
GeneCards; CD55; -.
HGNC; HGNC:2665; CD55.
HPA; CAB010454; -.
HPA; HPA002190; -.
HPA; HPA024386; -.
MIM; 125240; gene.
MIM; 613793; phenotype.
neXtProt; NX_P08174; -.
OpenTargets; ENSG00000196352; -.
PharmGKB; PA27137; -.
eggNOG; ENOG410IEGQ; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00900000140846; -.
HOGENOM; HOG000237360; -.
HOVERGEN; HBG001406; -.
InParanoid; P08174; -.
KO; K04006; -.
PhylomeDB; P08174; -.
TreeFam; TF334137; -.
Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SIGNOR; P08174; -.
ChiTaRS; CD55; human.
EvolutionaryTrace; P08174; -.
GeneWiki; Decay-accelerating_factor; -.
GenomeRNAi; 1604; -.
PRO; PR:P08174; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000196352; -.
CleanEx; HS_CD55; -.
ExpressionAtlas; P08174; baseline and differential.
Genevisible; P08174; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IDA:UniProtKB.
GO; GO:0035743; P:CD4-positive, alpha-beta T cell cytokine production; IDA:UniProtKB.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0045916; P:negative regulation of complement activation; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:2000516; P:positive regulation of CD4-positive, alpha-beta T cell activation; IDA:UniProtKB.
GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IDA:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0045730; P:respiratory burst; NAS:UniProtKB.
CDD; cd00033; CCP; 4.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00084; Sushi; 4.
SMART; SM00032; CCP; 4.
SUPFAM; SSF57535; SSF57535; 4.
PROSITE; PS50923; SUSHI; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood group antigen;
Cell membrane; Complement pathway; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
Host cell receptor for virus entry; Host-virus interaction; Immunity;
Innate immunity; Lipoprotein; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal; Sushi.
SIGNAL 1 34 {ECO:0000269|PubMed:1712233,
ECO:0000269|PubMed:2428813}.
CHAIN 35 353 Complement decay-accelerating factor.
/FTId=PRO_0000006000.
PROPEP 354 381 Removed in mature form.
/FTId=PRO_0000006001.
DOMAIN 35 96 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 96 160 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 161 222 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 223 285 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
COMPBIAS 287 356 Ser/Thr-rich.
LIPID 353 353 GPI-anchor amidated serine.
{ECO:0000269|PubMed:1824699}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 36 81 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:1377029}.
DISULFID 65 94 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:1377029}.
DISULFID 98 145 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:1377029}.
DISULFID 129 158 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:1377029}.
DISULFID 163 204 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:1377029}.
DISULFID 190 220 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:1377029}.
DISULFID 225 267 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:1377029}.
DISULFID 253 283 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:1377029}.
VAR_SEQ 326 326 Q -> QGTETPSVLQKHTTENVSATRTPPTPQKPTTVNVPA
TIVTPTPQKPTTINVPATGVSSTPQRHTIVNVSATGTLPTL
QKPTRANDSATKSPAAAQTSFISKTLSTKTPSAAQNPMMTN
ASATQATLTAQKFTTAKVAFTQSPSAARKSTNVHSPVTNGL
KSTQRFPSAHIT (in isoform 7).
{ECO:0000303|PubMed:16503113}.
/FTId=VSP_047634.
VAR_SEQ 327 327 A -> GTETPSVLQKHTTENVSATRTPPTPQKPTTVNVPAT
IVTPTPQKPTTINVPATGVSSTPQRHTIVNVSATGTLPTLQ
KPTRANDSATKSPAAAQTSFISKTLSTKTPSAAQNPMMTNA
SATQATLTAQKFTTAKVAFTQSPSAAP (in isoform
6). {ECO:0000303|PubMed:16503113}.
/FTId=VSP_047635.
VAR_SEQ 361 381 GHTCFTLTGLLGTLVTMGLLT -> ALQVRPFEVSGSSHIS
SKKMMCIL (in isoform 3).
{ECO:0000303|PubMed:16503113}.
/FTId=VSP_047636.
VAR_SEQ 361 381 GHTCFTLTGLLGTLVTMGLLT -> VLFM (in isoform
4). {ECO:0000303|PubMed:16503113}.
/FTId=VSP_047637.
VAR_SEQ 361 381 GHTCFTLTGLLGTLVTMGLLT -> ETVFHRVIQDGLDLLA
SRSACLGLPKCWDYRREPPHLARAHVFHVDRFAWDASNHGL
ADLAKEELRRKYTQVYRLFLVS (in isoform 5).
{ECO:0000303|PubMed:16503113}.
/FTId=VSP_047638.
VAR_SEQ 362 381 HTCFTLTGLLGTLVTMGLLT -> SRPVTQAGMRWCDRSSL
QSRTPGFKRSFHFSLPSSWYYRAHVFHVDRFAWDASNHGLA
DLAKEELRRKYTQVYRLFLVS (in isoform 1).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2433596}.
/FTId=VSP_001200.
VARIANT 52 52 R -> L (in Tc(b) antigen;
dbSNP:rs28371588). {ECO:0000269|Ref.4}.
/FTId=VAR_001997.
VARIANT 52 52 R -> P (in Tc(c) antigen;
dbSNP:rs28371588).
/FTId=VAR_001998.
VARIANT 82 82 L -> R (in WES(a) antigen;
dbSNP:rs147474393).
/FTId=VAR_001999.
VARIANT 199 199 S -> L (in Dr(a-) antigen).
{ECO:0000269|PubMed:7519480}.
/FTId=VAR_002000.
VARIANT 227 227 A -> P (in Cr(a-) antigen;
dbSNP:rs60822373).
/FTId=VAR_002001.
VARIANT 240 240 R -> H (in GUTI(-) antigen;
dbSNP:rs199705465).
{ECO:0000269|PubMed:12675719}.
/FTId=VAR_015884.
CONFLICT 80 80 I -> T (in Ref. 8; AAA52170 and 9;
AAA52167). {ECO:0000305}.
CONFLICT 85 85 S -> M (in Ref. 9; AAA52167).
{ECO:0000305}.
CONFLICT 187 187 S -> T (in Ref. 10; AAB48622).
{ECO:0000305}.
CONFLICT 297 297 Q -> H (in Ref. 10; AAB48622).
{ECO:0000305}.
STRAND 45 47 {ECO:0000244|PDB:1OK3}.
STRAND 60 65 {ECO:0000244|PDB:1OK3}.
STRAND 69 71 {ECO:0000244|PDB:1OJW}.
STRAND 78 82 {ECO:0000244|PDB:1OK3}.
TURN 83 85 {ECO:0000244|PDB:1OK3}.
STRAND 94 98 {ECO:0000244|PDB:1OJW}.
STRAND 105 109 {ECO:0000244|PDB:1OK3}.
HELIX 113 115 {ECO:0000244|PDB:1OK3}.
STRAND 124 129 {ECO:0000244|PDB:1OK3}.
STRAND 133 135 {ECO:0000244|PDB:1OK3}.
STRAND 136 138 {ECO:0000244|PDB:1NWV}.
STRAND 142 145 {ECO:0000244|PDB:1OK3}.
STRAND 149 151 {ECO:0000244|PDB:1OK9}.
STRAND 157 160 {ECO:0000244|PDB:1OK3}.
STRAND 172 175 {ECO:0000244|PDB:1H03}.
TURN 177 180 {ECO:0000244|PDB:1UOT}.
STRAND 185 190 {ECO:0000244|PDB:1H03}.
STRAND 194 198 {ECO:0000244|PDB:1H03}.
STRAND 200 207 {ECO:0000244|PDB:1H03}.
STRAND 210 215 {ECO:0000244|PDB:1H03}.
STRAND 219 222 {ECO:0000244|PDB:1H03}.
STRAND 234 236 {ECO:0000244|PDB:1H03}.
STRAND 241 244 {ECO:0000244|PDB:1H2P}.
STRAND 248 253 {ECO:0000244|PDB:1H03}.
STRAND 258 261 {ECO:0000244|PDB:1H03}.
STRAND 263 270 {ECO:0000244|PDB:1H03}.
STRAND 273 278 {ECO:0000244|PDB:1H03}.
STRAND 282 284 {ECO:0000244|PDB:1H03}.
SEQUENCE 381 AA; 41400 MW; C1CBE5300F60C176 CRC64;
MTVARPSVPA ALPLLGELPR LLLLVLLCLP AVWGDCGLPP DVPNAQPALE GRTSFPEDTV
ITYKCEESFV KIPGEKDSVI CLKGSQWSDI EEFCNRSCEV PTRLNSASLK QPYITQNYFP
VGTVVEYECR PGYRREPSLS PKLTCLQNLK WSTAVEFCKK KSCPNPGEIR NGQIDVPGGI
LFGATISFSC NTGYKLFGST SSFCLISGSS VQWSDPLPEC REIYCPAPPQ IDNGIIQGER
DHYGYRQSVT YACNKGFTMI GEHSIYCTVN NDEGEWSGPP PECRGKSLTS KVPPTVQKPT
TVNVPTTEVS PTSQKTTTKT TTPNAQATRS TPVSRTTKHF HETTPNKGSG TTSGTTRLLS
GHTCFTLTGL LGTLVTMGLL T


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