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Complement receptor type 2 (Cr2) (Complement C3d receptor) (Epstein-Barr virus receptor) (EBV receptor) (CD antigen CD21)

 CR2_HUMAN               Reviewed;        1033 AA.
P20023; C9JHD2; Q13866; Q14212; Q53EL2; Q5BKT9; Q5SR46; Q5SR48;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
12-SEP-2018, entry version 194.
RecName: Full=Complement receptor type 2;
Short=Cr2;
AltName: Full=Complement C3d receptor;
AltName: Full=Epstein-Barr virus receptor;
Short=EBV receptor;
AltName: CD_antigen=CD21;
Flags: Precursor;
Name=CR2; Synonyms=C3DR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT GLU-1003.
PubMed=2563370;
Fujisaku A., Harley J.B., Frank M.B., Gruner B.A., Frazier B.,
Holers V.M.;
"Genomic organization and polymorphisms of the human C3d/Epstein-Barr
virus receptor.";
J. Biol. Chem. 264:2118-2125(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-993.
TISSUE=B-cell;
PubMed=2832506; DOI=10.1084/jem.167.3.1047;
Weis J.J., Toothaker L.E., Smith J.A., Weis J.H., Fearon D.T.;
"Structure of the human B lymphocyte receptor for C3d and the Epstein-
Barr virus and relatedness to other members of the family of C3/C4
binding proteins.";
J. Exp. Med. 167:1047-1066(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND VARIANT GLU-1003.
PubMed=2827171; DOI=10.1073/pnas.84.24.9194;
Moore M., Cooper N., Tack B., Nemerow G.;
"Molecular cloning of the cDNA encoding the Epstein-Barr virus.C3d
receptor (complement receptor type 2) of human b lymphocytes.";
Proc. Natl. Acad. Sci. U.S.A. 84:9194-9198(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C AND D).
PubMed=10068037; DOI=10.1016/S0161-5890(98)00098-4;
Barel M., Balbo M., Frade R.;
"Evidence for a new transcript of the Epstein-Barr virus/C3d receptor
(CR2, CD21) which is due to alternative exon usage.";
Mol. Immunol. 35:1025-1031(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
TISSUE=Spleen;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[8]
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C), AND VARIANT
ASN-639.
TISSUE=Lymph;
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).
[10]
PROTEIN SEQUENCE OF 226-233; 256-267; 332-341; 667-677 AND 898-908.
PubMed=3016712; DOI=10.1073/pnas.83.15.5639;
Weis J.J., Fearon D.T., Klickstein L.B., Wong W.W., Richards S.A.,
de Bruyn Kops A., Smith J.A., Weis J.H.;
"Identification of a partial cDNA clone for the C3d/Epstein-Barr virus
receptor of human B lymphocytes: homology with the receptor for
fragments C3b and C4b of the third and fourth components of
complement.";
Proc. Natl. Acad. Sci. U.S.A. 83:5639-5643(1986).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 492-556 (ISOFORM B).
PubMed=8390533;
Sinha S.K., Todd S.C., Hedrick J.A., Speiser C.L., Lambris J.D.,
Tsoukas C.D.;
"Characterization of the EBV/C3d receptor on the human Jurkat T cell
line: evidence for a novel transcript.";
J. Immunol. 150:5311-5320(1993).
[12]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR
VIRUS GP350 PROTEIN.
PubMed=2460635;
Tanner J., Whang Y., Sample J., Sears A., Kieff E.;
"Soluble gp350/220 and deletion mutant glycoproteins block Epstein-
Barr virus adsorption to lymphocytes.";
J. Virol. 62:4452-4464(1988).
[13]
FUNCTION AS A RECEPTOR FOR HNRNPU.
PubMed=7753047; DOI=10.1016/0161-5890(95)00005-Y;
Barel M., Balbo M., Gauffre A., Frade R.;
"Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21)
for its three intracellular ligands, the p53 anti-oncoprotein, the p68
calcium binding protein and the nuclear p120 ribonucleoprotein.";
Mol. Immunol. 32:389-397(1995).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-623.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[15]
INVOLVEMENT IN CVID7.
PubMed=22035880; DOI=10.1016/j.jaci.2011.09.027;
Thiel J., Kimmig L., Salzer U., Grudzien M., Lebrecht D., Hagena T.,
Draeger R., Volxen N., Bergbreiter A., Jennings S., Gutenberger S.,
Aichem A., Illges H., Hannan J.P., Kienzler A.K., Rizzi M., Eibel H.,
Peter H.H., Warnatz K., Grimbacher B., Rump J.A., Schlesier M.;
"Genetic CD21 deficiency is associated with hypogammaglobulinemia.";
J. Allergy Clin. Immunol. 129:801-810(2012).
[16]
X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 21-153 IN COMPLEX WITH C3D,
AND DISULFIDE BONDS.
PubMed=11387479; DOI=10.1126/science.1059118;
Szakonyi G., Guthridge J.M., Li D., Young K., Holers V.M., Chen X.S.;
"Structure of complement receptor 2 in complex with its C3d ligand.";
Science 292:1725-1728(2001).
[17]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-148, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-121 AND ASN-127.
PubMed=12122212; DOI=10.1073/pnas.162360499;
Prota A.E., Sage D.R., Stehle T., Fingeroth J.D.;
"The crystal structure of human CD21: Implications for Epstein-Barr
virus and C3d binding.";
Proc. Natl. Acad. Sci. U.S.A. 99:10641-10646(2002).
[18]
X-RAY SCATTERING SOLUTION STRUCTURE OF 21-971.
PubMed=16950392; DOI=10.1016/j.jmb.2006.08.012;
Gilbert H.E., Asokan R., Holers V.M., Perkins S.J.;
"The 15 SCR flexible extracellular domains of human complement
receptor type 2 can mediate multiple ligand and antigen
interactions.";
J. Mol. Biol. 362:1132-1147(2006).
[19]
X-RAY CRYSTALLOGRAPHY (3.16 ANGSTROMS) OF 996-1303 IN COMPLEX WITH C3,
INTERACTION WITH CR2, DISULFIDE BONDS, AND MUTAGENESIS OF ARG-103;
ASP-112 AND LYS-128.
PubMed=21527715; DOI=10.1126/science.1201954;
van den Elsen J.M., Isenman D.E.;
"A crystal structure of the complex between human complement receptor
2 and its ligand C3d.";
Science 332:608-611(2011).
[20]
VARIANT ASN-639, AND INVOLVEMENT IN SLEB9.
PubMed=17360460; DOI=10.1073/pnas.0609101104;
Wu H., Boackle S.A., Hanvivadhanakul P., Ulgiati D., Grossman J.M.,
Lee Y., Shen N., Abraham L.J., Mercer T.R., Park E., Hebert L.A.,
Rovin B.H., Birmingham D.J., Chang D.-M., Chen C.J., McCurdy D.,
Badsha H.M., Thong B.Y.H., Chng H.H., Arnett F.C., Wallace D.J.,
Yu C.Y., Hahn B.H., Cantor R.M., Tsao B.P.;
"Association of a common complement receptor 2 haplotype with
increased risk of systemic lupus erythematosus.";
Proc. Natl. Acad. Sci. U.S.A. 104:3961-3966(2007).
-!- FUNCTION: Receptor for complement C3Dd, for the Epstein-Barr virus
on human B-cells and T-cells and for HNRNPU (PubMed:7753047).
Participates in B lymphocytes activation (PubMed:7753047).
{ECO:0000269|PubMed:7753047}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Epstein-
Barr virus. {ECO:0000269|PubMed:2460635}.
-!- SUBUNIT: Interacts (via Sushi domain 1 and 2) with C3dg.
{ECO:0000269|PubMed:11387479, ECO:0000269|PubMed:21527715}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
gp350 protein. {ECO:0000269|PubMed:2460635}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=A;
IsoId=P20023-1; Sequence=Displayed;
Name=B;
IsoId=P20023-2; Sequence=VSP_001208, VSP_001209;
Name=C;
IsoId=P20023-3; Sequence=VSP_001210;
Note=Ref.3 (AAA35784) sequence is in conflict in position:
663:S->P. {ECO:0000305};
Name=D;
IsoId=P20023-4; Sequence=VSP_001210, VSP_001211;
-!- TISSUE SPECIFICITY: Mature B-lymphocytes, T-lymphocytes,
pharyngeal epithelial cells, astrocytes and follicular dendritic
cells of the spleen.
-!- DISEASE: Systemic lupus erythematosus 9 (SLEB9) [MIM:610927]: A
chronic, relapsing, inflammatory, and often febrile multisystemic
disorder of connective tissue, characterized principally by
involvement of the skin, joints, kidneys and serosal membranes. It
is of unknown etiology, but is thought to represent a failure of
the regulatory mechanisms of the autoimmune system. The disease is
marked by a wide range of system dysfunctions, an elevated
erythrocyte sedimentation rate, and the formation of LE cells in
the blood or bone marrow. {ECO:0000269|PubMed:17360460}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Immunodeficiency, common variable, 7 (CVID7)
[MIM:614699]: A primary immunodeficiency characterized by antibody
deficiency, hypogammaglobulinemia, recurrent bacterial infections
and an inability to mount an antibody response to antigen. The
defect results from a failure of B-cell differentiation and
impaired secretion of immunoglobulins; the numbers of circulating
B-cells is usually in the normal range, but can be low.
{ECO:0000269|PubMed:22035880}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the receptors of complement activation
(RCA) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA35784.1; Type=Frameshift; Positions=758, 769, 776; Evidence={ECO:0000305};
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EMBL; M26004; AAA35786.1; -; mRNA.
EMBL; M26016; AAB04638.1; -; Genomic_DNA.
EMBL; M24007; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M24008; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M24009; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M24010; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M24011; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M26009; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M26010; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M26011; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M26012; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M26013; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M26014; AAB04638.1; JOINED; Genomic_DNA.
EMBL; M26015; AAB04638.1; JOINED; Genomic_DNA.
EMBL; Y00649; CAA68674.1; -; mRNA.
EMBL; J03565; AAA35784.1; ALT_FRAME; mRNA.
EMBL; AK223627; BAD97347.1; -; mRNA.
EMBL; AK301496; BAG63007.1; -; mRNA.
EMBL; EF064746; ABK41929.1; -; Genomic_DNA.
EMBL; AL391597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL691452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC090937; AAH90937.1; -; mRNA.
EMBL; BC136394; AAI36395.1; -; mRNA.
EMBL; S62696; AAB27186.1; -; mRNA.
CCDS; CCDS1478.1; -. [P20023-1]
CCDS; CCDS31007.1; -. [P20023-3]
PIR; JL0028; PL0009.
RefSeq; NP_001006659.1; NM_001006658.2. [P20023-3]
RefSeq; NP_001868.2; NM_001877.4. [P20023-1]
UniGene; Hs.445757; -.
PDB; 1GHQ; X-ray; 2.04 A; B/C=21-153.
PDB; 1LY2; X-ray; 1.80 A; A=22-148.
PDB; 1W2R; X-ray; -; A=21-153.
PDB; 1W2S; X-ray; -; B=21-153.
PDB; 2ATY; X-ray; -; A/B=21-153.
PDB; 2GSX; X-ray; -; A=21-971.
PDB; 3OED; X-ray; 3.16 A; C/D=20-153.
PDBsum; 1GHQ; -.
PDBsum; 1LY2; -.
PDBsum; 1W2R; -.
PDBsum; 1W2S; -.
PDBsum; 2ATY; -.
PDBsum; 2GSX; -.
PDBsum; 3OED; -.
ProteinModelPortal; P20023; -.
SMR; P20023; -.
BioGrid; 107771; 7.
CORUM; P20023; -.
IntAct; P20023; 1.
iPTMnet; P20023; -.
PhosphoSitePlus; P20023; -.
BioMuta; CR2; -.
DMDM; 215273962; -.
PeptideAtlas; P20023; -.
PRIDE; P20023; -.
ProteomicsDB; 53712; -.
ProteomicsDB; 53713; -. [P20023-2]
ProteomicsDB; 53714; -. [P20023-3]
ProteomicsDB; 53715; -. [P20023-4]
Ensembl; ENST00000367057; ENSP00000356024; ENSG00000117322. [P20023-3]
Ensembl; ENST00000367058; ENSP00000356025; ENSG00000117322. [P20023-1]
GeneID; 1380; -.
KEGG; hsa:1380; -.
UCSC; uc001hfv.4; human. [P20023-1]
CTD; 1380; -.
DisGeNET; 1380; -.
EuPathDB; HostDB:ENSG00000117322.16; -.
GeneCards; CR2; -.
GeneReviews; CR2; -.
HGNC; HGNC:2336; CR2.
HPA; CAB002659; -.
HPA; HPA052942; -.
HPA; HPA060715; -.
MalaCards; CR2; -.
MIM; 120650; gene.
MIM; 610927; phenotype.
MIM; 614699; phenotype.
neXtProt; NX_P20023; -.
OpenTargets; ENSG00000117322; -.
Orphanet; 1572; Common variable immunodeficiency.
Orphanet; 536; Systemic lupus erythematosus.
PharmGKB; PA26857; -.
GeneTree; ENSGT00760000118803; -.
HOGENOM; HOG000111964; -.
HOVERGEN; HBG005399; -.
InParanoid; P20023; -.
KO; K04012; -.
OMA; PEVKHGY; -.
OrthoDB; EOG091G0054; -.
PhylomeDB; P20023; -.
TreeFam; TF316872; -.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SIGNOR; P20023; -.
ChiTaRS; CR2; human.
EvolutionaryTrace; P20023; -.
GeneWiki; Complement_receptor_2; -.
GenomeRNAi; 1380; -.
PRO; PR:P20023; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117322; Expressed in 88 organ(s), highest expression level in vermiform appendix.
CleanEx; HS_CR2; -.
ExpressionAtlas; P20023; baseline and differential.
Genevisible; P20023; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0001848; F:complement binding; IDA:UniProtKB.
GO; GO:0004875; F:complement receptor activity; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IDA:UniProtKB.
GO; GO:0042100; P:B cell proliferation; IDA:UniProtKB.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
CDD; cd00033; CCP; 13.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00084; Sushi; 13.
SMART; SM00032; CCP; 14.
SUPFAM; SSF57535; SSF57535; 15.
PROSITE; PS50923; SUSHI; 15.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complement pathway;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Immunity; Innate immunity; Membrane;
Polymorphism; Receptor; Reference proteome; Repeat; Signal; Sushi;
Systemic lupus erythematosus; Transmembrane; Transmembrane helix.
SIGNAL 1 20
CHAIN 21 1033 Complement receptor type 2.
/FTId=PRO_0000006010.
TOPO_DOM 21 971 Extracellular. {ECO:0000255}.
TRANSMEM 972 999 Helical. {ECO:0000255}.
TOPO_DOM 1000 1033 Cytoplasmic. {ECO:0000255}.
DOMAIN 21 84 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 89 148 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 152 212 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 213 273 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 274 344 Sushi 5. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 349 408 Sushi 6. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 409 468 Sushi 7. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 469 524 Sushi 8. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 525 595 Sushi 9. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 600 659 Sushi 10. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 660 716 Sushi 11. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 717 781 Sushi 12. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 786 845 Sushi 13. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 849 909 Sushi 14. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 910 970 Sushi 15. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12122212}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12122212}.
CARBOHYD 294 294 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 372 372 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 492 492 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 623 623 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 682 682 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 800 800 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 823 823 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 861 861 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 911 911 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 23 65
DISULFID 51 82
DISULFID 91 132
DISULFID 118 146
DISULFID 154 197 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 183 210 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 215 256 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 242 271 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 276 325 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 305 342 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 351 393 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 379 406 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 410 453 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 439 466 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 471 509 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 495 522 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 527 576 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 556 593 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 602 644 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 630 657 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 662 699 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 685 714 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 719 762 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 748 779 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 788 830 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 816 843 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 851 894 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 880 907 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 912 955 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 941 968 {ECO:0000255|PROSITE-ProRule:PRU00302}.
VAR_SEQ 499 524 Missing (in isoform B).
{ECO:0000303|PubMed:8390533}.
/FTId=VSP_001208.
VAR_SEQ 525 556 ITCPPPPVIYNGAHTGSSLEDFPYGTTVTYTC -> NHLPT
TPCYLQWGTHREFLRRFSIWNHGHLHM (in isoform
B). {ECO:0000303|PubMed:8390533}.
/FTId=VSP_001209.
VAR_SEQ 659 659 K -> KGCQSPPGLHHGRHTGGNTVFFVSGMTVDYTCDPGY
LLVGNKSIHCMPSGNWSPSAPRCE (in isoform C
and isoform D).
{ECO:0000303|PubMed:10068037,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2827171,
ECO:0000303|Ref.6}.
/FTId=VSP_001210.
VAR_SEQ 716 723 Missing (in isoform D).
{ECO:0000303|PubMed:10068037}.
/FTId=VSP_001211.
VARIANT 639 639 S -> N (in dbSNP:rs17615).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17360460}.
/FTId=VAR_016164.
VARIANT 993 993 I -> V (in dbSNP:rs17618).
{ECO:0000269|PubMed:2832506}.
/FTId=VAR_016165.
VARIANT 1003 1003 A -> E (in dbSNP:rs17617).
{ECO:0000269|PubMed:2563370,
ECO:0000269|PubMed:2827171}.
/FTId=VAR_016166.
MUTAGEN 103 103 R->A: No effect on affinity for C3.
{ECO:0000269|PubMed:21527715}.
MUTAGEN 112 112 D->A: Reduced affinity for C3.
{ECO:0000269|PubMed:21527715}.
MUTAGEN 128 128 K->A: Strongly reduced affinity for C3.
{ECO:0000269|PubMed:21527715}.
CONFLICT 457 457 Missing (in Ref. 2; CAA68674).
{ECO:0000305}.
CONFLICT 646 646 A -> R (in Ref. 3; AAA35784).
{ECO:0000305}.
CONFLICT 667 667 Q -> D (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 774 774 G -> E (in Ref. 3; AAA35784).
{ECO:0000305}.
CONFLICT 783 787 PPVTR -> L (in Ref. 3; AAA35784).
{ECO:0000305}.
CONFLICT 844 844 I -> M (in Ref. 1; AAA35786/AAB04638).
{ECO:0000305}.
CONFLICT 886 886 L -> V (in Ref. 3; AAA35784).
{ECO:0000305}.
CONFLICT 890 890 A -> P (in Ref. 3; AAA35784).
{ECO:0000305}.
CONFLICT 902 902 Q -> G (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 906 906 H -> L (in Ref. 10; AA sequence).
{ECO:0000305}.
STRAND 32 34 {ECO:0000244|PDB:1LY2}.
STRAND 39 42 {ECO:0000244|PDB:1LY2}.
STRAND 46 51 {ECO:0000244|PDB:1LY2}.
STRAND 55 59 {ECO:0000244|PDB:1LY2}.
STRAND 61 66 {ECO:0000244|PDB:1LY2}.
STRAND 68 72 {ECO:0000244|PDB:1LY2}.
STRAND 74 77 {ECO:0000244|PDB:1LY2}.
STRAND 81 84 {ECO:0000244|PDB:1LY2}.
STRAND 99 103 {ECO:0000244|PDB:1LY2}.
STRAND 106 109 {ECO:0000244|PDB:1LY2}.
STRAND 113 118 {ECO:0000244|PDB:1LY2}.
STRAND 122 126 {ECO:0000244|PDB:1LY2}.
STRAND 128 132 {ECO:0000244|PDB:1LY2}.
STRAND 136 141 {ECO:0000244|PDB:1LY2}.
STRAND 145 148 {ECO:0000244|PDB:1LY2}.
SEQUENCE 1033 AA; 112916 MW; 7D89DB4A07847E9A CRC64;
MGAAGLLGVF LALVAPGVLG ISCGSPPPIL NGRISYYSTP IAVGTVIRYS CSGTFRLIGE
KSLLCITKDK VDGTWDKPAP KCEYFNKYSS CPEPIVPGGY KIRGSTPYRH GDSVTFACKT
NFSMNGNKSV WCQANNMWGP TRLPTCVSVF PLECPALPMI HNGHHTSENV GSIAPGLSVT
YSCESGYLLV GEKIINCLSS GKWSAVPPTC EEARCKSLGR FPNGKVKEPP ILRVGVTANF
FCDEGYRLQG PPSSRCVIAG QGVAWTKMPV CEEIFCPSPP PILNGRHIGN SLANVSYGSI
VTYTCDPDPE EGVNFILIGE STLRCTVDSQ KTGTWSGPAP RCELSTSAVQ CPHPQILRGR
MVSGQKDRYT YNDTVIFACM FGFTLKGSKQ IRCNAQGTWE PSAPVCEKEC QAPPNILNGQ
KEDRHMVRFD PGTSIKYSCN PGYVLVGEES IQCTSEGVWT PPVPQCKVAA CEATGRQLLT
KPQHQFVRPD VNSSCGEGYK LSGSVYQECQ GTIPWFMEIR LCKEITCPPP PVIYNGAHTG
SSLEDFPYGT TVTYTCNPGP ERGVEFSLIG ESTIRCTSND QERGTWSGPA PLCKLSLLAV
QCSHVHIANG YKISGKEAPY FYNDTVTFKC YSGFTLKGSS QIRCKADNTW DPEIPVCEKE
TCQHVRQSLQ ELPAGSRVEL VNTSCQDGYQ LTGHAYQMCQ DAENGIWFKK IPLCKVIHCH
PPPVIVNGKH TGMMAENFLY GNEVSYECDQ GFYLLGEKKL QCRSDSKGHG SWSGPSPQCL
RSPPVTRCPN PEVKHGYKLN KTHSAYSHND IVYVDCNPGF IMNGSRVIRC HTDNTWVPGV
PTCIKKAFIG CPPPPKTPNG NHTGGNIARF SPGMSILYSC DQGYLLVGEA LLLCTHEGTW
SQPAPHCKEV NCSSPADMDG IQKGLEPRKM YQYGAVVTLE CEDGYMLEGS PQSQCQSDHQ
WNPPLAVCRS RSLAPVLCGI AAGLILLTFL IVITLYVISK HRARNYYTDT SQKEAFHLEA
REVYSVDPYN PAS


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