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UniProtKB/Swiss-Prot entry P17927


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CR1_HUMAN
Primary accession number P17927
Secondary accession numbers Q16745 Q9UQV2
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on November 1, 1990 (Sequence version 1)
Annotations were last modified on    June 10, 2008 (Entry version 99)
Name and origin of the protein
Protein name Complement receptor type 1 [Precursor]
Synonyms C3b/C4b receptor
CD35 antigen
Gene name
Name: CR1
Synonyms: C3BR
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1084/jem.168.5.1699; PubMed=2972794 [NCBI, ExPASy, EBI, Israel, Japan]
Klickstein L.B., Bartow T.J., Miletic V., Rabson L.D., Smith J.A., Fearon D.T.;
"Identification of distinct C3b and C4b recognition sites in the human C3b/C4b receptor (CR1, CD35) by deletion mutagenesis.";
J. Exp. Med. 168:1699-1717(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-1615; ARG-1827 AND ASP-1850.
PubMed=8245463 [NCBI, ExPASy, EBI, Israel, Japan]
Vik D.P., Wong W.W.;
"Structure of the gene for the F allele of complement receptor type 1 and sequence of the coding region unique to the S allele.";
J. Immunol. 151:6214-6224(1993).
[3]
NUCLEOTIDE SEQUENCE OF 1-41.
DOI=10.1084/jem.169.3.847; PubMed=2564414 [NCBI, ExPASy, EBI, Israel, Japan]
Wong W.W., Cahill J.M., Rosen M.D., Kennedy C.A., Bonaccio E.T., Morris M.J., Wilson J.G., Klickstein L.B., Fearon D.T.;
"Structure of the human CR1 gene. Molecular basis of the structural and quantitative polymorphisms and identification of a new CR1-like allele.";
J. Exp. Med. 169:847-863(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 26-584.
DOI=10.1084/jem.168.4.1255; PubMed=2971757 [NCBI, ExPASy, EBI, Israel, Japan]
Hourcade D., Miesner D.R., Atkinson J.P., Holers V.M.;
"Identification of an alternative polyadenylation site in the human C3b/C4b receptor (complement receptor type 1) transcriptional unit and prediction of a secreted form of complement receptor type 1.";
J. Exp. Med. 168:1255-1270(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 503-2039.
DOI=10.1084/jem.165.4.1095; PubMed=2951479 [NCBI, ExPASy, EBI, Israel, Japan]
Klickstein L.B., Wong W.W., Smith J.A., Weis J.H., Wilson J.G., Fearon D.T.;
"Human C3b/C4b receptor (CR1). Demonstration of long homologous repeating domains that are composed of the short consensus repeats characteristics of C3/C4 binding proteins.";
J. Exp. Med. 165:1095-1112(1987).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 761-783; 831-845 AND 1179-1195.
PubMed=2933745 [NCBI, ExPASy, EBI, Israel, Japan]
Wong W.W., Klickstein L.B., Smith J.A., Weis J.H., Fearon D.T.;
"Identification of a partial cDNA clone for the human receptor for complement fragments C3b/C4b.";
Proc. Natl. Acad. Sci. U.S.A. 82:7711-7715(1985).
[7]
VARIANTS ARG-1208; GLU-1590; GLY-1601; THR-1610; VAL-1615; ARG-1827 AND ASP-1850.
DOI=10.1182/blood.V97.9.2879; PubMed=11313284 [NCBI, ExPASy, EBI, Israel, Japan]
Moulds J.M., Zimmerman P.A., Doumbo O.K., Kassambara L., Sagara I., Diallo D.A., Atkinson J.P., Krych-Goldberg M., Hauhart R.E., Hourcade D.E., McNamara D.T., Birmingham D.J., Rowe J.A., Moulds J.J., Miller L.H.;
"Molecular identification of Knops blood group polymorphisms found in long homologous region D of complement receptor 1.";
Blood 97:2879-2885(2001).
[8]
VARIANTS SL(2)/VIL GLY-1601 AND SL(3) THR-1610.
DOI=10.1046/j.1537-2995.2002.00002.x; PubMed=11896343 [NCBI, ExPASy, EBI, Israel, Japan]
Moulds J.M., Zimmerman P.A., Doumbo O.K., Diallo D.A., Atkinson J.P., Krych-Goldberg M., Hourcade D.E., Moulds J.J.;
"Expansion of the Knops blood group system and subdivision of Sl(a).";
Transfusion 42:251-256(2002).
[9]
STRUCTURE BY NMR OF 942-1133.
DOI=10.1016/S0092-8674(02)00672-4; PubMed=11955431 [NCBI, ExPASy, EBI, Israel, Japan]
Smith B.O., Mallin R.L., Krych-Goldberg M., Wang X., Hauhart R.E., Bromek K., Uhrin D., Atkinson J.P., Barlow P.N.;
"Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor.";
Cell 108:769-780(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M11569; AAA52297.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17418; AAB60694.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17390; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17399; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17409; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17419; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17420; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17421; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17422; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17423; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17391; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17392; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17393; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17394; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17395; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17396; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17397; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17398; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17400; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17401; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17402; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17403; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17404; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17405; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17406; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17407; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17408; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17410; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17411; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17412; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17413; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17414; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17415; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17416; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L17417; AAB60694.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14362; CAA32541.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11617; AAA52298.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11618; AAA52299.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00816; CAA68755.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X05309; CAA28933.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I73012; I73012.
RefSeq NP_000564.2; -.
NP_000642.3; -.
UniGene Hs.334019
3D structure databases
PDB
1GKG; NMR; -; A=1002-1133.[ExPASy / RCSB / EBI]
1GKN; NMR; -; A=942-1065.[ExPASy / RCSB / EBI]
1GOP; Model; -; A=942-1133.[ExPASy / RCSB / EBI]
1PPQ; NMR; -; A=1002-1065.[ExPASy / RCSB / EBI]
2Q7Z; X-ray; -; A=42-1972.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1GKG; -.
1GKN; -.
1GOP; -.
1PPQ; -.
2Q7Z; -.
SMR P17927; 102-233, 491-615, 552-683.
ModBase P17927.
PTM databases
PhosphoSite P17927; -.
Organism-specific databases
H-InvDB HIX0028732; -.
HGNC HGNC:2334; CR1.
GeneLynx CR1; Homo sapiens.
GenAtlas CR1.
MIM 120620; gene. [NCBI / EBI]
607486; phenotype. [NCBI / EBI]
Orphanet 536; Lupus erythematosus.
PharmGKB PA24772; -.
GeneCards P17927.
Gene expression databases
ArrayExpress P17927; -.
CleanEx HS_CR1; -.
GermOnline ENSG00000203710; Homo sapiens.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0004875; Molecular function: complement receptor activity (traceable author statement from ProtInc).
GO:0006956; Biological process: complement activation (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR016060; Complement_control_module.
IPR000436; Sushi_SCR_CCP.
Graphical view of domain structure.
Gene3D G3DSA:2.10.70.10; Complement_control_module; 2.
Pfam PF00084; Sushi; 30.
Pfam graphical view of domain structure.
SMART SM00032; CCP; 30.
SMART graphical view of domain structure.
PROSITE PS50923; SUSHI; 30.
PROSITE graphical view of domain structure (profiles).
BLOCKS P17927.
Genome annotation databases
Ensembl ENSG00000203710; Homo sapiens. [Contig view]
GeneID 1378; -.
KEGG hsa:1378; -.
Phylogenomic databases
HOVERGEN P17927; -.
Other
SOURCE CR1; Homo sapiens.
ProtoNet P17927.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Blood group antigen; Complement pathway; Glycoprotein; Immune response; Innate immunity; Membrane; Polymorphism; Pyrrolidone carboxylic acid; Receptor; Repeat; Signal; Sushi; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     41  41      
CHAIN   42   2039  1998     Complement receptor type 1. PRO_0000006009
TOPO_DOM   42   1971  1930     Extracellular (Potential). 
TRANSMEM   1972   1996  25     Potential. 
TOPO_DOM   1997   2039  43     Cytoplasmic (Potential). 
DOMAIN   42    101  60     Sushi 1. 
DOMAIN   102    163  62     Sushi 2. 
DOMAIN   164    234  71     Sushi 3. 
DOMAIN   236    295  60     Sushi 4. 
DOMAIN   295    355  61     Sushi 5. 
DOMAIN   356    418  63     Sushi 6. 
DOMAIN   419    489  71     Sushi 7. 
DOMAIN   491    551  61     Sushi 8. 
DOMAIN   552    613  62     Sushi 9. 
DOMAIN   614    684  71     Sushi 10. 
DOMAIN   686    745  60     Sushi 11. 
DOMAIN   745    805  61     Sushi 12. 
DOMAIN   806    868  63     Sushi 13. 
DOMAIN   869    939  71     Sushi 14. 
DOMAIN   941   1001  61     Sushi 15. 
DOMAIN   1002   1063  62     Sushi 16. 
DOMAIN   1064   1134  71     Sushi 17. 
DOMAIN   1136   1195  60     Sushi 18. 
DOMAIN   1195   1255  61     Sushi 19. 
DOMAIN   1256   1318  63     Sushi 20. 
DOMAIN   1319   1389  71     Sushi 21. 
DOMAIN   1394   1454  61     Sushi 22. 
DOMAIN   1455   1516  62     Sushi 23. 
DOMAIN   1517   1587  71     Sushi 24. 
DOMAIN   1589   1648  60     Sushi 25. 
DOMAIN   1648   1708  61     Sushi 26. 
DOMAIN   1709   1771  63     Sushi 27. 
DOMAIN   1772   1842  71     Sushi 28. 
DOMAIN   1846   1906  61     Sushi 29. 
DOMAIN   1907   1967  61     Sushi 30. 
MOD_RES   42     42        Pyrrolidone carboxylic acid (Potential). 
CARBOHYD   56     56        N-linked (GlcNAc...) (Potential). 
CARBOHYD   252    252        N-linked (GlcNAc...) (Potential). 
CARBOHYD   410    410        N-linked (GlcNAc...) (Potential). 
CARBOHYD   447    447        N-linked (GlcNAc...) (Potential). 
CARBOHYD   509    509        N-linked (GlcNAc...) (Potential). 
CARBOHYD   578    578        N-linked (GlcNAc...) (Potential). 
CARBOHYD   702    702        N-linked (GlcNAc...) (Potential). 
CARBOHYD   860    860        N-linked (GlcNAc...) (Potential). 
CARBOHYD   897    897        N-linked (GlcNAc...) (Potential). 
CARBOHYD   959    959        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1028   1028        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1152   1152        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1310   1310        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1481   1481        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1504   1504        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1534   1534        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1540   1540        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1605   1605        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1763   1763        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1908   1908        N-linked (GlcNAc...) (Potential). 
DISULFID   43     86        By similarity. 
DISULFID   73     99        By similarity. 
DISULFID   104    145        By similarity. 
DISULFID   131    161        By similarity. 
DISULFID   166    215        By similarity. 
DISULFID   195    232        By similarity. 
DISULFID   238    280        By similarity. 
DISULFID   266    293        By similarity. 
DISULFID   297    340        By similarity. 
DISULFID   326    353        By similarity. 
DISULFID   358    400        By similarity. 
DISULFID   386    416        By similarity. 
DISULFID   421    470        By similarity. 
DISULFID   450    487        By similarity. 
DISULFID   493    536        By similarity. 
DISULFID   523    549        By similarity. 
DISULFID   554    595        By similarity. 
DISULFID   581    611        By similarity. 
DISULFID