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P17927 (CR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement receptor type 1
Alternative name(s):
C3b/C4b receptor
CD_antigen=CD35
Gene names
Name:CR1
Synonyms:C3BR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2039 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates cellular binding of particles and immune complexes that have activated complement.

Subunit structure

Monomer.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Present on erythrocytes, leukocytes, glomerular podocytes, and splenic follicular dendritic cells.

Polymorphism

CR1 contains a system of antigens called the Knops blood group system. Polymorphisms within this system are involved in malarial rosetting, a process associated with cerebral malaria, the major cause of mortality in Plasmodium falciparum malaria. Common Knops system antigens include McCoy (McC) and Sl(a)/Vil (Kn4, or Swain-Langley; Vil or Villien). Sl(a-) phenotype is more common in persons of African descent and may protect against fatal malaria.

Other polymorphic forms of CR1 contain 23, 37 or 44 Sushi (CCP/SCR) domains instead of the 30 Sushi (CCP/SCR) domains. The most frequent alleles are the F allotype (shown here) and the S allotype (37 repeat Sushi domains). The gene frequencies of the F allotype and S allotype are 0.87 and 0.11 in Caucasians, 0.82 and 0.11 in African Americans, 0.89 and 0.11 in Mexicans.

Genetic variations in CR1 resulting in CR1 deficiency are involved in protection against severe malaria [MIM:611162]. Parasitized red blood cells (RBCs) from children suffering from severe malaria often adhere to complement receptor 1 (CR1) on uninfected RBCs to form clumps of cells known as rosettes. CR1-deficient red blood cells show greatly reduced rosetting and CR1 deficiency occurs in healthy individuals from malaria-endemic regions.

Sequence similarities

Belongs to the receptors of complement activation (RCA) family.

Contains 30 Sushi (CCP/SCR) domains.

Ontologies

Keywords
   Biological processComplement pathway
Immunity
Innate immunity
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Sushi
Transmembrane
Transmembrane helix
   Molecular functionBlood group antigen
Receptor
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcomplement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

complement receptor mediated signaling pathway

Inferred from direct assay Ref.1. Source: GOC

innate immune response

Traceable author statement. Source: Reactome

negative regulation of complement activation, alternative pathway

Inferred from direct assay PubMed 10531307. Source: UniProtKB

negative regulation of complement activation, classical pathway

Inferred from direct assay PubMed 10531307PubMed 6910481. Source: UniProtKB

negative regulation of serine-type endopeptidase activity

Inferred from direct assay PubMed 6910481. Source: UniProtKB

positive regulation of serine-type endopeptidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of complement activation

Traceable author statement. Source: Reactome

   Cellular_componentcell surface

Inferred from direct assay Ref.1PubMed 6978375. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of plasma membrane

Inferred from direct assay PubMed 6910481. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncomplement component C3b binding

Inferred from direct assay Ref.1. Source: UniProtKB

complement component C3b receptor activity

Inferred from direct assay Ref.1. Source: UniProtKB

complement component C4b binding

Inferred from direct assay Ref.1. Source: UniProtKB

complement component C4b receptor activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141
Chain42 – 20391998Complement receptor type 1
PRO_0000006009

Regions

Topological domain42 – 19711930Extracellular Potential
Transmembrane1972 – 199625Helical; Potential
Topological domain1997 – 203943Cytoplasmic Potential
Domain42 – 10160Sushi 1
Domain102 – 16362Sushi 2
Domain164 – 23471Sushi 3
Domain236 – 29560Sushi 4
Domain295 – 35561Sushi 5
Domain356 – 41863Sushi 6
Domain419 – 48971Sushi 7
Domain491 – 55161Sushi 8
Domain552 – 61362Sushi 9
Domain614 – 68471Sushi 10
Domain686 – 74560Sushi 11
Domain745 – 80561Sushi 12
Domain806 – 86863Sushi 13
Domain869 – 93971Sushi 14
Domain941 – 100161Sushi 15
Domain1002 – 106362Sushi 16
Domain1064 – 113471Sushi 17
Domain1136 – 119560Sushi 18
Domain1195 – 125561Sushi 19
Domain1256 – 131863Sushi 20
Domain1319 – 138971Sushi 21
Domain1394 – 145461Sushi 22
Domain1455 – 151662Sushi 23
Domain1517 – 158771Sushi 24
Domain1589 – 164860Sushi 25
Domain1648 – 170861Sushi 26
Domain1709 – 177163Sushi 27
Domain1772 – 184271Sushi 28
Domain1846 – 190661Sushi 29
Domain1907 – 196761Sushi 30

Amino acid modifications

Modified residue421Pyrrolidone carboxylic acid Potential
Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Potential
Glycosylation5091N-linked (GlcNAc...) Potential
Glycosylation5781N-linked (GlcNAc...) Potential
Glycosylation7021N-linked (GlcNAc...) Potential
Glycosylation8601N-linked (GlcNAc...) Potential
Glycosylation8971N-linked (GlcNAc...) Potential
Glycosylation9591N-linked (GlcNAc...) Potential
Glycosylation10281N-linked (GlcNAc...) Potential
Glycosylation11521N-linked (GlcNAc...) Potential
Glycosylation13101N-linked (GlcNAc...) Potential
Glycosylation14811N-linked (GlcNAc...) Potential
Glycosylation15041N-linked (GlcNAc...) Potential
Glycosylation15341N-linked (GlcNAc...) Potential
Glycosylation15401N-linked (GlcNAc...) Potential
Glycosylation16051N-linked (GlcNAc...) Potential
Glycosylation17631N-linked (GlcNAc...) Potential
Glycosylation19081N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 86 By similarity
Disulfide bond73 ↔ 99 By similarity
Disulfide bond104 ↔ 145 By similarity
Disulfide bond131 ↔ 161 By similarity
Disulfide bond166 ↔ 215 By similarity
Disulfide bond195 ↔ 232 By similarity
Disulfide bond238 ↔ 280 By similarity
Disulfide bond266 ↔ 293 By similarity
Disulfide bond297 ↔ 340 By similarity
Disulfide bond326 ↔ 353 By similarity
Disulfide bond358 ↔ 400 By similarity
Disulfide bond386 ↔ 416 By similarity
Disulfide bond421 ↔ 470 By similarity
Disulfide bond450 ↔ 487 By similarity
Disulfide bond493 ↔ 536 By similarity
Disulfide bond523 ↔ 549 By similarity
Disulfide bond554 ↔ 595 By similarity
Disulfide bond581 ↔ 611 By similarity
Disulfide bond616 ↔ 665 By similarity
Disulfide bond645 ↔ 682 By similarity
Disulfide bond688 ↔ 730 By similarity
Disulfide bond716 ↔ 743 By similarity
Disulfide bond747 ↔ 790 By similarity
Disulfide bond776 ↔ 803 By similarity
Disulfide bond808 ↔ 850 By similarity
Disulfide bond836 ↔ 866 By similarity
Disulfide bond871 ↔ 920 By similarity
Disulfide bond900 ↔ 937 By similarity
Disulfide bond943 ↔ 986 By similarity
Disulfide bond973 ↔ 999 By similarity
Disulfide bond1004 ↔ 1045
Disulfide bond1031 ↔ 1061
Disulfide bond1066 ↔ 1115
Disulfide bond1095 ↔ 1132
Disulfide bond1138 ↔ 1180 By similarity
Disulfide bond1166 ↔ 1193 By similarity
Disulfide bond1197 ↔ 1240 By similarity
Disulfide bond1226 ↔ 1253 By similarity
Disulfide bond1258 ↔ 1300 By similarity
Disulfide bond1286 ↔ 1316 By similarity
Disulfide bond1321 ↔ 1370 By similarity
Disulfide bond1350 ↔ 1387 By similarity
Disulfide bond1396 ↔ 1439 By similarity
Disulfide bond1426 ↔ 1452 By similarity
Disulfide bond1457 ↔ 1498 By similarity
Disulfide bond1484 ↔ 1514 By similarity
Disulfide bond1519 ↔ 1568 By similarity
Disulfide bond1548 ↔ 1585 By similarity
Disulfide bond1591 ↔ 1633 By similarity
Disulfide bond1619 ↔ 1646 By similarity
Disulfide bond1650 ↔ 1693 By similarity
Disulfide bond1679 ↔ 1706 By similarity
Disulfide bond1711 ↔ 1753 By similarity
Disulfide bond1739 ↔ 1769 By similarity
Disulfide bond1774 ↔ 1823 By similarity
Disulfide bond1803 ↔ 1840 By similarity
Disulfide bond1848 ↔ 1891 By similarity
Disulfide bond1877 ↔ 1904 By similarity
Disulfide bond1909 ↔ 1952 By similarity
Disulfide bond1938 ↔ 1965 By similarity

Natural variations

Natural variant12081H → R. Ref.10
Corresponds to variant rs2274567 [ dbSNP | Ensembl ].
VAR_013819
Natural variant14081T → I.
VAR_013820
Natural variant14081T → M.
Corresponds to variant rs3737002 [ dbSNP | Ensembl ].
VAR_020263
Natural variant15401N → S.
Corresponds to variant rs17259045 [ dbSNP | Ensembl ].
VAR_055685
Natural variant15901K → E in MCC(b) antigen. Ref.10
Corresponds to variant rs17047660 [ dbSNP | Ensembl ].
VAR_013821
Natural variant16011R → G in Sl(2)/Vil antigen and Sl(3) antigen. Ref.10 Ref.11
Corresponds to variant rs17047661 [ dbSNP | Ensembl ].
VAR_013822
Natural variant16101S → T in Sl(3) antigen. Ref.3 Ref.10 Ref.11
Corresponds to variant rs4844609 [ dbSNP | Ensembl ].
VAR_013823
Natural variant16151I → V. Ref.2 Ref.10
Corresponds to variant rs6691117 [ dbSNP | Ensembl ].
VAR_013824
Natural variant18271P → R. Ref.2 Ref.10
Corresponds to variant rs3811381 [ dbSNP | Ensembl ].
VAR_013825
Natural variant18501H → D. Ref.2 Ref.10
VAR_013826
Natural variant19691T → A. Ref.2 Ref.6
Corresponds to variant rs2296160 [ dbSNP | Ensembl ].
VAR_055686

Experimental info

Sequence conflict1731T → A in CAI16042. Ref.3
Sequence conflict1731T → A in CAI16723. Ref.3
Sequence conflict4451T → A in CAA68755. Ref.1
Sequence conflict4451T → A in AAB60694. Ref.2
Sequence conflict4451T → A in CAA32541. Ref.5
Sequence conflict18761I → T in CAA68755. Ref.1
Sequence conflict18761I → T in CAA28933. Ref.6

Secondary structure

................................................................... 2039
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17927 [UniParc].

Last modified March 2, 2010. Version 3.
Checksum: FB01870F19D5E6DD

FASTA2,039223,663
        10         20         30         40         50         60 
MGASSPRSPE PVGPPAPGLP FCCGGSLLAV VVLLALPVAW GQCNAPEWLP FARPTNLTDE 

        70         80         90        100        110        120 
FEFPIGTYLN YECRPGYSGR PFSIICLKNS VWTGAKDRCR RKSCRNPPDP VNGMVHVIKG 

       130        140        150        160        170        180 
IQFGSQIKYS CTKGYRLIGS SSATCIISGD TVIWDNETPI CDRIPCGLPP TITNGDFIST 

       190        200        210        220        230        240 
NRENFHYGSV VTYRCNPGSG GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP 

       250        260        270        280        290        300 
PNVENGILVS DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP 

       310        320        330        340        350        360 
PDVLHAERTQ RDKDNFSPGQ EVFYSCEPGY DLRGAASMRC TPQGDWSPAA PTCEVKSCDD 

       370        380        390        400        410        420 
FMGQLLNGRV LFPVNLQLGA KVDFVCDEGF QLKGSSASYC VLAGMESLWN SSVPVCEQIF 

       430        440        450        460        470        480 
CPSPPVIPNG RHTGKPLEVF PFGKTVNYTC DPHPDRGTSF DLIGESTIRC TSDPQGNGVW 

       490        500        510        520        530        540 
SSPAPRCGIL GHCQAPDHFL FAKLKTQTNA SDFPIGTSLK YECRPEYYGR PFSITCLDNL 

       550        560        570        580        590        600 
VWSSPKDVCK RKSCKTPPDP VNGMVHVITD IQVGSRINYS CTTGHRLIGH SSAECILSGN 

       610        620        630        640        650        660 
AAHWSTKPPI CQRIPCGLPP TIANGDFIST NRENFHYGSV VTYRCNPGSG GRKVFELVGE 

       670        680        690        700        710        720 
PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS DNRSLFSLNE VVEFRCQPGF 

       730        740        750        760        770        780 
VMKGPRRVKC QALNKWEPEL PSCSRVCQPP PDVLHAERTQ RDKDNFSPGQ EVFYSCEPGY 

       790        800        810        820        830        840 
DLRGAASMRC TPQGDWSPAA PTCEVKSCDD FMGQLLNGRV LFPVNLQLGA KVDFVCDEGF 

       850        860        870        880        890        900 
QLKGSSASYC VLAGMESLWN SSVPVCEQIF CPSPPVIPNG RHTGKPLEVF PFGKAVNYTC 

       910        920        930        940        950        960 
DPHPDRGTSF DLIGESTIRC TSDPQGNGVW SSPAPRCGIL GHCQAPDHFL FAKLKTQTNA 

       970        980        990       1000       1010       1020 
SDFPIGTSLK YECRPEYYGR PFSITCLDNL VWSSPKDVCK RKSCKTPPDP VNGMVHVITD 

      1030       1040       1050       1060       1070       1080 
IQVGSRINYS CTTGHRLIGH SSAECILSGN TAHWSTKPPI CQRIPCGLPP TIANGDFIST 

      1090       1100       1110       1120       1130       1140 
NRENFHYGSV VTYRCNLGSR GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP 

      1150       1160       1170       1180       1190       1200 
PNVENGILVS DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP 

      1210       1220       1230       1240       1250       1260 
PEILHGEHTP SHQDNFSPGQ EVFYSCEPGY DLRGAASLHC TPQGDWSPEA PRCAVKSCDD 

      1270       1280       1290       1300       1310       1320 
FLGQLPHGRV LFPLNLQLGA KVSFVCDEGF RLKGSSVSHC VLVGMRSLWN NSVPVCEHIF 

      1330       1340       1350       1360       1370       1380 
CPNPPAILNG RHTGTPSGDI PYGKEISYTC DPHPDRGMTF NLIGESTIRC TSDPHGNGVW 

      1390       1400       1410       1420       1430       1440 
SSPAPRCELS VRAGHCKTPE QFPFASPTIP INDFEFPVGT SLNYECRPGY FGKMFSISCL 

      1450       1460       1470       1480       1490       1500 
ENLVWSSVED NCRRKSCGPP PEPFNGMVHI NTDTQFGSTV NYSCNEGFRL IGSPSTTCLV 

      1510       1520       1530       1540       1550       1560 
SGNNVTWDKK APICEIISCE PPPTISNGDF YSNNRTSFHN GTVVTYQCHT GPDGEQLFEL 

      1570       1580       1590       1600       1610       1620 
VGERSIYCTS KDDQVGVWSS PPPRCISTNK CTAPEVENAI RVPGNRSFFS LTEIIRFRCQ 

      1630       1640       1650       1660       1670       1680 
PGFVMVGSHT VQCQTNGRWG PKLPHCSRVC QPPPEILHGE HTLSHQDNFS PGQEVFYSCE 

      1690       1700       1710       1720       1730       1740 
PSYDLRGAAS LHCTPQGDWS PEAPRCTVKS CDDFLGQLPH GRVLLPLNLQ LGAKVSFVCD 

      1750       1760       1770       1780       1790       1800 
EGFRLKGRSA SHCVLAGMKA LWNSSVPVCE QIFCPNPPAI LNGRHTGTPF GDIPYGKEIS 

      1810       1820       1830       1840       1850       1860 
YACDTHPDRG MTFNLIGESS IRCTSDPQGN GVWSSPAPRC ELSVPAACPH PPKIQNGHYI 

      1870       1880       1890       1900       1910       1920 
GGHVSLYLPG MTISYICDPG YLLVGKGFIF CTDQGIWSQL DHYCKEVNCS FPLFMNGISK 

      1930       1940       1950       1960       1970       1980 
ELEMKKVYHY GDYVTLKCED GYTLEGSPWS QCQADDRWDP PLAKCTSRTH DALIVGTLSG 

      1990       2000       2010       2020       2030 
TIFFILLIIF LSWIILKHRK GNNAHENPKE VAIHLHSQGG SSVHPRTLQT NEENSRVLP 

« Hide

References

« Hide 'large scale' references
[1]"Identification of distinct C3b and C4b recognition sites in the human C3b/C4b receptor (CR1, CD35) by deletion mutagenesis."
Klickstein L.B., Bartow T.J., Miletic V., Rabson L.D., Smith J.A., Fearon D.T.
J. Exp. Med. 168:1699-1717(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE S AND ALLELE F).
[2]"Structure of the gene for the F allele of complement receptor type 1 and sequence of the coding region unique to the S allele."
Vik D.P., Wong W.W.
J. Immunol. 151:6214-6224(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE S AND ALLELE F), VARIANTS VAL-1615; ARG-1827; ASP-1850 AND ALA-1969.
[3]"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. expand/collapse author list , 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], VARIANT THR-1610.
[4]"Structure of the human CR1 gene. Molecular basis of the structural and quantitative polymorphisms and identification of a new CR1-like allele."
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.
J. Exp. Med. 169:847-863(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-41.
[5]"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."
Hourcade D., Miesner D.R., Atkinson J.P., Holers V.M.
J. Exp. Med. 168:1255-1270(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-584.
[6]"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."
Klickstein L.B., Wong W.W., Smith J.A., Weis J.H., Wilson J.G., Fearon D.T.
J. Exp. Med. 165:1095-1112(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 503-2039, VARIANT ALA-1969.
[7]"Identification of a partial cDNA clone for the human receptor for complement fragments C3b/C4b."
Wong W.W., Klickstein L.B., Smith J.A., Weis J.H., Fearon D.T.
Proc. Natl. Acad. Sci. U.S.A. 82:7711-7715(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 761-783; 831-845 AND 1179-1195.
[8]"Structural polymorphisms of complement receptor 1 (CR1) in systemic lupus erythematosus (SLE) patients and normal controls of three ethnic groups."
Moulds J.M., Reveille J.D., Arnett F.C.
Clin. Exp. Immunol. 105:302-305(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM.
[9]"A human complement receptor 1 polymorphism that reduces Plasmodium falciparum rosetting confers protection against severe malaria."
Cockburn I.A., Mackinnon M.J., O'Donnell A., Allen S.J., Moulds J.M., Baisor M., Bockarie M., Reeder J.C., Rowe J.A.
Proc. Natl. Acad. Sci. U.S.A. 101:272-277(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM, INVOLVEMENT IN PROTECTION AGAINST MALARIA.
[10]"Molecular identification of Knops blood group polymorphisms found in long homologous region D of complement receptor 1."
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.
Blood 97:2879-2885(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-1208; GLU-1590; GLY-1601; THR-1610; VAL-1615; ARG-1827 AND ASP-1850.
[11]"Expansion of the Knops blood group system and subdivision of Sl(a)."
Moulds J.M., Zimmerman P.A., Doumbo O.K., Diallo D.A., Atkinson J.P., Krych-Goldberg M., Hourcade D.E., Moulds J.J.
Transfusion 42:251-256(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SL(2)/VIL GLY-1601 AND SL(3) THR-1610.
[12]"Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor."
Smith B.O., Mallin R.L., Krych-Goldberg M., Wang X., Hauhart R.E., Bromek K., Uhrin D., Atkinson J.P., Barlow P.N.
Cell 108:769-780(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 942-1133.
+Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00816 mRNA. Translation: CAA68755.1.
L17418 expand/collapse EMBL AC list , L17390, L17399, L17409, L17419, L17420, L17421, L17422, L17423, L17391, L17392, L17393, L17394, L17395, L17396, L17397, L17398, L17400, L17401, L17402, L17403, L17404, L17405, L17406, L17407, L17408, L17410, L17411, L17412, L17413, L17414, L17415, L17416, L17417 Genomic DNA. Translation: AAB60694.1.
L17418 expand/collapse EMBL AC list , L17390, L17391, L17392, L17393, L17394, L17395, L17396, L17397, L17398, L17399, L17400, L17401, L17402, L17403, L17404, L17405, L17406, L17407, L17408, L17409, L17410, L17411, L17412, L17413, L17414, L17415, L17416, L17417, L17419, L17420, L17421, L17422, L17423, L17424, L17425, L17426, L17427, L17428, L17429, L17430 Genomic DNA. Translation: AAB60695.1.
AL137789, AL691452 Genomic DNA. Translation: CAI16042.1.
AL137789, AL691452 Genomic DNA. Translation: CAI16043.1.
AL691452, AL137789 Genomic DNA. Translation: CAI16723.1.
AL691452, AL137789 Genomic DNA. Translation: CAI16725.1.
X14362 mRNA. Translation: CAA32541.1.
X05309 mRNA. Translation: CAA28933.1.
M11569 mRNA. Translation: AAA52297.1.
M11617 mRNA. Translation: AAA52298.1.
M11618 mRNA. Translation: AAA52299.1.
CCDSCCDS44309.1.
PIRI73012.
RefSeqNP_000564.2. NM_000573.3.
NP_000642.3. NM_000651.4.
UniGeneHs.334019.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GKGNMR-A1002-1133[»]
1GKNNMR-A942-1065[»]
1GOPmodel-A942-1133[»]
1PPQNMR-A1002-1065[»]
2MCYNMR-A102-233[»]
2MCZNMR-A41-163[»]
2Q7ZX-ray-A42-1972[»]
ProteinModelPortalP17927.
SMRP17927. Positions 42-1961.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107769. 1 interaction.
IntActP17927. 7 interactions.
MINTMINT-1508305.
STRING9606.ENSP00000356016.

PTM databases

PhosphoSiteP17927.

Polymorphism databases

DMDM290457678.

Proteomic databases

PaxDbP17927.
PRIDEP17927.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367051; ENSP00000356018; ENSG00000203710.
ENST00000367053; ENSP00000356020; ENSG00000203710.
ENST00000400960; ENSP00000383744; ENSG00000203710.
GeneID1378.
KEGGhsa:1378.
UCSCuc001hfy.3. human.

Organism-specific databases

CTD1378.
GeneCardsGC01P207669.
HGNCHGNC:2334. CR1.
HPACAB002491.
CAB016271.
HPA042455.
HPA043579.
HPA049348.
MIM120620. gene.
607486. phenotype.
611162. phenotype.
neXtProtNX_P17927.
Orphanet536. Systemic lupus erythematosus.
PharmGKBPA26855.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000139590.
HOVERGENHBG005397.
KOK04011.
PhylomeDBP17927.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP17927.
BgeeP17927.
CleanExHS_CR1.
GenevestigatorP17927.

Family and domain databases

InterProIPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00084. Sushi. 30 hits.
[Graphical view]
SMARTSM00032. CCP. 30 hits.
[Graphical view]
SUPFAMSSF57535. SSF57535. 30 hits.
PROSITEPS50923. SUSHI. 30 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17927.
GeneWikiComplement_receptor_1.
GenomeRNAi1378.
NextBio5589.
PROP17927.
SOURCESearch...

Entry information

Entry nameCR1_HUMAN
AccessionPrimary (citable) accession number: P17927
Secondary accession number(s): Q16744 expand/collapse secondary AC list , Q16745, Q5SR43, Q5SR45, Q9UQV2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: March 2, 2010
Last modified: July 9, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries