P17927 (CR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Complement receptor type 1

Alternative name(s):
C3b/C4b receptor
CD_antigen=CD35

Gene names

Name:	CR1
Synonyms:	C3BR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2039 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Complement pathway Immunity Innate immunity
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Sushi Transmembrane Transmembrane helix
Molecular function	Blood group antigen Receptor
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW 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
Cellular_component	cell surface Inferred from direct assay Ref.1PubMed 6978375. Source: UniProtKB integral to plasma membrane Inferred from direct assay PubMed 6910481. Source: UniProtKB
Molecular_function	complement 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 41

41

Chain

42 – 2039

1998

Complement receptor type 1

PRO_0000006009

Regions

Topological domain

42 – 1971

1930

Extracellular Potential

Transmembrane

1972 – 1996

25

Helical; Potential

Topological domain

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

Amino acid modifications

Modified residue

42

1

Pyrrolidone carboxylic acid Potential

Glycosylation

56

1

N-linked (GlcNAc...) Potential

Glycosylation

252

1

N-linked (GlcNAc...) Potential

Glycosylation

410

1

N-linked (GlcNAc...) Potential

Glycosylation

447

1

N-linked (GlcNAc...) Potential

Glycosylation

509

1

N-linked (GlcNAc...) Potential

Glycosylation

578

1

N-linked (GlcNAc...) Potential

Glycosylation

702

1

N-linked (GlcNAc...) Potential

Glycosylation

860

1

N-linked (GlcNAc...) Potential

Glycosylation

897

1

N-linked (GlcNAc...) Potential

Glycosylation

959

1

N-linked (GlcNAc...) Potential

Glycosylation

1028

1

N-linked (GlcNAc...) Potential

Glycosylation

1152

1

N-linked (GlcNAc...) Potential

Glycosylation

1310

1

N-linked (GlcNAc...) Potential

Glycosylation

1481

1

N-linked (GlcNAc...) Potential

Glycosylation

1504

1

N-linked (GlcNAc...) Potential

Glycosylation

1534

1

N-linked (GlcNAc...) Potential

Glycosylation

1540

1

N-linked (GlcNAc...) Potential

Glycosylation

1605

1

N-linked (GlcNAc...) Potential

Glycosylation

1763

1

N-linked (GlcNAc...) Potential

Glycosylation

1908

1

N-linked (GlcNAc...) Potential

Disulfide bond

43 ↔ 86

By similarity

Disulfide bond

73 ↔ 99

By similarity

Disulfide bond

104 ↔ 145

By similarity

Disulfide bond

131 ↔ 161

By similarity

Disulfide bond

166 ↔ 215

By similarity

Disulfide bond

195 ↔ 232

By similarity

Disulfide bond

238 ↔ 280

By similarity

Disulfide bond

266 ↔ 293

By similarity

Disulfide bond

297 ↔ 340

By similarity

Disulfide bond

326 ↔ 353

By similarity

Disulfide bond

358 ↔ 400

By similarity

Disulfide bond

386 ↔ 416

By similarity

Disulfide bond

421 ↔ 470

By similarity

Disulfide bond

450 ↔ 487

By similarity

Disulfide bond

493 ↔ 536

By similarity

Disulfide bond

523 ↔ 549

By similarity

Disulfide bond

554 ↔ 595

By similarity

Disulfide bond

581 ↔ 611

By similarity

Disulfide bond

616 ↔ 665

By similarity

Disulfide bond

645 ↔ 682

By similarity

Disulfide bond

688 ↔ 730

By similarity

Disulfide bond

716 ↔ 743

By similarity

Disulfide bond

747 ↔ 790

By similarity

Disulfide bond

776 ↔ 803

By similarity

Disulfide bond

808 ↔ 850

By similarity

Disulfide bond

836 ↔ 866

By similarity

Disulfide bond

871 ↔ 920

By similarity

Disulfide bond

900 ↔ 937

By similarity

Disulfide bond

943 ↔ 986

By similarity

Disulfide bond

973 ↔ 999

By similarity

Disulfide bond

1004 ↔ 1045

Disulfide bond

1031 ↔ 1061

Disulfide bond

1066 ↔ 1115

Disulfide bond

1095 ↔ 1132

Disulfide bond

1138 ↔ 1180

By similarity

Disulfide bond

1166 ↔ 1193

By similarity

Disulfide bond

1197 ↔ 1240

By similarity

Disulfide bond

1226 ↔ 1253

By similarity

Disulfide bond

1258 ↔ 1300

By similarity

Disulfide bond

1286 ↔ 1316

By similarity

Disulfide bond

1321 ↔ 1370

By similarity

Disulfide bond

1350 ↔ 1387

By similarity

Disulfide bond

1396 ↔ 1439

By similarity

Disulfide bond

1426 ↔ 1452

By similarity

Disulfide bond

1457 ↔ 1498

By similarity

Disulfide bond

1484 ↔ 1514

By similarity

Disulfide bond

1519 ↔ 1568

By similarity

Disulfide bond

1548 ↔ 1585

By similarity

Disulfide bond

1591 ↔ 1633

By similarity

Disulfide bond

1619 ↔ 1646

By similarity

Disulfide bond

1650 ↔ 1693

By similarity

Disulfide bond

1679 ↔ 1706

By similarity

Disulfide bond

1711 ↔ 1753

By similarity

Disulfide bond

1739 ↔ 1769

By similarity

Disulfide bond

1774 ↔ 1823

By similarity

Disulfide bond

1803 ↔ 1840

By similarity

Disulfide bond

1848 ↔ 1891

By similarity

Disulfide bond

1877 ↔ 1904

By similarity

Disulfide bond

1909 ↔ 1952

By similarity

Disulfide bond

1938 ↔ 1965

By similarity

Natural variations

Natural variant

1208

1

H → R. Ref.10
Corresponds to variant rs2274567 [ dbSNP | Ensembl ].

VAR_013819

Natural variant

1408

1

T → I.

VAR_013820

Natural variant

1408

1

T → M.
Corresponds to variant rs3737002 [ dbSNP | Ensembl ].

VAR_020263

Natural variant

1540

1

N → S.
Corresponds to variant rs17259045 [ dbSNP | Ensembl ].

VAR_055685

Natural variant

1590

1

K → E in MCC(b) antigen. Ref.10
Corresponds to variant rs17047660 [ dbSNP | Ensembl ].

VAR_013821

Natural variant

1601

1

R → G in Sl(2)/Vil antigen and Sl(3) antigen. Ref.10 Ref.11
Corresponds to variant rs17047661 [ dbSNP | Ensembl ].

VAR_013822

Natural variant

1610

1

S → T in Sl(3) antigen. Ref.3 Ref.10 Ref.11
Corresponds to variant rs4844609 [ dbSNP | Ensembl ].

VAR_013823

Natural variant

1615

1

I → V. Ref.2 Ref.10
Corresponds to variant rs6691117 [ dbSNP | Ensembl ].

VAR_013824

Natural variant

1827

1

P → R. Ref.2 Ref.10
Corresponds to variant rs3811381 [ dbSNP | Ensembl ].

VAR_013825

Natural variant

1850

1

H → D. Ref.2 Ref.10

VAR_013826

Natural variant

1969

1

T → A. Ref.2 Ref.6
Corresponds to variant rs2296160 [ dbSNP | Ensembl ].

VAR_055686

Experimental info

Sequence conflict

173

1

T → A in CAI16042. Ref.3

Sequence conflict

173

1

T → A in CAI16723. Ref.3

Sequence conflict

445

1

T → A in CAA68755. Ref.1

Sequence conflict

445

1

T → A in AAB60694. Ref.2

Sequence conflict

445

1

T → A in CAA32541. Ref.5

Sequence conflict

1876

1

I → T in CAA68755. Ref.1

Sequence conflict

1876

1

I → T in CAA28933. Ref.6

Secondary structure

1

.

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2039

Helix Strand Turn

Details...

Beta strand

950 – 954

5

Beta strand

961 – 966

6

Beta strand

968 – 973

6

Beta strand

977 – 979

3

Beta strand

982 – 986

5

Beta strand

988 – 990

3

Beta strand

1014 – 1016

3

Beta strand

1026 – 1030

5

Beta strand

1033 – 1037

5

Beta strand

1041 – 1047

7

Beta strand

1049 – 1056

8

Beta strand

1061 – 1063

3

Beta strand

1090 – 1093

4

Beta strand

1107 – 1109

3

Beta strand

1112 – 1114

3

Beta strand

1118 – 1122

5

Sequences

	Sequence		Length	Mass (Da)
	P17927 [UniParc]. Last modified March 2, 2010. Version 3. Checksum: FB01870F19D5E6DD	FASTA	2,039	223,663
	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

References

	« Hide 'large scale' referencesShow '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. , 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 , 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 , 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.

IPI

IPI00940136.

PIR

I73012.

RefSeq

NP_000564.2. NM_000573.3.
NP_000642.3. NM_000651.4.

UniGene

Hs.334019.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GKG	NMR	-	A	1002-1133	[»]
1GKN	NMR	-	A	942-1065	[»]
1GOP	model	-	A	942-1133	[»]
1PPQ	NMR	-	A	1002-1065	[»]
2Q7Z	X-ray	-	A	42-1972	[»]

ProteinModelPortal

P17927.

SMR

P17927. Positions 42-1961.

ModBase

Search...

Protein-protein interaction databases

IntAct

P17927. 7 interactions.

STRING

9606.ENSP00000356016.

PTM databases

PhosphoSite

P17927.

Polymorphism databases

DMDM

290457678.

Proteomic databases

PaxDb

P17927.

PRIDE

P17927.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367051; ENSP00000356018; ENSG00000203710.
ENST00000367053; ENSP00000356020; ENSG00000203710.
ENST00000400960; ENSP00000383744; ENSG00000203710.

GeneID

1378.

KEGG

hsa:1378.

UCSC

uc001hfy.3. human.

Organism-specific databases

CTD

1378.

GeneCards

GC01P207669.

HGNC

HGNC:2334. CR1.

HPA

CAB002491.
CAB016271.
HPA042455.
HPA043579.
HPA049348.

MIM

120620. gene.
607486. phenotype.
611162. phenotype.

neXtProt

NX_P17927.

Orphanet

536. Systemic lupus erythematosus.

PharmGKB

PA26855.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOGENOM

HOG000139590.

HOVERGEN

HBG005397.

KO

K04011.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P17927.

Bgee

P17927.

CleanEx

HS_CR1.

Genevestigator

P17927.

GermOnline

ENSG00000203710. Homo sapiens.

Family and domain databases

InterPro

IPR000436. Sushi_SCR_CCP.
[Graphical view]

Pfam

PF00084. Sushi. 30 hits.
[Graphical view]

SMART

SM00032. CCP. 30 hits.
[Graphical view]

SUPFAM

SSF57535. Complement_control_module. 30 hits.

PROSITE

PS50923. SUSHI. 30 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P17927.

GenomeRNAi

1378.

NextBio

5589.

SOURCE

Search...

Entry information

Entry name

CR1_HUMAN

Accession

Primary (citable) accession number: P17927
Secondary accession number(s): Q16744 , Q16745, Q5SR43, Q5SR45, Q9UQV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	March 2, 2010
Last modified:	May 1, 2013
This is version 144 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.