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P17927

- CR1_HUMAN

UniProt

P17927 - CR1_HUMAN

Protein

Complement receptor type 1

Gene

CR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (02 Mar 2010)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. complement component C3b binding Source: UniProtKB
    2. complement component C3b receptor activity Source: UniProtKB
    3. complement component C4b binding Source: UniProtKB
    4. complement component C4b receptor activity Source: UniProtKB

    GO - Biological processi

    1. complement activation, classical pathway Source: UniProtKB-KW
    2. complement receptor mediated signaling pathway Source: GOC
    3. innate immune response Source: Reactome
    4. negative regulation of complement activation, alternative pathway Source: UniProtKB
    5. negative regulation of complement activation, classical pathway Source: UniProtKB
    6. negative regulation of serine-type endopeptidase activity Source: UniProtKB
    7. positive regulation of serine-type endopeptidase activity Source: UniProtKB
    8. regulation of complement activation Source: Reactome

    Keywords - Molecular functioni

    Blood group antigen, Receptor

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_118707. Regulation of Complement cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement receptor type 1
    Alternative name(s):
    C3b/C4b receptor
    CD_antigen: CD35
    Gene namesi
    Name:CR1
    Synonyms:C3BR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2334. CR1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: UniProtKB
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    MIMi607486. phenotype.
    611162. phenotype.
    Orphaneti536. Systemic lupus erythematosus.
    PharmGKBiPA26855.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Add
    BLAST
    Chaini42 – 20391998Complement receptor type 1PRO_0000006009Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421Pyrrolidone carboxylic acidSequence Analysis
    Disulfide bondi43 ↔ 86PROSITE-ProRule annotation
    Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi73 ↔ 99PROSITE-ProRule annotation
    Disulfide bondi104 ↔ 145PROSITE-ProRule annotation
    Disulfide bondi131 ↔ 161PROSITE-ProRule annotation
    Disulfide bondi166 ↔ 215PROSITE-ProRule annotation
    Disulfide bondi195 ↔ 232PROSITE-ProRule annotation
    Disulfide bondi238 ↔ 280PROSITE-ProRule annotation
    Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi266 ↔ 293PROSITE-ProRule annotation
    Disulfide bondi297 ↔ 340PROSITE-ProRule annotation
    Disulfide bondi326 ↔ 353PROSITE-ProRule annotation
    Disulfide bondi358 ↔ 400PROSITE-ProRule annotation
    Disulfide bondi386 ↔ 416PROSITE-ProRule annotation
    Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi421 ↔ 470PROSITE-ProRule annotation
    Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi450 ↔ 487PROSITE-ProRule annotation
    Disulfide bondi493 ↔ 536PROSITE-ProRule annotation
    Glycosylationi509 – 5091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi523 ↔ 549PROSITE-ProRule annotation
    Disulfide bondi554 ↔ 595PROSITE-ProRule annotation
    Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi581 ↔ 611PROSITE-ProRule annotation
    Disulfide bondi616 ↔ 665PROSITE-ProRule annotation
    Disulfide bondi645 ↔ 682PROSITE-ProRule annotation
    Disulfide bondi688 ↔ 730PROSITE-ProRule annotation
    Glycosylationi702 – 7021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi716 ↔ 743PROSITE-ProRule annotation
    Disulfide bondi747 ↔ 790PROSITE-ProRule annotation
    Disulfide bondi776 ↔ 803PROSITE-ProRule annotation
    Disulfide bondi808 ↔ 850PROSITE-ProRule annotation
    Disulfide bondi836 ↔ 866PROSITE-ProRule annotation
    Glycosylationi860 – 8601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi871 ↔ 920PROSITE-ProRule annotation
    Glycosylationi897 – 8971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi900 ↔ 937PROSITE-ProRule annotation
    Disulfide bondi943 ↔ 986PROSITE-ProRule annotation
    Glycosylationi959 – 9591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi973 ↔ 999PROSITE-ProRule annotation
    Disulfide bondi1004 ↔ 1045
    Glycosylationi1028 – 10281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1031 ↔ 1061
    Disulfide bondi1066 ↔ 1115
    Disulfide bondi1095 ↔ 1132
    Disulfide bondi1138 ↔ 1180PROSITE-ProRule annotation
    Glycosylationi1152 – 11521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1166 ↔ 1193PROSITE-ProRule annotation
    Disulfide bondi1197 ↔ 1240PROSITE-ProRule annotation
    Disulfide bondi1226 ↔ 1253PROSITE-ProRule annotation
    Disulfide bondi1258 ↔ 1300PROSITE-ProRule annotation
    Disulfide bondi1286 ↔ 1316PROSITE-ProRule annotation
    Glycosylationi1310 – 13101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1321 ↔ 1370PROSITE-ProRule annotation
    Disulfide bondi1350 ↔ 1387PROSITE-ProRule annotation
    Disulfide bondi1396 ↔ 1439PROSITE-ProRule annotation
    Disulfide bondi1426 ↔ 1452PROSITE-ProRule annotation
    Disulfide bondi1457 ↔ 1498PROSITE-ProRule annotation
    Glycosylationi1481 – 14811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1484 ↔ 1514PROSITE-ProRule annotation
    Glycosylationi1504 – 15041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1519 ↔ 1568PROSITE-ProRule annotation
    Glycosylationi1534 – 15341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1540 – 15401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1548 ↔ 1585PROSITE-ProRule annotation
    Disulfide bondi1591 ↔ 1633PROSITE-ProRule annotation
    Glycosylationi1605 – 16051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1619 ↔ 1646PROSITE-ProRule annotation
    Disulfide bondi1650 ↔ 1693PROSITE-ProRule annotation
    Disulfide bondi1679 ↔ 1706PROSITE-ProRule annotation
    Disulfide bondi1711 ↔ 1753PROSITE-ProRule annotation
    Disulfide bondi1739 ↔ 1769PROSITE-ProRule annotation
    Glycosylationi1763 – 17631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1774 ↔ 1823PROSITE-ProRule annotation
    Disulfide bondi1803 ↔ 1840PROSITE-ProRule annotation
    Disulfide bondi1848 ↔ 1891PROSITE-ProRule annotation
    Disulfide bondi1877 ↔ 1904PROSITE-ProRule annotation
    Glycosylationi1908 – 19081N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1909 ↔ 1952PROSITE-ProRule annotation
    Disulfide bondi1938 ↔ 1965PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    PaxDbiP17927.
    PRIDEiP17927.

    PTM databases

    PhosphoSiteiP17927.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP17927.
    BgeeiP17927.
    CleanExiHS_CR1.
    GenevestigatoriP17927.

    Organism-specific databases

    HPAiCAB002491.
    CAB016271.
    HPA042455.
    HPA043579.
    HPA049348.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi107769. 1 interaction.
    IntActiP17927. 7 interactions.
    MINTiMINT-1508305.
    STRINGi9606.ENSP00000356016.

    Structurei

    Secondary structure

    1
    2039
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni57 – 593
    Beta strandi85 – 884
    Beta strandi91 – 933
    Beta strandi111 – 1133
    Beta strandi115 – 1195
    Beta strandi126 – 1283
    Beta strandi135 – 1395
    Beta strandi141 – 1477
    Beta strandi149 – 1568
    Beta strandi161 – 1633
    Beta strandi173 – 1753
    Beta strandi180 – 1834
    Beta strandi190 – 1923
    Beta strandi197 – 2015
    Beta strandi212 – 2154
    Beta strandi219 – 2235
    Beta strandi225 – 2284
    Beta strandi950 – 9545
    Beta strandi961 – 9666
    Beta strandi968 – 9736
    Beta strandi977 – 9793
    Beta strandi982 – 9865
    Beta strandi988 – 9903
    Beta strandi1014 – 10163
    Beta strandi1026 – 10305
    Beta strandi1033 – 10375
    Beta strandi1041 – 10477
    Beta strandi1049 – 10568
    Beta strandi1061 – 10633
    Beta strandi1090 – 10934
    Beta strandi1107 – 11093
    Beta strandi1112 – 11143
    Beta strandi1118 – 11225

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP17927.
    SMRiP17927. Positions 42-1961.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17927.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 19711930ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1997 – 203943CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1972 – 199625HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 10160Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini102 – 16362Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini164 – 23471Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini236 – 29560Sushi 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini295 – 35561Sushi 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini356 – 41863Sushi 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini419 – 48971Sushi 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini491 – 55161Sushi 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini552 – 61362Sushi 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini614 – 68471Sushi 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini686 – 74560Sushi 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini745 – 80561Sushi 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini806 – 86863Sushi 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini869 – 93971Sushi 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini941 – 100161Sushi 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1002 – 106362Sushi 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini1064 – 113471Sushi 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini1136 – 119560Sushi 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini1195 – 125561Sushi 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini1256 – 131863Sushi 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini1319 – 138971Sushi 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini1394 – 145461Sushi 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini1455 – 151662Sushi 23PROSITE-ProRule annotationAdd
    BLAST
    Domaini1517 – 158771Sushi 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini1589 – 164860Sushi 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini1648 – 170861Sushi 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini1709 – 177163Sushi 27PROSITE-ProRule annotationAdd
    BLAST
    Domaini1772 – 184271Sushi 28PROSITE-ProRule annotationAdd
    BLAST
    Domaini1846 – 190661Sushi 29PROSITE-ProRule annotationAdd
    BLAST
    Domaini1907 – 196761Sushi 30PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 30 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000139590.
    HOVERGENiHBG005397.
    KOiK04011.
    PhylomeDBiP17927.

    Family and domain databases

    InterProiIPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PfamiPF00084. Sushi. 30 hits.
    [Graphical view]
    SMARTiSM00032. CCP. 30 hits.
    [Graphical view]
    SUPFAMiSSF57535. SSF57535. 30 hits.
    PROSITEiPS50923. SUSHI. 30 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P17927-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGASSPRSPE PVGPPAPGLP FCCGGSLLAV VVLLALPVAW GQCNAPEWLP     50
    FARPTNLTDE FEFPIGTYLN YECRPGYSGR PFSIICLKNS VWTGAKDRCR 100
    RKSCRNPPDP VNGMVHVIKG IQFGSQIKYS CTKGYRLIGS SSATCIISGD 150
    TVIWDNETPI CDRIPCGLPP TITNGDFIST NRENFHYGSV VTYRCNPGSG 200
    GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS 250
    DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP 300
    PDVLHAERTQ RDKDNFSPGQ EVFYSCEPGY DLRGAASMRC TPQGDWSPAA 350
    PTCEVKSCDD FMGQLLNGRV LFPVNLQLGA KVDFVCDEGF QLKGSSASYC 400
    VLAGMESLWN SSVPVCEQIF CPSPPVIPNG RHTGKPLEVF PFGKTVNYTC 450
    DPHPDRGTSF DLIGESTIRC TSDPQGNGVW SSPAPRCGIL GHCQAPDHFL 500
    FAKLKTQTNA SDFPIGTSLK YECRPEYYGR PFSITCLDNL VWSSPKDVCK 550
    RKSCKTPPDP VNGMVHVITD IQVGSRINYS CTTGHRLIGH SSAECILSGN 600
    AAHWSTKPPI CQRIPCGLPP TIANGDFIST NRENFHYGSV VTYRCNPGSG 650
    GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS 700
    DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP 750
    PDVLHAERTQ RDKDNFSPGQ EVFYSCEPGY DLRGAASMRC TPQGDWSPAA 800
    PTCEVKSCDD FMGQLLNGRV LFPVNLQLGA KVDFVCDEGF QLKGSSASYC 850
    VLAGMESLWN SSVPVCEQIF CPSPPVIPNG RHTGKPLEVF PFGKAVNYTC 900
    DPHPDRGTSF DLIGESTIRC TSDPQGNGVW SSPAPRCGIL GHCQAPDHFL 950
    FAKLKTQTNA SDFPIGTSLK YECRPEYYGR PFSITCLDNL VWSSPKDVCK 1000
    RKSCKTPPDP VNGMVHVITD IQVGSRINYS CTTGHRLIGH SSAECILSGN 1050
    TAHWSTKPPI CQRIPCGLPP TIANGDFIST NRENFHYGSV VTYRCNLGSR 1100
    GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS 1150
    DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP 1200
    PEILHGEHTP SHQDNFSPGQ EVFYSCEPGY DLRGAASLHC TPQGDWSPEA 1250
    PRCAVKSCDD FLGQLPHGRV LFPLNLQLGA KVSFVCDEGF RLKGSSVSHC 1300
    VLVGMRSLWN NSVPVCEHIF CPNPPAILNG RHTGTPSGDI PYGKEISYTC 1350
    DPHPDRGMTF NLIGESTIRC TSDPHGNGVW SSPAPRCELS VRAGHCKTPE 1400
    QFPFASPTIP INDFEFPVGT SLNYECRPGY FGKMFSISCL ENLVWSSVED 1450
    NCRRKSCGPP PEPFNGMVHI NTDTQFGSTV NYSCNEGFRL IGSPSTTCLV 1500
    SGNNVTWDKK APICEIISCE PPPTISNGDF YSNNRTSFHN GTVVTYQCHT 1550
    GPDGEQLFEL VGERSIYCTS KDDQVGVWSS PPPRCISTNK CTAPEVENAI 1600
    RVPGNRSFFS LTEIIRFRCQ PGFVMVGSHT VQCQTNGRWG PKLPHCSRVC 1650
    QPPPEILHGE HTLSHQDNFS PGQEVFYSCE PSYDLRGAAS LHCTPQGDWS 1700
    PEAPRCTVKS CDDFLGQLPH GRVLLPLNLQ LGAKVSFVCD EGFRLKGRSA 1750
    SHCVLAGMKA LWNSSVPVCE QIFCPNPPAI LNGRHTGTPF GDIPYGKEIS 1800
    YACDTHPDRG MTFNLIGESS IRCTSDPQGN GVWSSPAPRC ELSVPAACPH 1850
    PPKIQNGHYI GGHVSLYLPG MTISYICDPG YLLVGKGFIF CTDQGIWSQL 1900
    DHYCKEVNCS FPLFMNGISK ELEMKKVYHY GDYVTLKCED GYTLEGSPWS 1950
    QCQADDRWDP PLAKCTSRTH DALIVGTLSG TIFFILLIIF LSWIILKHRK 2000
    GNNAHENPKE VAIHLHSQGG SSVHPRTLQT NEENSRVLP 2039
    Length:2,039
    Mass (Da):223,663
    Last modified:March 2, 2010 - v3
    Checksum:iFB01870F19D5E6DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti173 – 1731T → A in CAI16042. (PubMed:16710414)Curated
    Sequence conflicti173 – 1731T → A in CAI16723. (PubMed:16710414)Curated
    Sequence conflicti445 – 4451T → A in CAA68755. (PubMed:2972794)Curated
    Sequence conflicti445 – 4451T → A in AAB60694. (PubMed:8245463)Curated
    Sequence conflicti445 – 4451T → A in CAA32541. (PubMed:2971757)Curated
    Sequence conflicti1876 – 18761I → T in CAA68755. (PubMed:2972794)Curated
    Sequence conflicti1876 – 18761I → T in CAA28933. (PubMed:2951479)Curated

    Polymorphismi

    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 [MIMi: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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1208 – 12081H → R.1 Publication
    Corresponds to variant rs2274567 [ dbSNP | Ensembl ].
    VAR_013819
    Natural varianti1408 – 14081T → I.
    VAR_013820
    Natural varianti1408 – 14081T → M.
    Corresponds to variant rs3737002 [ dbSNP | Ensembl ].
    VAR_020263
    Natural varianti1540 – 15401N → S.
    Corresponds to variant rs17259045 [ dbSNP | Ensembl ].
    VAR_055685
    Natural varianti1590 – 15901K → E in MCC(b) antigen. 1 Publication
    Corresponds to variant rs17047660 [ dbSNP | Ensembl ].
    VAR_013821
    Natural varianti1601 – 16011R → G in Sl(2)/Vil antigen and Sl(3) antigen. 2 Publications
    Corresponds to variant rs17047661 [ dbSNP | Ensembl ].
    VAR_013822
    Natural varianti1610 – 16101S → T in Sl(3) antigen. 3 Publications
    Corresponds to variant rs4844609 [ dbSNP | Ensembl ].
    VAR_013823
    Natural varianti1615 – 16151I → V.2 Publications
    Corresponds to variant rs6691117 [ dbSNP | Ensembl ].
    VAR_013824
    Natural varianti1827 – 18271P → R.2 Publications
    Corresponds to variant rs3811381 [ dbSNP | Ensembl ].
    VAR_013825
    Natural varianti1850 – 18501H → D.2 Publications
    VAR_013826
    Natural varianti1969 – 19691T → A.2 Publications
    Corresponds to variant rs2296160 [ dbSNP | Ensembl ].
    VAR_055686

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS44309.1.
    PIRiI73012.
    RefSeqiNP_000564.2. NM_000573.3.
    NP_000642.3. NM_000651.4.
    UniGeneiHs.334019.

    Genome annotation databases

    EnsembliENST00000367051; ENSP00000356018; ENSG00000203710.
    ENST00000367053; ENSP00000356020; ENSG00000203710.
    ENST00000400960; ENSP00000383744; ENSG00000203710.
    GeneIDi1378.
    KEGGihsa:1378.
    UCSCiuc001hfy.3. human.

    Polymorphism databases

    DMDMi290457678.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    dbRBC/BGMUT

    Blood group antigen gene mutation database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS44309.1.
    PIRi I73012.
    RefSeqi NP_000564.2. NM_000573.3.
    NP_000642.3. NM_000651.4.
    UniGenei Hs.334019.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    2MCY NMR - A 102-233 [» ]
    2MCZ NMR - A 41-163 [» ]
    2Q7Z X-ray - A 42-1972 [» ]
    ProteinModelPortali P17927.
    SMRi P17927. Positions 42-1961.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107769. 1 interaction.
    IntActi P17927. 7 interactions.
    MINTi MINT-1508305.
    STRINGi 9606.ENSP00000356016.

    PTM databases

    PhosphoSitei P17927.

    Polymorphism databases

    DMDMi 290457678.

    Proteomic databases

    PaxDbi P17927.
    PRIDEi P17927.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367051 ; ENSP00000356018 ; ENSG00000203710 .
    ENST00000367053 ; ENSP00000356020 ; ENSG00000203710 .
    ENST00000400960 ; ENSP00000383744 ; ENSG00000203710 .
    GeneIDi 1378.
    KEGGi hsa:1378.
    UCSCi uc001hfy.3. human.

    Organism-specific databases

    CTDi 1378.
    GeneCardsi GC01P207669.
    HGNCi HGNC:2334. CR1.
    HPAi CAB002491.
    CAB016271.
    HPA042455.
    HPA043579.
    HPA049348.
    MIMi 120620. gene.
    607486. phenotype.
    611162. phenotype.
    neXtProti NX_P17927.
    Orphaneti 536. Systemic lupus erythematosus.
    PharmGKBi PA26855.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000139590.
    HOVERGENi HBG005397.
    KOi K04011.
    PhylomeDBi P17927.

    Enzyme and pathway databases

    Reactomei REACT_118707. Regulation of Complement cascade.

    Miscellaneous databases

    EvolutionaryTracei P17927.
    GeneWikii Complement_receptor_1.
    GenomeRNAii 1378.
    NextBioi 5589.
    PROi P17927.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17927.
    Bgeei P17927.
    CleanExi HS_CR1.
    Genevestigatori P17927.

    Family and domain databases

    InterProi IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    Pfami PF00084. Sushi. 30 hits.
    [Graphical view ]
    SMARTi SM00032. CCP. 30 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 30 hits.
    PROSITEi PS50923. SUSHI. 30 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiCR1_HUMAN
    AccessioniPrimary (citable) accession number: P17927
    Secondary accession number(s): Q16744
    , Q16745, Q5SR43, Q5SR45, Q9UQV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: March 2, 2010
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Blood group antigen proteins
      Nomenclature of blood group antigens and list of entries
    2. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    3. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3