CR1_HUMAN
ID CR1_HUMAN Reviewed; 2039 AA.
AC P17927; Q16744; Q16745; Q5SR43; Q5SR45; Q9UQV2;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Complement receptor type 1;
DE AltName: Full=C3b/C4b receptor;
DE AltName: CD_antigen=CD35;
DE Flags: Precursor;
GN Name=CR1; Synonyms=C3BR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE S AND ALLELE F), FUNCTION, AND
RP INTERACTION WITH C3B AND C4B.
RX PubMed=2972794; DOI=10.1084/jem.168.5.1699;
RA Klickstein L.B., Bartow T.J., Miletic V., Rabson L.D., Smith J.A.,
RA Fearon D.T.;
RT "Identification of distinct C3b and C4b recognition sites in the human
RT C3b/C4b receptor (CR1, CD35) by deletion mutagenesis.";
RL J. Exp. Med. 168:1699-1717(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE S AND ALLELE F), AND VARIANTS
RP VAL-1615; ARG-1827; ASP-1850 AND ALA-1969.
RX PubMed=8245463;
RA Vik D.P., Wong W.W.;
RT "Structure of the gene for the F allele of complement receptor type 1 and
RT sequence of the coding region unique to the S allele.";
RL J. Immunol. 151:6214-6224(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-1610.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-41.
RX PubMed=2564414; DOI=10.1084/jem.169.3.847;
RA Wong W.W., Cahill J.M., Rosen M.D., Kennedy C.A., Bonaccio E.T.,
RA Morris M.J., Wilson J.G., Klickstein L.B., Fearon D.T.;
RT "Structure of the human CR1 gene. Molecular basis of the structural and
RT quantitative polymorphisms and identification of a new CR1-like allele.";
RL J. Exp. Med. 169:847-863(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-584.
RX PubMed=2971757; DOI=10.1084/jem.168.4.1255;
RA Hourcade D., Miesner D.R., Atkinson J.P., Holers V.M.;
RT "Identification of an alternative polyadenylation site in the human C3b/C4b
RT receptor (complement receptor type 1) transcriptional unit and prediction
RT of a secreted form of complement receptor type 1.";
RL J. Exp. Med. 168:1255-1270(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 503-2039, AND VARIANT ALA-1969.
RX PubMed=2951479; DOI=10.1084/jem.165.4.1095;
RA Klickstein L.B., Wong W.W., Smith J.A., Weis J.H., Wilson J.G.,
RA Fearon D.T.;
RT "Human C3b/C4b receptor (CR1). Demonstration of long homologous repeating
RT domains that are composed of the short consensus repeats characteristics of
RT C3/C4 binding proteins.";
RL J. Exp. Med. 165:1095-1112(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 761-783; 831-845 AND 1179-1195.
RX PubMed=2933745; DOI=10.1073/pnas.82.22.7711;
RA Wong W.W., Klickstein L.B., Smith J.A., Weis J.H., Fearon D.T.;
RT "Identification of a partial cDNA clone for the human receptor for
RT complement fragments C3b/C4b.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7711-7715(1985).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=6233222; DOI=10.1016/0165-2478(84)90089-0;
RA Takemura S., Deguchi M., Ueda M., Yoshida N., Kato H., Yoshikawa T.,
RA Sugino S., Kondo M.;
RT "C3b receptor (CR1) on erythrocytes in various diseases.";
RL Immunol. Lett. 7:325-328(1984).
RN [9]
RP FUNCTION.
RX PubMed=2963069;
RA Schifferli J.A., Ng Y.C., Estreicher J., Walport M.J.;
RT "The clearance of tetanus toxoid/anti-tetanus toxoid immune complexes from
RT the circulation of humans. Complement- and erythrocyte complement receptor
RT 1-dependent mechanisms.";
RL J. Immunol. 140:899-904(1988).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=1385479; DOI=10.1172/jci116080;
RA Dovezenski N., Billetta R., Gigli I.;
RT "Expression and localization of proteins of the complement system in human
RT skin.";
RL J. Clin. Invest. 90:2000-2012(1992).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=1534036; DOI=10.1016/0008-8749(92)90277-v;
RA Yaskanin D.D., Thompson L.F., Waxman F.J.;
RT "Distribution and quantitative expression of the complement receptor type 1
RT (CR1) on human peripheral blood T lymphocytes.";
RL Cell. Immunol. 142:159-176(1992).
RN [12]
RP FUNCTION, AND INTERACTION WITH C3B AND C4B.
RX PubMed=8175757; DOI=10.1016/s0021-9258(17)36829-1;
RA Krych M., Clemenza L., Howdeshell D., Hauhart R., Hourcade D.,
RA Atkinson J.P.;
RT "Analysis of the functional domains of complement receptor type 1 (C3b/C4b
RT receptor; CD35) by substitution mutagenesis.";
RL J. Biol. Chem. 269:13273-13278(1994).
RN [13]
RP POLYMORPHISM.
RX PubMed=8706338; DOI=10.1046/j.1365-2249.1996.d01-748.x;
RA Moulds J.M., Reveille J.D., Arnett F.C.;
RT "Structural polymorphisms of complement receptor 1 (CR1) in systemic lupus
RT erythematosus (SLE) patients and normal controls of three ethnic groups.";
RL Clin. Exp. Immunol. 105:302-305(1996).
RN [14]
RP INTERACTION WITH C1QA.
RX PubMed=9324355; DOI=10.1016/s1074-7613(00)80356-8;
RA Klickstein L.B., Barbashov S.F., Liu T., Jack R.M., Nicholson-Weller A.;
RT "Complement receptor type 1 (CR1, CD35) is a receptor for C1q.";
RL Immunity 7:345-355(1997).
RN [15]
RP POLYMORPHISM, AND INVOLVEMENT IN PROTECTION AGAINST MALARIA.
RX PubMed=14694201; DOI=10.1073/pnas.0305306101;
RA Cockburn I.A., Mackinnon M.J., O'Donnell A., Allen S.J., Moulds J.M.,
RA Baisor M., Bockarie M., Reeder J.C., Rowe J.A.;
RT "A human complement receptor 1 polymorphism that reduces Plasmodium
RT falciparum rosetting confers protection against severe malaria.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:272-277(2004).
RN [16]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR VIRUS
RP GP350 PROTEIN (MICROBIAL INFECTION).
RX PubMed=23416052; DOI=10.1016/j.celrep.2013.01.023;
RA Ogembo J.G., Kannan L., Ghiran I., Nicholson-Weller A., Finberg R.W.,
RA Tsokos G.C., Fingeroth J.D.;
RT "Human complement receptor type 1/CD35 is an Epstein-Barr Virus receptor.";
RL Cell Rep. 3:371-385(2013).
RN [17]
RP INTERACTION WITH MBL2 AND FCN2.
RX PubMed=23460739; DOI=10.4049/jimmunol.1202451;
RA Jacquet M., Lacroix M., Ancelet S., Gout E., Gaboriaud C., Thielens N.M.,
RA Rossi V.;
RT "Deciphering complement receptor type 1 interactions with recognition
RT proteins of the lectin complement pathway.";
RL J. Immunol. 190:3721-3731(2013).
RN [18]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25742728; DOI=10.1016/j.imlet.2015.02.009;
RA Toeroek K., Dezso B., Bencsik A., Uzonyi B., Erdei A.;
RT "Complement receptor type 1 (CR1/CD35) expressed on activated human CD4+ T
RT cells contributes to generation of regulatory T cells.";
RL Immunol. Lett. 164:117-124(2015).
RN [19]
RP INTERACTION WITH C1QA AND MBL2.
RX PubMed=29563915; DOI=10.3389/fimmu.2018.00453;
RA Jacquet M., Cioci G., Fouet G., Bally I., Thielens N.M., Gaboriaud C.,
RA Rossi V.;
RT "C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on
RT CCP24-25 Modules.";
RL Front. Immunol. 9:453-453(2018).
RN [20]
RP VARIANTS ARG-1208; GLU-1590; GLY-1601; THR-1610; VAL-1615; ARG-1827 AND
RP ASP-1850.
RX PubMed=11313284; DOI=10.1182/blood.v97.9.2879;
RA Moulds J.M., Zimmerman P.A., Doumbo O.K., Kassambara L., Sagara I.,
RA Diallo D.A., Atkinson J.P., Krych-Goldberg M., Hauhart R.E., Hourcade D.E.,
RA McNamara D.T., Birmingham D.J., Rowe J.A., Moulds J.J., Miller L.H.;
RT "Molecular identification of Knops blood group polymorphisms found in long
RT homologous region D of complement receptor 1.";
RL Blood 97:2879-2885(2001).
RN [21]
RP VARIANTS SL(2)/VIL GLY-1601 AND SL(3) THR-1610.
RX PubMed=11896343; DOI=10.1046/j.1537-2995.2002.00002.x;
RA Moulds J.M., Zimmerman P.A., Doumbo O.K., Diallo D.A., Atkinson J.P.,
RA Krych-Goldberg M., Hourcade D.E., Moulds J.J.;
RT "Expansion of the Knops blood group system and subdivision of Sl(a).";
RL Transfusion 42:251-256(2002).
RN [22]
RP STRUCTURE BY NMR OF 942-1133.
RX PubMed=11955431; DOI=10.1016/s0092-8674(02)00672-4;
RA Smith B.O., Mallin R.L., Krych-Goldberg M., Wang X., Hauhart R.E.,
RA Bromek K., Uhrin D., Atkinson J.P., Barlow P.N.;
RT "Structure of the C3b binding site of CR1 (CD35), the immune adherence
RT receptor.";
RL Cell 108:769-780(2002).
CC -!- FUNCTION: Membrane immune adherence receptor that plays a critical role
CC in the capture and clearance of complement-opsonized pathogens by
CC erythrocytes and monocytes/macrophages (PubMed:2963069). Mediates the
CC binding by these cells of particles and immune complexes that have
CC activated complement to eliminate them from the circulation
CC (PubMed:2963069). Acts also in the inhibition of spontaneous complement
CC activation by impairing the formation and function of the alternative
CC and classical pathway C3/C5 convertases, and by serving as a cofactor
CC for the cleavage by factor I of C3b to iC3b, C3c and C3d,g, and of C4b
CC to C4c and C4d (PubMed:2972794, PubMed:8175757). Also plays a role in
CC immune regulation by contributing, upon ligand binding, to the
CC generation of regulatory T cells from activated helper T cells
CC (PubMed:25742728). {ECO:0000269|PubMed:25742728,
CC ECO:0000269|PubMed:2963069, ECO:0000269|PubMed:2972794,
CC ECO:0000269|PubMed:8175757}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Epstein-Barr
CC virus. {ECO:0000269|PubMed:23416052}.
CC -!- SUBUNIT: Interacts (via Sushi 1 and Sushi 2 domains) with complement
CC factor C4b (PubMed:2972794, PubMed:8175757). Interacts (via Sushi 8 and
CC Sushi 9 domains) with complement factor C3b (PubMed:2972794,
CC PubMed:8175757). Interacts (via Sushi 24 and Sushi 25 domains) with
CC MBL2 (PubMed:23460739, PubMed:29563915). Interacts with FCN2
CC (PubMed:2972794). Interacts (via Sushi 24 and Sushi 25 domains) with
CC C1QA (PubMed:9324355, PubMed:29563915). {ECO:0000269|PubMed:23460739,
CC ECO:0000269|PubMed:29563915, ECO:0000269|PubMed:2972794,
CC ECO:0000269|PubMed:8175757, ECO:0000269|PubMed:9324355}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus gp350.
CC {ECO:0000269|PubMed:23460739}.
CC -!- INTERACTION:
CC P17927; Q15485: FCN2; NbExp=7; IntAct=EBI-2807625, EBI-7468784;
CC P17927; O75636: FCN3; NbExp=2; IntAct=EBI-2807625, EBI-11786958;
CC P17927; P11226: MBL2; NbExp=8; IntAct=EBI-2807625, EBI-5325353;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:1385479}; Single-
CC pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Present on erythrocytes, a subset of T cells,
CC mature B cells, follicular dendritic cells, monocytes and granulocytes.
CC {ECO:0000269|PubMed:1534036, ECO:0000269|PubMed:25742728,
CC ECO:0000269|PubMed:6233222}.
CC -!- POLYMORPHISM: CR1 contains a system of antigens called the Knops blood
CC group system. Polymorphisms within this system are involved in malarial
CC rosetting, a process associated with cerebral malaria, the major cause
CC of mortality in Plasmodium falciparum malaria. Common Knops system
CC antigens include McCoy (McC) and Sl(a)/Vil (Kn4, or Swain-Langley; Vil
CC or Villien). Sl(a-) phenotype is more common in persons of African
CC descent and may protect against fatal malaria.
CC -!- POLYMORPHISM: Other polymorphic forms of CR1 contain 23, 37 or 44 Sushi
CC (CCP/SCR) domains instead of the 30 Sushi (CCP/SCR) domains. The most
CC frequent alleles are the F allotype (shown here) and the S allotype (37
CC repeat Sushi domains). The gene frequencies of the F allotype and S
CC allotype are 0.87 and 0.11 in Caucasians, 0.82 and 0.11 in African
CC Americans, 0.89 and 0.11 in Mexicans.
CC -!- POLYMORPHISM: Genetic variations in CR1 resulting in CR1 deficiency are
CC involved in protection against severe malaria [MIM:611162]. Parasitized
CC red blood cells (RBCs) from children suffering from severe malaria
CC often adhere to complement receptor 1 (CR1) on uninfected RBCs to form
CC clumps of cells known as rosettes. CR1-deficient red blood cells show
CC greatly reduced rosetting and CR1 deficiency occurs in healthy
CC individuals from malaria-endemic regions.
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=knops";
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DR EMBL; Y00816; CAA68755.1; -; mRNA.
DR EMBL; L17418; AAB60694.1; -; Genomic_DNA.
DR EMBL; L17390; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17399; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17409; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17419; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17420; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17421; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17422; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17423; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17391; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17392; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17393; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17394; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17395; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17396; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17397; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17398; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17400; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17401; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17402; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17403; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17404; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17405; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17406; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17407; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17408; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17410; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17411; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17412; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17413; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17414; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17415; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17416; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17417; AAB60694.1; JOINED; Genomic_DNA.
DR EMBL; L17418; AAB60695.1; -; Genomic_DNA.
DR EMBL; L17390; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17391; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17392; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17393; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17394; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17395; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17396; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17397; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17398; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17399; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17400; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17401; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17402; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17403; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17404; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17405; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17406; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17407; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17408; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17409; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17410; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17411; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17412; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17413; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17414; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17415; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17416; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17417; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17419; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17420; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17421; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17422; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17423; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17424; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17425; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17426; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17427; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17428; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17429; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; L17430; AAB60695.1; JOINED; Genomic_DNA.
DR EMBL; AL137789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X14362; CAA32541.1; -; mRNA.
DR EMBL; X05309; CAA28933.1; -; mRNA.
DR EMBL; M11569; AAA52297.1; -; mRNA.
DR EMBL; M11617; AAA52298.1; -; mRNA.
DR EMBL; M11618; AAA52299.1; -; mRNA.
DR CCDS; CCDS44309.1; -.
DR PIR; I73012; I73012.
DR RefSeq; NP_000564.2; NM_000573.3.
DR RefSeq; NP_000642.3; NM_000651.4.
DR PDB; 1GKG; NMR; -; A=1002-1133.
DR PDB; 1GKN; NMR; -; A=942-1065.
DR PDB; 1PPQ; NMR; -; A=1002-1065.
DR PDB; 2MCY; NMR; -; A=102-233.
DR PDB; 2MCZ; NMR; -; A=41-163.
DR PDB; 2Q7Z; X-ray; -; A=42-1972.
DR PDB; 5FO9; X-ray; 3.30 A; C/F=941-1136.
DR PDBsum; 1GKG; -.
DR PDBsum; 1GKN; -.
DR PDBsum; 1PPQ; -.
DR PDBsum; 2MCY; -.
DR PDBsum; 2MCZ; -.
DR PDBsum; 2Q7Z; -.
DR PDBsum; 5FO9; -.
DR AlphaFoldDB; P17927; -.
DR BMRB; P17927; -.
DR SMR; P17927; -.
DR BioGRID; 107769; 2.
DR IntAct; P17927; 12.
DR ChEMBL; CHEMBL3713643; -.
DR GlyConnect; 1929; 8 N-Linked glycans (5 sites).
DR GlyGen; P17927; 21 sites, 8 N-linked glycans (5 sites).
DR iPTMnet; P17927; -.
DR PhosphoSitePlus; P17927; -.
DR BioMuta; CR1; -.
DR DMDM; 290457678; -.
DR EPD; P17927; -.
DR jPOST; P17927; -.
DR MassIVE; P17927; -.
DR PaxDb; P17927; -.
DR PeptideAtlas; P17927; -.
DR PRIDE; P17927; -.
DR ProteomicsDB; 53525; -.
DR ABCD; P17927; 14 sequenced antibodies.
DR Antibodypedia; 4269; 1260 antibodies from 45 providers.
DR DNASU; 1378; -.
DR Ensembl; ENST00000367051.6; ENSP00000356018.1; ENSG00000203710.12.
DR Ensembl; ENST00000367053.6; ENSP00000356020.1; ENSG00000203710.12.
DR Ensembl; ENST00000400960.7; ENSP00000383744.2; ENSG00000203710.12.
DR GeneID; 1378; -.
DR KEGG; hsa:1378; -.
DR UCSC; uc057ozo.1; human.
DR CTD; 1378; -.
DR DisGeNET; 1378; -.
DR GeneCards; CR1; -.
DR HGNC; HGNC:2334; CR1.
DR HPA; ENSG00000203710; Tissue enhanced (adipose tissue, lymphoid tissue).
DR MalaCards; CR1; -.
DR MIM; 120620; gene.
DR MIM; 607486; phenotype.
DR MIM; 611162; phenotype.
DR neXtProt; NX_P17927; -.
DR NIAGADS; ENSG00000203710; -.
DR PharmGKB; PA26855; -.
DR VEuPathDB; HostDB:ENSG00000203710; -.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_233290_0_0_1; -.
DR InParanoid; P17927; -.
DR OrthoDB; 46968at2759; -.
DR PhylomeDB; P17927; -.
DR PathwayCommons; P17927; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P17927; -.
DR SIGNOR; P17927; -.
DR BioGRID-ORCS; 1378; 11 hits in 1066 CRISPR screens.
DR ChiTaRS; CR1; human.
DR EvolutionaryTrace; P17927; -.
DR GeneWiki; Complement_receptor_1; -.
DR GenomeRNAi; 1378; -.
DR Pharos; P17927; Tbio.
DR PRO; PR:P17927; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P17927; protein.
DR Bgee; ENSG00000203710; Expressed in blood and 122 other tissues.
DR ExpressionAtlas; P17927; baseline and differential.
DR Genevisible; P17927; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0044853; C:plasma membrane raft; IDA:ARUK-UCL.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0001851; F:complement component C3b binding; IDA:UniProtKB.
DR GO; GO:0004877; F:complement component C3b receptor activity; IDA:UniProtKB.
DR GO; GO:0001855; F:complement component C4b binding; IDA:UniProtKB.
DR GO; GO:0001861; F:complement component C4b receptor activity; IDA:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:1904669; P:ATP export; IDA:ARUK-UCL.
DR GO; GO:0006957; P:complement activation, alternative pathway; IMP:ARUK-UCL.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IDA:ARUK-UCL.
DR GO; GO:0002435; P:immune complex clearance by erythrocytes; IDA:ARUK-UCL.
DR GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IDA:ARUK-UCL.
DR GO; GO:0045916; P:negative regulation of complement activation; IDA:ARUK-UCL.
DR GO; GO:0045957; P:negative regulation of complement activation, alternative pathway; IDA:UniProtKB.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IDA:UniProtKB.
DR GO; GO:0045918; P:negative regulation of cytolysis; IDA:ARUK-UCL.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; IDA:ARUK-UCL.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:ARUK-UCL.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:ARUK-UCL.
DR GO; GO:1900099; P:negative regulation of plasma cell differentiation; IDA:ARUK-UCL.
DR GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:ARUK-UCL.
DR GO; GO:0007009; P:plasma membrane organization; IDA:ARUK-UCL.
DR GO; GO:0001970; P:positive regulation of activation of membrane attack complex; IMP:ARUK-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:ARUK-UCL.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IDA:ARUK-UCL.
DR GO; GO:1900005; P:positive regulation of serine-type endopeptidase activity; IDA:UniProtKB.
DR CDD; cd00033; CCP; 30.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 30.
DR SMART; SM00032; CCP; 30.
DR SUPFAM; SSF57535; SSF57535; 30.
DR PROSITE; PS50923; SUSHI; 30.
PE 1: Evidence at protein level;
KW 3D-structure; Blood group antigen; Complement pathway; Disulfide bond;
KW Glycoprotein; Host cell receptor for virus entry; Host-virus interaction;
KW Immunity; Innate immunity; Membrane; Pyrrolidone carboxylic acid; Receptor;
KW Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..41
FT CHAIN 42..2039
FT /note="Complement receptor type 1"
FT /id="PRO_0000006009"
FT TOPO_DOM 42..1971
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1972..1996
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1997..2039
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..101
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 102..163
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 164..234
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 236..295
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 295..355
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 356..418
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 419..489
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 491..551
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 552..613
FT /note="Sushi 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 614..684
FT /note="Sushi 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 686..745
FT /note="Sushi 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 745..805
FT /note="Sushi 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 806..868
FT /note="Sushi 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 869..939
FT /note="Sushi 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 941..1001
FT /note="Sushi 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1002..1063
FT /note="Sushi 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1064..1134
FT /note="Sushi 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1136..1195
FT /note="Sushi 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1195..1255
FT /note="Sushi 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1256..1318
FT /note="Sushi 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1319..1389
FT /note="Sushi 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1394..1454
FT /note="Sushi 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1455..1516
FT /note="Sushi 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1517..1587
FT /note="Sushi 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1589..1648
FT /note="Sushi 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1648..1708
FT /note="Sushi 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1709..1771
FT /note="Sushi 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1772..1842
FT /note="Sushi 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1846..1906
FT /note="Sushi 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1907..1967
FT /note="Sushi 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 2017..2039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2020..2039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 959
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 73..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 104..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 131..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 166..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 195..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 238..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 266..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 297..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 326..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 358..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 386..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 421..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 450..487
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 493..536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 523..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 554..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 581..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 616..665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 645..682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 688..730
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 716..743
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 747..790
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 776..803
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 808..850
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 836..866
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 871..920
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 900..937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 943..986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 973..999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1004..1045
FT DISULFID 1031..1061
FT DISULFID 1066..1115
FT DISULFID 1095..1132
FT DISULFID 1138..1180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1166..1193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1197..1240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1226..1253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1258..1300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1286..1316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1321..1370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1350..1387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1396..1439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1426..1452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1457..1498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1484..1514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1519..1568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1548..1585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1591..1633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1619..1646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1650..1693
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1679..1706
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1711..1753
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1739..1769
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1774..1823
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1803..1840
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1848..1891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1877..1904
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1909..1952
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1938..1965
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VARIANT 1208
FT /note="H -> R (in dbSNP:rs2274567)"
FT /evidence="ECO:0000269|PubMed:11313284"
FT /id="VAR_013819"
FT VARIANT 1408
FT /note="T -> I"
FT /id="VAR_013820"
FT VARIANT 1408
FT /note="T -> M (in dbSNP:rs3737002)"
FT /id="VAR_020263"
FT VARIANT 1540
FT /note="N -> S (in dbSNP:rs17259045)"
FT /id="VAR_055685"
FT VARIANT 1590
FT /note="K -> E (in MCC(b) antigen; dbSNP:rs17047660)"
FT /evidence="ECO:0000269|PubMed:11313284"
FT /id="VAR_013821"
FT VARIANT 1601
FT /note="R -> G (in Sl(2)/Vil antigen and Sl(3) antigen;
FT dbSNP:rs17047661)"
FT /evidence="ECO:0000269|PubMed:11313284,
FT ECO:0000269|PubMed:11896343"
FT /id="VAR_013822"
FT VARIANT 1610
FT /note="S -> T (in Sl(3) antigen; dbSNP:rs4844609)"
FT /evidence="ECO:0000269|PubMed:11313284,
FT ECO:0000269|PubMed:11896343, ECO:0000269|PubMed:16710414"
FT /id="VAR_013823"
FT VARIANT 1615
FT /note="I -> V (in dbSNP:rs6691117)"
FT /evidence="ECO:0000269|PubMed:11313284,
FT ECO:0000269|PubMed:8245463"
FT /id="VAR_013824"
FT VARIANT 1827
FT /note="P -> R (in dbSNP:rs3811381)"
FT /evidence="ECO:0000269|PubMed:11313284,
FT ECO:0000269|PubMed:8245463"
FT /id="VAR_013825"
FT VARIANT 1850
FT /note="H -> D"
FT /evidence="ECO:0000269|PubMed:11313284,
FT ECO:0000269|PubMed:8245463"
FT /id="VAR_013826"
FT VARIANT 1969
FT /note="T -> A (in dbSNP:rs2296160)"
FT /evidence="ECO:0000269|PubMed:2951479,
FT ECO:0000269|PubMed:8245463"
FT /id="VAR_055686"
FT CONFLICT 445
FT /note="T -> A (in Ref. 1; CAA68755, 2; AAB60694 and 5;
FT CAA32541)"
FT /evidence="ECO:0000305"
FT CONFLICT 1876
FT /note="I -> T (in Ref. 1; CAA68755 and 6; CAA28933)"
FT /evidence="ECO:0000305"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2MCZ"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2MCZ"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2MCZ"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2MCZ"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2MCZ"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:2MCY"
FT STRAND 950..954
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 961..963
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 971..973
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 977..979
FT /evidence="ECO:0007829|PDB:1GKN"
FT STRAND 982..986
FT /evidence="ECO:0007829|PDB:1GKN"
FT STRAND 988..990
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1013..1017
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1026..1031
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1035..1039
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1041..1047
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1049..1056
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1060..1063
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1089..1093
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1107..1109
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1113..1116
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1118..1122
FT /evidence="ECO:0007829|PDB:5FO9"
FT STRAND 1124..1126
FT /evidence="ECO:0007829|PDB:5FO9"
SQ SEQUENCE 2039 AA; 223663 MW; FB01870F19D5E6DD CRC64;
MGASSPRSPE PVGPPAPGLP FCCGGSLLAV VVLLALPVAW GQCNAPEWLP FARPTNLTDE
FEFPIGTYLN YECRPGYSGR PFSIICLKNS VWTGAKDRCR RKSCRNPPDP VNGMVHVIKG
IQFGSQIKYS CTKGYRLIGS SSATCIISGD TVIWDNETPI CDRIPCGLPP TITNGDFIST
NRENFHYGSV VTYRCNPGSG GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP
PNVENGILVS DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP
PDVLHAERTQ RDKDNFSPGQ EVFYSCEPGY DLRGAASMRC TPQGDWSPAA PTCEVKSCDD
FMGQLLNGRV LFPVNLQLGA KVDFVCDEGF QLKGSSASYC VLAGMESLWN SSVPVCEQIF
CPSPPVIPNG RHTGKPLEVF PFGKTVNYTC DPHPDRGTSF DLIGESTIRC TSDPQGNGVW
SSPAPRCGIL GHCQAPDHFL FAKLKTQTNA SDFPIGTSLK YECRPEYYGR PFSITCLDNL
VWSSPKDVCK RKSCKTPPDP VNGMVHVITD IQVGSRINYS CTTGHRLIGH SSAECILSGN
AAHWSTKPPI CQRIPCGLPP TIANGDFIST NRENFHYGSV VTYRCNPGSG GRKVFELVGE
PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS DNRSLFSLNE VVEFRCQPGF
VMKGPRRVKC QALNKWEPEL PSCSRVCQPP PDVLHAERTQ RDKDNFSPGQ EVFYSCEPGY
DLRGAASMRC TPQGDWSPAA PTCEVKSCDD FMGQLLNGRV LFPVNLQLGA KVDFVCDEGF
QLKGSSASYC VLAGMESLWN SSVPVCEQIF CPSPPVIPNG RHTGKPLEVF PFGKAVNYTC
DPHPDRGTSF DLIGESTIRC TSDPQGNGVW SSPAPRCGIL GHCQAPDHFL FAKLKTQTNA
SDFPIGTSLK YECRPEYYGR PFSITCLDNL VWSSPKDVCK RKSCKTPPDP VNGMVHVITD
IQVGSRINYS CTTGHRLIGH SSAECILSGN TAHWSTKPPI CQRIPCGLPP TIANGDFIST
NRENFHYGSV VTYRCNLGSR GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP
PNVENGILVS DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP
PEILHGEHTP SHQDNFSPGQ EVFYSCEPGY DLRGAASLHC TPQGDWSPEA PRCAVKSCDD
FLGQLPHGRV LFPLNLQLGA KVSFVCDEGF RLKGSSVSHC VLVGMRSLWN NSVPVCEHIF
CPNPPAILNG RHTGTPSGDI PYGKEISYTC DPHPDRGMTF NLIGESTIRC TSDPHGNGVW
SSPAPRCELS VRAGHCKTPE QFPFASPTIP INDFEFPVGT SLNYECRPGY FGKMFSISCL
ENLVWSSVED NCRRKSCGPP PEPFNGMVHI NTDTQFGSTV NYSCNEGFRL IGSPSTTCLV
SGNNVTWDKK APICEIISCE PPPTISNGDF YSNNRTSFHN GTVVTYQCHT GPDGEQLFEL
VGERSIYCTS KDDQVGVWSS PPPRCISTNK CTAPEVENAI RVPGNRSFFS LTEIIRFRCQ
PGFVMVGSHT VQCQTNGRWG PKLPHCSRVC QPPPEILHGE HTLSHQDNFS PGQEVFYSCE
PSYDLRGAAS LHCTPQGDWS PEAPRCTVKS CDDFLGQLPH GRVLLPLNLQ LGAKVSFVCD
EGFRLKGRSA SHCVLAGMKA LWNSSVPVCE QIFCPNPPAI LNGRHTGTPF GDIPYGKEIS
YACDTHPDRG MTFNLIGESS IRCTSDPQGN GVWSSPAPRC ELSVPAACPH PPKIQNGHYI
GGHVSLYLPG MTISYICDPG YLLVGKGFIF CTDQGIWSQL DHYCKEVNCS FPLFMNGISK
ELEMKKVYHY GDYVTLKCED GYTLEGSPWS QCQADDRWDP PLAKCTSRTH DALIVGTLSG
TIFFILLIIF LSWIILKHRK GNNAHENPKE VAIHLHSQGG SSVHPRTLQT NEENSRVLP
