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UniProtKB/Swiss-Prot entry P00736


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

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Entry information
Entry name C1R_HUMAN
Primary accession number P00736
Secondary accession number Q8J012
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on August 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 119)
Name and origin of the protein
Protein name Complement C1r subcomponent [Precursor]
Synonyms EC 3.4.21.41
Complement component 1, r subcomponent
Contains Complement C1r subcomponent heavy chain
Complement C1r subcomponent light chain
Gene name
Name: C1R
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00365a020; PubMed=3021205 [NCBI, ExPASy, EBI, Israel, Japan]
Leytus S.P., Kurachi K., Sakariassen K.S., Davie E.W.;
"Nucleotide sequence of the cDNA coding for human complement C1r.";
Biochemistry 25:4855-4863(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-152.
PubMed=3030286 [NCBI, ExPASy, EBI, Israel, Japan]
Journet A., Tosi M.;
"Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r.";
Biochem. J. 240:783-787(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-131; LEU-152; TYR-163; LYS-184 AND ARG-261.
DOI=10.1046/j.1469-1809.2003.00019.x; PubMed=12914573 [NCBI, ExPASy, EBI, Israel, Japan]
Nakagawa M., Yuasa I., Irizawa Y., Umetsu K.;
"The human complement component C1R gene: the exon-intron structure and the molecular basis of allelic diversity.";
Ann. Hum. Genet. 67:207-215(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-152.
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 18-463.
PubMed=3036070 [NCBI, ExPASy, EBI, Israel, Japan]
Arlaud G.J., Willis A.C., Gagnon J.;
"Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r.";
Biochem. J. 241:711-720(1987).
[6]
PROTEIN SEQUENCE OF 464-705.
DOI=10.1021/bi00277a003; PubMed=6303394 [NCBI, ExPASy, EBI, Israel, Japan]
Arlaud G.J., Gagnon J.;
"Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r.";
Biochemistry 22:1758-1764(1983).
[7]
PROTEIN SEQUENCE OF 152-186, AND HYDROXYLATION.
DOI=10.1016/0014-5793(87)80205-3; PubMed=2820791 [NCBI, ExPASy, EBI, Israel, Japan]
Arlaud G.J., van Dorsselaer A., Bell A., Mancini M., Aude C., Gagnon J.;
"Identification of erythro-beta-hydroxyasparagine in the EGF-like domain of human C1r.";
FEBS Lett. 222:129-134(1987).
[8]
PROTEIN SEQUENCE OF 133-137; 187-211 AND 609-613, AND PHOSPHORYLATION.
DOI=10.1016/0014-5793(96)00403-6; PubMed=8635594 [NCBI, ExPASy, EBI, Israel, Japan]
Pelloux S., Thielens N.M., Hudry-Clergeon G., Petillot Y., Filhol O., Arlaud G.J.;
"Identification of a cryptic protein kinase CK2 phosphorylation site in human complement protease Clr, and its use to probe intramolecular interaction.";
FEBS Lett. 386:15-20(1996).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125; ASN-221 AND ASN-514, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[10]
STRUCTURE BY NMR OF 140-192.
DOI=10.1021/bi971851v; PubMed=9477945 [NCBI, ExPASy, EBI, Israel, Japan]
Bersch B., Hernandez J.-F., Marion D., Arlaud G.J.;
"Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family.";
Biochemistry 37:1204-1214(1998).
[11]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 307-702.
DOI=10.1093/emboj/21.3.231; PubMed=11823416 [NCBI, ExPASy, EBI, Israel, Japan]
Budayova-Spano M., Lacroix M., Thielens N.M., Arlaud G.J., Fontecilla-Camps J.-C., Gaboriaud C.;
"The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex.";
EMBO J. 21:231-239(2002).
[12]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 375-702.
DOI=10.1016/S0969-2126(02)00881-X; PubMed=12429092 [NCBI, ExPASy, EBI, Israel, Japan]
Budayova-Spano M., Grabarse W., Thielens N.M., Hillen H., Lacroix M., Schmidt M., Fontecilla-Camps J.-C., Arlaud G.J., Gaboriaud C.;
"Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism.";
Structure 10:1509-1519(2002).
[13]
VARIANT LEU-152.
DOI=10.1093/hmg/3.1.217-a; PubMed=8162045 [NCBI, ExPASy, EBI, Israel, Japan]
Nothen M.M., Dewald G.;
"A common amino acid polymorphism in complement component C1R.";
Hum. Mol. Genet. 3:217-217(1994).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X04701; CAA28407.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14058; AAA51851.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB083037; BAC19850.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC035220; AAH35220.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A24170; C1HURB.
RefSeq NP_001724.3; -.
UniGene Hs.524224
3D structure databases
PDB
1APQ; NMR; -; A=140-192.[ExPASy / RCSB / EBI]
1GPZ; X-ray; 2.90 A; A/B=307-705.[ExPASy / RCSB / EBI]
1MD7; X-ray; 3.20 A; A=375-702.[ExPASy / RCSB / EBI]
1MD8; X-ray; 2.80 A; A=375-703.[ExPASy / RCSB / EBI]
2QY0; X-ray; 2.60 A; A/C=309-463, B/D=464-705.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1APQ; -.
1GPZ; -.
1MD7; -.
1MD8; -.
2QY0; -.
ModBase P00736.
Protein family/group databases
MEROPS S01.192; -.
PTM databases
PhosphoSite P00736; -.
Enzyme and pathway databases
Reactome REACT_6900; Signaling in Immune System.
Organism-specific databases
H-InvDB HIX0036748; -.
HIX0060170; -.
HGNC HGNC:1246; C1R.
GenAtlas C1R.
HPA HPA001551; -.
MIM 216950; gene+phenotype. [NCBI / EBI]
PharmGKB PA25635; -.
GeneCards P00736.
Gene expression databases
CleanEx HS_C1R; -.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0003815; Molecular function: complement component C1r activity (inferred from experiment from Reactome).
GO:0004252; Molecular function: serine-type endopeptidase activity (traceable author statement from ProtInc).
GO:0006955; Biological process: immune response (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR016060; Complement_control_module.
IPR000859; CUB.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR013091; EGF_Ca_bd_2.
IPR013032; EGF_like_reg_CS.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR000436; Sushi_SCR_CCP.
Graphical view of domain structure.
Gene3D G3DSA:2.10.70.10; Complement_control_module; 1.
G3DSA:2.60.120.290; CUB; 2.
Pfam PF00431; CUB; 2.
PF07645; EGF_CA; 1.
PF00084; Sushi; 2.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
SMART SM00032; CCP; 2.
SM00042; CUB; 2.
SM00179; EGF_CA; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS00010; ASX_HYDROXYL; 1.
PS01180; CUB; 2.
PS00022; EGF_1; FALSE_NEG.
PS01186; EGF_2; 1.
PS50026; EGF_3; FALSE_NEG.
PS01187; EGF_CA; 1.
PS50923; SUSHI; 2.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; FALSE_NEG.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00736.
ProtoNet P00736.
Proteomic databases
PeptideAtlas P00736; -.
Genome annotation databases
Ensembl ENSG00000159403; Homo sapiens. [Contig view]
GeneID 715; -.
KEGG hsa:715; -.
Phylogenomic databases
HOVERGEN P00736; -.
Other
DrugBank DB00054; Abciximab.
DB00051; Adalimumab.
DB00092; Alefacept.
DB00087; Alemtuzumab.
DB00074; Basiliximab.
DB00112; Bevacizumab.
DB00002; Cetuximab.
DB00111; Daclizumab.
DB00095; Efalizumab.
DB00005; Etanercept.
DB00056; Gemtuzumab ozogamicin.
DB00078; Ibritumomab.
DB00028; Immune globulin.
DB00075; Muromonab.
DB00108; Natalizumab.
DB00110; Palivizumab.
DB00073; Rituximab.
DB00081; Tositumomab.
DB00072; Trastuzumab.
LinkHub P00736; -.
NextBio 2906; -.
SOURCE C1R; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complement pathway; Direct protein sequencing; EGF-like domain; Glycoprotein; Hydrolase; Hydroxylation; Immune response; Innate immunity; Phosphoprotein; Polymorphism; Protease; Repeat; Serine protease; Signal; Sushi.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    17  17      
CHAIN   18   705  688     Complement C1r subcomponent. PRO_0000027577
CHAIN   18   463  446     Complement C1r subcomponent heavy chain. PRO_0000027578
CHAIN   464   705  242     Complement C1r subcomponent light chain. PRO_0000027579
DOMAIN   18   141  124     CUB 1. 
DOMAIN   142   190  49     EGF-like; calcium-binding (Potential). 
DOMAIN   193   305  113     CUB 2. 
DOMAIN   307   373  67     Sushi 1. 
DOMAIN   374   449  76     Sushi 2. 
DOMAIN   464   702  239     Peptidase S1. 
ACT_SITE   502   502        Charge relay system. 
ACT_SITE   557   557        Charge relay system. 
ACT_SITE   654   654        Charge relay system. 
MOD_RES   167   167        3-hydroxyasparagine. 
MOD_RES   206   206        Phosphoserine; by CK2. 
CARBOHYD   125   125        N-linked (GlcNAc...). 
CARBOHYD   221   221        N-linked (GlcNAc...). 
CARBOHYD   514   514        N-linked (GlcNAc...). 
CARBOHYD   581   581        N-linked (GlcNAc...). 
DISULFID   71    89        Probable. 
DISULFID   146   165         
DISULFID   161   174         
DISULFID   176   189         
DISULFID   193   220        Probable. 
DISULFID   250   268        Probable. 
DISULFID   309   358         
DISULFID   338   371         
DISULFID   376   429         
DISULFID   406   447         
DISULFID   451   577        Interchain (between heavy and light chains). 
DISULFID   620   639         
DISULFID   650   680         
VARIANT   131   131  1     Y -> H. VAR_018667 
VARIANT   152   152  1     S -> L (common polymorphism; dbSNP:rs1801046 [NCBI]). VAR_016103 
VARIANT   163   163  1     H -> Y. VAR_018668 
VARIANT   184   184  1     E -> K. VAR_018669 
VARIANT   261   261  1     G -> R. VAR_018670 
TURN   145   147  3      
TURN   150   152  3      
STRAND   156   158  3      
STRAND   162   168  7      
STRAND   171   175  5      
STRAND   319   323  5      
STRAND   326   328  3      
STRAND   333   338  6      
STRAND   342   348  7      
STRAND   350   352  3      
STRAND   354   358  5      
STRAND   364   366  3      
STRAND   370   373  4      
STRAND   385   392  8      
STRAND   401   406  6      
TURN   408   410  3      
STRAND   411   414  4      
STRAND   426   429  4      
STRAND   433   440  8      
STRAND   446   449  4      
STRAND   478   492  15      
TURN   493   495  3      
STRAND   496   499  4      
HELIX   501   503  3      
STRAND   518   522  5      
HELIX   526   531  6      
STRAND   537   542  6      
STRAND   548   552  5      
STRAND   559   565  7      
HELIX   582   585  4      
STRAND   590   595  6      
STRAND   608   615  8      
HELIX   617   621  5      
STRAND   636   641  6      
HELIX   643   650  8      
STRAND   657   662  6      
TURN   663   666  4      
STRAND   667   674  8      
TURN   678   683  6      
STRAND   684   689  6      
HELIX   690   693  4      
HELIX   694   700  7      
Sequence information
Length: 705 AA [This is the length of the unprocessed precursor] Molecular weight: 80174 Da [This is the MW of the unprocessed precursor] CRC64: 5CBCCC0201061463 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWLLYLLVPA LFCRAGGSIP IPQKLFGEVT SPLFPKPYPN NFETTTVITV PTGYRVKLVF 

        70         80         90        100        110        120 
QQFDLEPSEG CFYDYVKISA DKKSLGRFCG QLGSPLGNPP GKKEFMSQGN KMLLTFHTDF 

       130        140        150        160        170        180 
SNEENGTIMF YKGFLAYYQA VDLDECASRS KSGEEDPQPQ CQHLCHNYVG GYFCSCRPGY 

       190        200        210        220        230        240 
ELQEDRHSCQ AECSSELYTE ASGYISSLEY PRSYPPDLRC NYSIRVERGL TLHLKFLEPF 

       250        260        270        280        290        300 
DIDDHQQVHC PYDQLQIYAN GKNIGEFCGK QRPPDLDTSS NAVDLLFFTD ESGDSRGWKL 

       310        320        330        340        350        360 
RYTTEIIKCP QPKTLDEFTI IQNLQPQYQF RDYFIATCKQ GYQLIEGNQV LHSFTAVCQD 

       370        380        390        400        410        420 
DGTWHRAMPR CKIKDCGQPR NLPNGDFRYT TTMGVNTYKA RIQYYCHEPY YKMQTRAGSR 

       430        440        450        460        470        480 
ESEQGVYTCT AQGIWKNEQK GEKIPRCLPV CGKPVNPVEQ RQRIIGGQKA KMGNFPWQVF 

       490        500        510        520        530        540 
TNIHGRGGGA LLGDRWILTA AHTLYPKEHE AQSNASLDVF LGHTNVEELM KLGNHPIRRV 

       550        560        570        580        590        600 
SVHPDYRQDE SYNFEGDIAL LELENSVTLG PNLLPICLPD NDTFYDLGLM GYVSGFGVME 

       610        620        630        640        650        660 
EKIAHDLRFV RLPVANPQAC ENWLRGKNRM DVFSQNMFCA GHPSLKQDAC QGDSGGVFAV 

       670        680        690        700 
RDPNTDRWVA TGIVSWGIGC SRGYGFYTKV LNYVDWIKKE MEEED 

P00736 in FASTA format

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