| ID |
3814 |
| Name |
Complement C1r subcomponent |
| Synonyms |
- EC 3.4.21.41
- Complement component 1, r subcomponent
- Complement C1r subcomponent precursor
|
| Gene Name |
C1R |
| Protein Sequence |
>Complement C1r subcomponent
MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVF
QQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDF
SNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGY
ELQEDRHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPF
DIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKL
RYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQD
DGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSR
ESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVF
TNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRV
SVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVME
EKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAV
RDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED
|
| Number of Residues |
705 |
| Molecular Weight |
80174 |
| Theoretical pI |
6.24 |
| GO Classification |
| Component |
| extracellular region |
| Function |
| calcium ion binding |
| peptidase activity |
| endopeptidase activity |
| binding |
| serine-type endopeptidase activity |
| catalytic activity |
| ion binding |
| cation binding |
| hydrolase activity |
| Process |
| physiological process |
| proteolysis |
| response to stimulus |
| response to biotic stimulus |
| metabolism |
| defense response |
| immune response |
| macromolecule metabolism |
| humoral immune response |
| protein metabolism |
| complement activation |
| cellular protein metabolism |
|
| General Function |
Not Available |
| Specific Function |
C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system |
| Pathways |
Not Available |
| Reactions |
- Selective cleavage of Lys(or Arg)!Ile bond in complement subcomponent C1s to form C_overbar_1s_ (internal_xref(ec_num(3,4,21,42)))
|
| Pfam Domain Function |
|
| Signals |
1-17 |
| Transmembrane Regions |
None |
| Essentiality |
Non-Essential |
| GenBank Protein ID |
29539  |
| UniProtKB ID |
P00736 |
| UniProtKB Entry Name |
C1R_HUMAN |
| PDB ID |
1GPZ |
| PDB File |
show |
| 3D Structure |
View 3D Structure |
| Cellular Location |
Cytoplasmic |
| Gene Sequence |
>2118 bp
ATGTGGCTCTTGTACCTCCTGGTGCCGGCCCTGTTCTGCAGGGCAGGAGGCTCCATTCCC
ATCCCTCAGAAGTTATTTGGGGAGGTGACTTCCCCTCTGTTCCCCAAGCCTTACCCCAAC
AACTTTGAAACAACCACTGTGATCACAGTCCCCACGGGATACAGGGTGAAGCTCGTCTTC
CAGCAGTTTGACCTGGAGCCTTCTGAAGGCTGCTTCTATGATTATGTCAAGATCTCTGCT
GATAAGAAAAGCCTGGGGAGGTTCTGTGGGCAACTGGGTTCTCCACTGGGCAACCCCCCG
GGAAAGAAGGAATTTATGTCCCAAGGGAACAAGATGCTGCTGACCTTCCACACAGACTTC
TCCAACGAGGAGAATGGGACCATCATGTTCTACAAGGGCTTCCTGGCCTACTACCAAGCT
GTGGACCTTGATGAATGTGCTTCCCGGAGCAAATTAGGGGAGGAGGATCCCCAGCCCCAG
TGCCAGCACCTGTGTCACAACTACGTTGGAGGCTACTTCTGTTCCTGCCGTCCAGGCTAT
GAGCTTCAGGAAGACAGGCATTCCTGCCAGGCTGAGTGCAGCAGCGAGCTGTACACGGAG
GCATCAGGCTACATCTCCAGCCTGGAGTACCCTCGGTCCTACCCCCCTGACCTGCGCTGC
AACTACAGCATCCGGGTGGAGCGGGGCCTCACCCTGCACCTCAAGTTCCTGGAGCCTTTT
GATATTGATGACCACCAGCAAGTACACTGCCCCTATGACCAGCTACAGATCTATGCCAAC
GGGAAGAACATTGGCGAGTTCTGTGGGAAGCAAAGGCCCCCCGACCTCGACACCAGCAGC
AATGCTGTGGATCTGCTGTTCTTCACAGATGAGTCGGGGGACAGCCGGGGCTGGAAGCTG
CGCTACACCACCGAGATCATCAAGTGCCCCCAGCCCAAGACCCTAGACGAGTTCACCATC
ATCCAGAACCTGCAGCCTCAGTACCAGTTCCGTGACTACTTCATTGCTACCTGCAAGCAA
GGCTACCAGCTCATAGAGGGGAACCAGGTGCTGCATTCCTTCACAGCTGTCTGCCAGGAT
GATGGCACGTGGCATCGTGCCATGCCCAGATGCAAGATCAAGGACTGTGGGCAGCCCCGA
AACCTGCCTAATGGTGACTTCCGTTACACCACCACAATGGGAGTGAACACCTACAAGGCC
CGTATCCAGTACTACTGCCATGAGCCATATTACAAGATGCAGACCAGAGCTGGCAGCAGG
GAGTCTGAGCAAGGGGTGTACACCTGCACAGCACAGGGCATTTGGAAGAATGAACAGAAG
GGAGAGAAGATTCCTCGGTGCTTGCCAGTGTGTGGGAAGCCCGTGAACCCCGTGGAACAG
AGGCAGCGCATCATCGGAGGGCAAAAAGCCAAGATGGGCAACTTCCCCTGGCAGGTGTTC
ACCAACATCCACGGGCGCGGGGGCGGGGCCCTGCTGGGCGACCGCTGGATCCTCACAGCT
GCCCACACCCTGTATCCCAAGGAACACGAAGCGCAAAGCAACGCCTCTTTGGATGTGTTC
CTGGGCCACACAAATGTGGAAGAGCTCATGAAGCTAGGAAATCACCCCATCCGCAGGGTC
AGCGTCCACCCGGACTACCGTCAGGATGAGTCCTACAATTTTGAGGGGGACATCGCCCTG
CTGGAGCTGGAAAATAGTGTCACCCTGGGTCCCAACCTCCTCCCCATCTGCCTCCCTGAC
AACGATACCTTCTACGACCTGGGCTTGATGGGCTATGTCAGTGGCTTCGGGGTCATGGAG
GAGAAGATTGCTCATGACCTCAGGTTTGTCCGTCTGCCCGTAGCTAATCCACAGGCCTGT
GAGAACTGGCTCCGGGGAAAGAATAGGATGGATGTGTTCTCTCAAAACATGTTCTGTGCT
GGACACCCATCTCTAAAGCAGGACGCCTGCCAGGGGGATAGTGGGGGCGTTTTTGCAGTA
AGGGACCCGAACACTGATCGCTGGGTGGCCACGGGCATCGTGTCCTGGGGCATCGGGTGC
AGCAGGGGCTATGGCTTCTACACCAAAGTGCTCAACTACGTGGACTGGATCAAGAAAGAG
ATGGAGGAGGAGGACTGA
|
| GenBank Gene ID |
X04701 |
| GeneCard ID |
C1R |
| GenAtlas ID |
C1R |
| HGNC ID |
HGNC:1246 |
| HPRD ID |
Not Available |
| IUPHAR ID |
Not Available |
| Guide to Pharmacology ID |
Not Available |
| Chromosome Location |
Not Available |
| Locus |
12p13 |
| SNPs |
C1R |
| General References |
- Leytus SP, Kurachi K, Sakariassen KS, Davie EW: Nucleotide sequence of the cDNA coding for human complement C1r. Biochemistry. 1986 Aug 26;25(17):4855-63. Pubmed
- Journet A, Tosi M: Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r. Biochem J. 1986 Dec 15;240(3):783-7. Pubmed
- Arlaud GJ, Willis AC, Gagnon J: Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r. Biochem J. 1987 Feb 1;241(3):711-20. Pubmed
- Arlaud GJ, Gagnon J: Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r. Biochemistry. 1983 Apr 12;22(8):1758-64. Pubmed
- Arlaud GJ, 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. 1987 Sep 28;222(1):129-34. Pubmed
- Pelloux S, Thielens NM, Hudry-Clergeon G, Petillot Y, Filhol O, Arlaud GJ: Identification of a cryptic protein kinase CK2 phosphorylation site in human complement protease Clr, and its use to probe intramolecular interaction. FEBS Lett. 1996 May 13;386(1):15-20. Pubmed
- Bersch B, Hernandez JF, Marion D, Arlaud GJ: Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family. Biochemistry. 1998 Feb 3;37(5):1204-14. Pubmed
|
| Drugs |
| # |
DrugBank ID |
Drug Name |
Drug Type |
Drug Groups |
| 1 |
DB00054 |
Abciximab |
biotech |
approved |
| 2 |
DB00051 |
Adalimumab |
biotech |
approved |
| 3 |
DB00092 |
Alefacept |
biotech |
approved, investigational |
| 4 |
DB00087 |
Alemtuzumab |
biotech |
approved, investigational |
| 5 |
DB02944 |
Alpha-D-Mannose |
small molecule |
experimental |
| 6 |
DB00074 |
Basiliximab |
biotech |
approved, investigational |
| 7 |
DB00112 |
Bevacizumab |
biotech |
approved, investigational |
| 8 |
DB00002 |
Cetuximab |
biotech |
approved |
| 9 |
DB00111 |
Daclizumab |
biotech |
approved, investigational |
| 10 |
DB00095 |
Efalizumab |
biotech |
approved, investigational |
| 11 |
DB00005 |
Etanercept |
biotech |
approved, investigational |
| 12 |
DB00056 |
Gemtuzumab ozogamicin |
biotech |
approved, investigational |
| 13 |
DB00078 |
Ibritumomab |
biotech |
approved |
| 14 |
DB00075 |
Muromonab |
biotech |
approved |
| 15 |
DB00108 |
Natalizumab |
biotech |
approved, investigational |
| 16 |
DB00110 |
Palivizumab |
biotech |
approved, investigational |
| 17 |
DB00073 |
Rituximab |
biotech |
approved |
| 18 |
DB00081 |
Tositumomab |
biotech |
approved |
| 19 |
DB00072 |
Trastuzumab |
biotech |
approved, investigational |
|
