| General information | | DisProt: | DP00621 | | Name: | Complement C1r subcomponent | | Synonym(s): | C1R_HUMAN
Complement component 1 subcomponent r
| | First appeared in release: | Release 5.1 (05/28/2010) | | UniProt: | P00736 | | UniGene: | Hs.524224 | | SwissProt: | C1R_HUMAN | | TrEMBL: | | | NCBI (GI): | 218511956 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 705 | | Percent disordered: | 16% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MWLLYLLVPA LFCRAGGSIP IPQKLFGEVT SPLFPKPYPN NFETTTVITV PTGYRVKLVF - 60
QQFDLEPSEG CFYDYVKISA DKKSLGRFCG QLGSPLGNPP GKKEFMSQGN KMLLTFHTDF - 120
SNEENGTIMF YKGFLAYYQA VDLDECASRS KSGEEDPQPQ CQHLCHNYVG GYFCSCRPGY - 180
ELQEDTHSCQ AECSSELYTE ASGYISSLEY PRSYPPDLRC NYSIRVERGL TLHLKFLEPF - 240
DIDDHQQVHC PYDQLQIYAN GKNIGEFCGK QRPPDLDTSS NAVDLLFFTD ESGDSRGWKL - 300
RYTTEIIKCP QPKTLDEFTI IQNLQPQYQF RDYFIATCKQ GYQLIEGNQV LHSFTAVCQD - 360
DGTWHRAMPR CKIKDCGQPR NLPNGDFRYT TTMGVNTYKA RIQYYCHEPY YKMQTRAGSR - 420
ESEQGVYTCT AQGIWKNEQK GEKIPRCLPV CGKPVNPVEQ RQRIIGGQKA KMGNFPWQVF - 480
TNIHGRGGGA LLGDRWILTA AHTLYPKEHE AQSNASLDVF LGHTNVEELM KLGNHPIRRV - 540
SVHPDYRQDE SYNFEGDIAL LELENSVTLG PNLLPICLPD NDTFYDLGLM GYVSGFGVME - 600
EKIAHDLRFV RLPVANPQAC ENWLRGKNRM DVFSQNMFCA GHPSLKQDAC QGDSGGVFAV - 660
RDPNTDRWVA TGIVSWGIGC SRGYGFYTKV LNYVDWIKKE MEEED
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| Functional narrative |
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.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | CUB2 domain | | Location: | 193 - 305 | | Length: | 113 | | Region sequence: |
CSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPY
DQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTE | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Substrate/ligand binding
| Detection methods:
- Hydrogen-deuterium exchange (573 K; pH: 3.5; ammonium formiate in D2O 10 mM; capillary voltage 4000 V; flow rate 0.2 mL/min; flow rate (drying nitrogen gas) 10 L/min)
- Circular dichroism (CD) spectroscopy, far-UV (bandwidth 1 nm; protein (sample) 0.1 mg/mL; quartz cells 1 mm; scanning speed 10 nm/min)
| References:
- Major B, Kardos J, Kékesi KA, Lorincz Z, Závodszky P, Gál P. "Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r." J Biol Chem. 2010; 285(16): 11863-11869. PubMed: 20178990
| Comments:
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