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Reviewed, UniProtKB/Swiss-Prot Q5R544 (C1R_PONAB)

Last modified June 16, 2009. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Complement C1r subcomponent
    EC=3.4.21.41
Alternative name(s):
    Complement component 1, r subcomponent
Cleaved into the following 2 chains:
    1- Recommended name:
            Complement C1r subcomponent heavy chain
    2- Recommended name:
            Complement C1r subcomponent light chain
Gene names
Name: C1R
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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Protein attributes

Sequence length705 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

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 By similarity.

Catalytic activity

Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form the active form of C1s (EC 3.4.21.42).

Subunit structure

C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. C1r is a dimer of identical chains, each of which is activated by cleavage into two chains, A and B, connected by disulfide bonds By similarity.

Post-translational modification

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains By similarity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 CUB domains.

Contains 1 EGF-like domain.

Contains 1 peptidase S1 domain.

Contains 2 Sushi (CCP/SCR) domains.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 705688Complement C1r subcomponent
PRO_0000042190
Chain18 – 463446Complement C1r subcomponent heavy chain By similarity
PRO_0000042191
Chain464 – 705242Complement C1r subcomponent light chain By similarity
PRO_0000042192

Regions

Domain18 – 141124CUB 1
Domain142 – 19049EGF-like; calcium-binding Potential
Domain193 – 305113CUB 2
Domain307 – 37367Sushi 1
Domain374 – 44976Sushi 2
Domain464 – 702239Peptidase S1

Sites

Active site5021Charge relay system By similarity
Active site5571Charge relay system By similarity
Active site6541Charge relay system By similarity

Amino acid modifications

Modified residue1671(3R)-3-hydroxyasparagine By similarity
Modified residue2061Phosphoserine; by CK2 By similarity
Glycosylation1251N-linked (GlcNAc...) Potential
Glycosylation2211N-linked (GlcNAc...) Potential
Glycosylation5141N-linked (GlcNAc...) Potential
Glycosylation5811N-linked (GlcNAc...) Potential
Disulfide bond71 ↔ 89 By similarity
Disulfide bond146 ↔ 165 By similarity
Disulfide bond161 ↔ 174 By similarity
Disulfide bond176 ↔ 189 By similarity
Disulfide bond193 ↔ 220 By similarity
Disulfide bond250 ↔ 268 By similarity
Disulfide bond309 ↔ 358 By similarity
Disulfide bond338 ↔ 371 By similarity
Disulfide bond376 ↔ 429 By similarity
Disulfide bond406 ↔ 447 By similarity
Disulfide bond451 ↔ 577Interchain (between heavy and light chains) By similarity
Disulfide bond620 ↔ 639 By similarity
Disulfide bond650 ↔ 680 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5R544-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 4DFA4080BB75174B

FASTA70580,064
        10         20         30         40         50         60 
MWLLYLLVPA MFCRAGGSIP IPQKLFGEVT SPLFPKPYPN NFETTTVITV PTGYRVKLVF 

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

       130        140        150        160        170        180 
SNEENGTIMF YKGFLAYYQA VDLDECASQS KSGEEDPQPQ CQHLCHNYVG GYFCSCLPGY 

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

       250        260        270        280        290        300 
EIDDHQQVHC PYDQLQIYAN GKNIGEFCGK QRPPDLDTSS NAVDLLFFTD ESGDSRGWNL 

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

       370        380        390        400        410        420 
DGTWHRAMPR CKIKDCGQPR NLPNGAFRYT TTMGVNTYKA RIQYYCHKPY YKMQTRAGSR 

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

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

       550        560        570        580        590        600 
SVHPDYRQDE SHNFEGDIAL LELENSVTLG PNLLPICLPD NETFYDLGLM GYVSGFGVME 

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

       670        680        690        700 
RDPNTDRWVA TGIVSWGIGC SRGYGFYTKV LNYVDWIKKE MEEED

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.

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Cross-references

Sequence databases

CR861030 mRNA. Translation: CAH93122.1.
RefSeqNP_001126847.1.
UniGenePab.18568

3D structure databases

SMRQ5R544. Positions 307-702, 375-703.
ModBaseSearch...

Genome annotation databases

GeneID100173855.

Phylogenomic databases

HOVERGENQ5R544.

Enzyme and pathway databases

BRENDA3.4.21.41. 269192.

Family and domain databases

InterProIPR016060. Complement_control_module.
IPR000859. CUB.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR001881. EGF_Ca_bd.
IPR013091. EGF_Ca_bd_2.
IPR018097. EGF_Ca_bd_CS.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
Gene3DG3DSA:2.10.70.10. Complement_control_module. 1 hit.
G3DSA:2.60.120.290. CUB. 2 hits.
PfamPF00431. CUB. 2 hits.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. False negative.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. False negative.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameC1R_PONAB
AccessionPrimary (citable) accession number: Q5R544
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: December 21, 2004
Last modified: June 16, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents