Complement C1r-A subcomponent precursor

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Q8CG16 (C1RA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Complement C1r-A subcomponent
EC=3.4.21.41

Alternative name(s):
Complement component 1 subcomponent r-A

Cleaved into the following 2 chains:

Complement C1r-A subcomponent heavy chain
Complement C1r-A subcomponent light chain

Gene names

Name:	C1ra
Synonyms:	C1r

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	707 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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.
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.

Ontologies

Keywords
Biological process	Complement pathway Immunity Innate immunity
Domain	EGF-like domain Repeat Signal Sushi
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Hydroxylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

By similarity

Chain

17 – 707

691

Complement C1r-A subcomponent

PRO_0000027580

Chain

17 – 462

446

Complement C1r-A subcomponent heavy chain By similarity

PRO_0000027581

Chain

463 – 707

245

Complement C1r-A subcomponent light chain By similarity

PRO_0000027582

Regions

Domain

17 – 140

124

CUB 1

Domain

141 – 189

EGF-like; calcium-binding Potential

Domain

192 – 304

113

CUB 2

Domain

306 – 372

Sushi 1

Domain

373 – 448

Sushi 2

Domain

463 – 704

242

Peptidase S1

Sites

Active site

501

Charge relay system By similarity

Active site

559

Charge relay system By similarity

Active site

656

Charge relay system By similarity

Amino acid modifications

Modified residue

166

(3R)-3-hydroxyasparagine By similarity

Modified residue

205

Phosphoserine; by CK2 By similarity

Glycosylation

124

N-linked (GlcNAc...) Potential

Glycosylation

220

N-linked (GlcNAc...) Ref.4

Glycosylation

583

N-linked (GlcNAc...) Potential

Disulfide bond

70 ↔ 88

By similarity

Disulfide bond

145 ↔ 164

By similarity

Disulfide bond

160 ↔ 173

By similarity

Disulfide bond

175 ↔ 188

By similarity

Disulfide bond

192 ↔ 219

By similarity

Disulfide bond

249 ↔ 267

By similarity

Disulfide bond

308 ↔ 357

By similarity

Disulfide bond

337 ↔ 370

By similarity

Disulfide bond

375 ↔ 428

By similarity

Disulfide bond

405 ↔ 446

By similarity

Disulfide bond

450 ↔ 579

Interchain (between heavy and light chains) By similarity

Disulfide bond

622 ↔ 641

By similarity

Disulfide bond

652 ↔ 682

By similarity

Experimental info

Sequence conflict

101

S → R in AAG01898. Ref.1

Sequence conflict

359

N → H in AAH04637. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q8CG16 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 29DAAEB3C047D8E8
Show »

FASTA

707

80,073

        10         20         30         40         50         60 
MWLFALLVTL FYGVEGSIYL PQKLYGEVTS PLYPKPYPSD LETTTVITVP MGYRVKLVFW 

        70         80         90        100        110        120 
QFDVEPSEGC FYDYVKISAD KQTLGRFCGQ LDSPLGNPPG SKEFMSQGNK MLLTFHTDFS 

       130        140        150        160        170        180 
NEENGTIMFY KGFLAYYQAV DLDECASQPN SVEEGLQPRC QHLCHNYVGG YFCSCHPGYE 

       190        200        210        220        230        240 
LQKDGQSCQA ECSSELYTEP SGYVSSLEYP QPYPPDLRCN YSIRVERGLT VHLKFLDPFE 

       250        260        270        280        290        300 
IDDHQQVHCP YDQLQIYANG KNLGEFCGKQ RPPDLDTSSN AVDLLFFTDE SGDSRGWKLH 

       310        320        330        340        350        360 
YTTETIKCPQ PKALDEFTII QDPQPQYQFR DYFIVTCKQG YQLMEGNQAL LSFTAVCQND 

       370        380        390        400        410        420 
GTWHRAMPRC KIKNCGQPQS LSNGDFRYIT TKGVTTYEAS IQYHCHEPYY KMLTRAGSSE 

       430        440        450        460        470        480 
SMRGIYTCTA QGIWKNEEEG EKMPRCLPVC GKPVNPVTQK ERIIRGQPAR PGNFPWQAFT 

       490        500        510        520        530        540 
TTHGRGGGAL LGDRWILTAA HTIYPKHHNK ENDNANPKML VFLGHTNVEQ IKKLGHHPVR 

       550        560        570        580        590        600 
RVIIHPDYRQ DEPNNFEGDI ALLELENSVT LGPELLPICL PDNETFYGQG LMGYVSGFGI 

       610        620        630        640        650        660 
TEDKLAFDLR FVRLPVADSE ACQRWLQTKK DTSPFSQNMF CSGDPAVQQD ACQGDSGGVF 

       670        680        690        700 
AVRDRNRDIW VATGIVSWGI GCGEGYGFYT KVLNYVDWIK KEMGDEN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a cDNA encoding a serine protease homologous to human complement C1r precursor from an allografted mouse skin and its expression in Escherichia coli." Byun S.J., Hyun J.H., Hwang H.Y., Ryoo Z.Y., Kim T.Y. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6.
[2]	"Complement C1r and C1s genes are duplicated in the mouse: differential expression generates alternative isomorphs in the liver and in the male reproductive system." Garnier G., Circolo A., Xu Y., Volanakis J.E. Biochem. J. 371:631-640(2003) [PubMed: 12513694] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Strain: 129/SvJ.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides." Bernhard O.K., Kapp E.A., Simpson R.J. J. Proteome Res. 6:987-995(2007) [PubMed: 17330941] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-220, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF148216 mRNA. Translation: AAG01898.1. AF459011 , AF459008, AF459009, AF459010 Genomic DNA. Translation: AAO15553.1. BC004637 mRNA. Translation: AAH04637.1.
IPI	IPI00407502.
RefSeq	NP_075632.3. NM_023143.3.
UniGene	Mm.333375.
3D structure databases
ProteinModelPortal	Q8CG16.
SMR	Q8CG16. Positions 24-303, 306-703.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8CG16.
Protein family/group databases
MEROPS	S01.192.
PTM databases
PhosphoSite	Q8CG16.
Proteomic databases
PRIDE	Q8CG16.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000068593; ENSMUSP00000063707; ENSMUSG00000055172.
GeneID	50909.
KEGG	mmu:50909.
UCSC	uc009dra.2. mouse.
Organism-specific databases
CTD	50909.
MGI	MGI:1355313. C1ra.
Phylogenomic databases
HOGENOM	HBG505493.
HOVERGEN	HBG000559.
InParanoid	Q8CG16.
OMA	FTAVCQD.
Gene expression databases
ArrayExpress	Q8CG16.
Bgee	Q8CG16.
CleanEx	MM_C1R.
Genevestigator	Q8CG16.
GermOnline	ENSMUSG00000055172. Mus musculus.
Family and domain databases
InterPro	IPR016060. Complement_control_module. IPR000859. CUB. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR009003. Pept_cys/ser_Trypsin-like. IPR024175. Pept_S1A_C1r/C1S/mannan-bd. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. IPR000436. Sushi_SCR_CCP. [Graphical view]
Gene3D	G3DSA:2.10.70.10. Complement_control_module. 2 hits. G3DSA:2.60.120.290. CUB. 2 hits.
KO	K01330.
Pfam	PF00431. CUB. 2 hits. PF07645. EGF_CA. 1 hit. PF00084. Sushi. 2 hits. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00032. CCP. 2 hits. SM00042. CUB. 2 hits. SM00179. EGF_CA. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF57535. Complement_control_module. 2 hits. SSF49854. CUB. 2 hits. SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS00010. 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]
ProtoNet	Search...
Other
NextBio	307891.
SOURCE	Search...

Entry information

Entry name

C1RA_MOUSE

Accession

Primary (citable) accession number: Q8CG16
Secondary accession number(s): Q99KI6, Q9ET60

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	March 1, 2003
Last modified:	November 16, 2011
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents