Complement C1s-B subcomponent precursor

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Reviewed, UniProtKB/Swiss-Prot Q8CFG8 (CS1B_MOUSE)

Last modified June 16, 2009. Version 47. History...

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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 names

Recommended name:
    Complement C1s-B subcomponent
    EC=3.4.21.42
Alternative name(s):
    C1 esterase
Cleaved into the following 2 chains:
    1- Recommended name:
            Complement C1s-B subcomponent heavy chain
    2- Recommended name:
            Complement C1s-B subcomponent light chain

Gene names

Name:	C1sb
Synonyms:	C1s

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

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Protein attributes

Sequence length	688 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

Function	C1s 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. C1r activates C1s so that it can, in turn, activate C2 and C4 By similarity.
Catalytic activity	Cleavage of Arg-\|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-\|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase.
Enzyme regulation	Inhibited by SERPING1 By similarity.
Subunit structure	C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. Activated C1s is an disulfide-linked heterodimer of a heavy chain and a light chain By similarity.
Tissue specificity	Specifically expressed in male reproductive tissues. Ref.1
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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Ontologies

Keywords
Biological process	Complement pathway Immune response Innate immunity
Domain	EGF-like domain Repeat Signal Sushi
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Hydroxylation
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: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

By similarity

Chain

16 – 688

673

Complement C1s-B subcomponent

PRO_0000042196

Chain

16 – 437

422

Complement C1s-B subcomponent heavy chain By similarity

PRO_0000042197

Chain

438 – 688

251

Complement C1s-B subcomponent light chain By similarity

PRO_0000042198

Regions

Domain

16 – 130

115

CUB 1

Domain

131 – 172

EGF-like; calcium-binding Potential

Domain

175 – 290

116

CUB 2

Domain

292 – 356

Sushi 1

Domain

357 – 423

Sushi 2

Domain

438 – 680

243

Peptidase S1

Sites

Active site

475

Charge relay system By similarity

Active site

529

Charge relay system By similarity

Active site

631

Charge relay system By similarity

Metal binding

Calcium By similarity

Metal binding

Calcium By similarity

Metal binding

113

Calcium By similarity

Metal binding

131

Calcium By similarity

Metal binding

132

Calcium; via carbonyl oxygen By similarity

Metal binding

134

Calcium By similarity

Metal binding

149

Calcium By similarity

Metal binding

150

Calcium; via carbonyl oxygen By similarity

Metal binding

153

Calcium; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue

149

(3R)-3-hydroxyasparagine By similarity

Glycosylation

174

N-linked (GlcNAc...) Potential

Disulfide bond

65 ↔ 83

By similarity

Disulfide bond

135 ↔ 147

By similarity

Disulfide bond

143 ↔ 156

By similarity

Disulfide bond

158 ↔ 171

By similarity

Disulfide bond

175 ↔ 202

By similarity

Disulfide bond

234 ↔ 251

By similarity

Disulfide bond

294 ↔ 341

By similarity

Disulfide bond

321 ↔ 354

By similarity

Disulfide bond

359 ↔ 403

By similarity

Disulfide bond

386 ↔ 421

By similarity

Disulfide bond

425 ↔ 549

Interchain (between heavy and light chains) By similarity

Disulfide bond

595 ↔ 618

By similarity

Disulfide bond

627 ↔ 659

By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q8CFG8-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F10A1DC565875A73
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FASTA

688

76,700

        10         20         30         40         50         60 
MWYLVLFSLL ASFSAEPTMH GEILSPNYPQ AYPNDVVKSW DIEVPEGFGI HLYFTHVDIE 

        70         80         90        100        110        120 
PSESCAYDSV QIISGGIEEG RLCGQRTSKS PNSPIIEEFQ FPYNKLQVVF TSDFSIEEQF 

       130        140        150        160        170        180 
TGFAAYYTAI DVNECTDFTD VPCSHFCNNF IGGYFCSCPP EYFLHDDMRN CGVNCSGDVF 

       190        200        210        220        230        240 
TALIGEISSP NYPNPYPENS RCEYQIQLQE GFQVVVTMQR EDFDVEPADS EGNCPDSLTF 

       250        260        270        280        290        300 
AAKNQQFGPY CGDGFPGPLT IRTQSNTLGI VFQTDLMGQK KGWKLRYHGD PISCPKESTA 

       310        320        330        340        350        360 
NSNWEPDKAK YVFKDVVKIT CVDGFEVVEG HVSSTSYYST CQSDGQWSNS GLKCQPVYCG 

       370        380        390        400        410        420 
IPDPIANGKV EEPENSVFGT VIHYTCEEPY YYMEHEEGGE YRCAANGRWV NDQLGIELPR 

       430        440        450        460        470        480 
CIPVCGVPTE PFQVQQKIFG GQPAKIENFP WQVFFNHPTA GGALINEYWV LTAAHVVEKN 

       490        500        510        520        530        540 
SDPSMYAGIT ALRLADLENA QRLYTKRVII HPGWKEDDDL NPRTNFDNDI ALVQLKDPVK 

       550        560        570        580        590        600 
MGPKFSPICL PGTSSEYNLS PGDMGLISGW GRTEKRLHVI NLRGAKVPVT SLETCKQVKE 

       610        620        630        640        650        660 
ENPTARPEDY VITDNMICAG EKGVDSCKGD SGGAFAFQVP NVKAPKFYVA GLVSWGKKCG 

       670        680 
AYGVYTKVKN YVDWILKTMQ ENSGPRKD

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References

[1]

"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 [MRNA], TISSUE SPECIFICITY.
Strain: C57BL/6.

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Cross-references

Sequence databases
	AF459020 mRNA. Translation: AAO15559.1.
IPI	IPI00474340.
RefSeq	NP_776289.1.
UniGene	Mm.476267
3D structure databases
HSSP	HSSP built from PDB template 1NZI based on UniProtKB Q9UCV4.
SMR	Q8CFG8. Positions 18-174, 359-683.
ModBase	Search...
Protein family/group databases
MEROPS	S01.210.
PTM databases
PhosphoSite	Q8CFG8.
Genome annotation databases
Ensembl	ENSMUSG00000079343. Mus musculus. [Contig view]
GeneID	317677.
KEGG	mmu:317677.
Organism-specific databases
MGI	MGI:3644269. EG317677.
Phylogenomic databases
HOVERGEN	Q8CFG8.
Enzyme and pathway databases
BRENDA	3.4.21.42. 244.
Gene expression databases
ArrayExpress	Q8CFG8.
CleanEx	MM_C1S.
GermOnline	ENSMUSG00000038521. Mus musculus.
Family and domain databases
InterPro	IPR016060. Complement_control_module. IPR000859. CUB. IPR006209. EGF. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_CS. IPR001881. EGF_Ca_bd. IPR018097. EGF_Ca_bd_CS. 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. 1 hit. G3DSA:2.60.120.290. CUB. 2 hits.
Pfam	PF00431. CUB. 2 hits. PF00008. EGF. 1 hit. PF00084. Sushi. 2 hits. PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00032. CCP. 2 hits. SM00042. CUB. 2 hits. SM00179. EGF_CA. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS00010. ASX_HYDROXYL. 1 hit. PS01180. CUB. 2 hits. PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. 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 Resources
NextBio	394148.
SOURCE	Search...

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Entry information

Entry name

CS1B_MOUSE

Accession

Primary (citable) accession number: Q8CFG8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

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)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents