Complement C1s subcomponent precursor - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q6P6T1 (C1S_RAT)

Last modified January 19, 2010. Version 52. 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

Hide | Top

Names and origin

Protein names

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

Gene names

Name:	C1s
Synonyms:	r-gsp

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Hide | Top

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.

Hide | Top

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.
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.
Caution	Ref.2 (AAH27183) sequence was reported to derive from mouse origin.

Hide | Top

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 glial cell differentiation Ref.1 Inferred from expression pattern. Source: RGD innate immune response Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro response to cAMP Inferred from expression pattern. Source: RGD
Cellular component	extracellular region Inferred from direct assay. Source: RGD
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

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 subcomponent

PRO_0000042202

Chain

16 – 437

422

Complement C1s subcomponent heavy chain By similarity

PRO_0000042203

Chain

438 – 688

251

Complement C1s subcomponent light chain By similarity

PRO_0000042204

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

Glycosylation

406

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

Experimental info

Sequence conflict

T → S in BAA25797. Ref.1

Sequence conflict

T → I in AAH27183. Ref.2

Sequence conflict

554

S → F in BAA25797. Ref.1

Sequence conflict

562

G → V in BAA25797. Ref.1

Sequence conflict

575

N → I in BAA25797. Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q6P6T1-1 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: B69C43027AE7A85F
Show »

FASTA

688

77,071

        10         20         30         40         50         60 
MWCFVFFSLL ASFSAEPTMY GEILSPNYPQ AYPNEVVKTW DIEVPEGFGI HLYFTHLDME 

        70         80         90        100        110        120 
LSENCAYDSV QIISGGIEEE RLCGQRTSKS PNSPTVEEFQ FPYNRLQVVF TSDFSNEERF 

       130        140        150        160        170        180 
TGFAAYYSAV DVNECTDFTD VPCSHFCNNF IGGYFCSCPP EYFLHDDMRT CGVNCSGDVF 

       190        200        210        220        230        240 
TALIGEIASP NYPNPYPENS RCEYQIRLQE GFRLVLTIRR EDFDVEPADS EGNCHDSLTF 

       250        260        270        280        290        300 
AAKNQQFGPY CGNGFPGPLT IKTQSNTLDI VFQTDLTGQN KGWKLRYHGD PIPCPKEISA 

       310        320        330        340        350        360 
NSIWEPEKAK YVFKDVVKIT CVDGFEVVEG NVGSTSFYST CQSNGQWSNS RLECQPVDCG 

       370        380        390        400        410        420 
VPEPIENGKV EDPEDTVFGS VIHYTCEEPY YYMEQEEGGE YHCAANGSWV NDQLGVELPK 

       430        440        450        460        470        480 
CIPVCGVPTE PFKVQQRIFG GYSTKIQSFP WQVYFESPRG GGALIDEYWV LTAAHVVEGN 

       490        500        510        520        530        540 
SDPVMYVGST LLKIERLRNA QRLITERVII HPSWKQEDDL NTRTNFDNDI ALVQLKDPVK 

       550        560        570        580        590        600 
MGPTVAPICL PETSSDYNPS EGDLGLISGW GRTENRTNVI QLRGAKLPIT SLEKCQQVKV 

       610        620        630        640        650        660 
ENPKARSNDY VFTDNMICAG EKGVDSCEGD SGGAFALPVP NVKDPKFYVA GLVSWGKKCG 

       670        680 
TYGIYTKVKN YVDWILKTMQ ENSGPKKD

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a cDNA encoding a serine protease homologous to complement Cls precursor from rat C6 glial cells and its expression during glial differentiation." Sakai H., Nakashima S., Yoshimura S., Nishimura Y., Sakai N., Nozawa Y. Gene 209:87-94(1998) [PubMed: 9524231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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]. Tissue: Prostate.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
EMBL GenBank DDBJ	D88250 mRNA. Translation: BAA25797.1. Different initiation. BC027183 mRNA. Translation: AAH27183.1. Different initiation. BC062042 mRNA. Translation: AAH62042.1. Different initiation.
IPI	IPI00199519.
PIR	JC6554.
RefSeq	NP_620255.1.
UniGene	Rn.4037
3D structure databases
SMR	Q6P6T1. Positions 18-288, 175-290, 292-680.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6P6T1.
Protein family/group databases
MEROPS	S01.193.
PTM databases
PhosphoSite	Q6P6T1.
Genome annotation databases
Ensembl	ENSRNOT00000016330; ENSRNOP00000016330; ENSRNOG00000011971; Rattus norvegicus. [Genome view]
GeneID	192262.
KEGG	rno:192262.
UCSC	BC062042. rat.
Organism-specific databases
CTD	192262.
RGD	619983. C1s.
Phylogenomic databases
eggNOG	roNOG09194.
HOVERGEN	Q6P6T1.
InParanoid	Q6P6T1.
Enzyme and pathway databases
BRENDA	3.4.21.42. 248.
Gene expression databases
ArrayExpress	Q6P6T1.
Genevestigator	Q6P6T1.
GermOnline	ENSRNOG00000011971. Rattus norvegicus.
Family and domain databases
InterPro	IPR016060. Complement_control_module. IPR000859. CUB. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. 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. IPR009003. Ser/Cys_Pept_Trypsin-like. 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. PF07645. EGF_CA. 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	622938.

Hide | Top

Entry information

Entry name

C1S_RAT

Accession

Primary (citable) accession number: Q6P6T1
Secondary accession number(s): O70542, Q8R099

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	September 27, 2005
Last modified:	January 19, 2010
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

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)

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

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