Reviewed,
UniProtKB/Swiss-Prot Q0VCX1 (C1S_BOVIN)
Last modified
June 16, 2009.
Version 29.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 689 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
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. |
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 responseInferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: InterPro |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred 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 – 15 | 15 | Potential | ||||||||
| Chain | 16 – 689 | 674 | Complement C1s subcomponent | PRO_0000285867 | |||||||
| Chain | 16 – 437 | 422 | Complement C1s subcomponent heavy chain By similarity | PRO_0000285868 | |||||||
| Chain | 438 – 689 | 252 | Complement C1s subcomponent light chain By similarity | PRO_0000285869 | |||||||
Regions | |||||||||||
| Domain | 16 – 130 | 115 | CUB 1 | ||||||||
| Domain | 131 – 172 | 42 | EGF-like; calcium-binding Potential | ||||||||
| Domain | 175 – 290 | 116 | CUB 2 | ||||||||
| Domain | 292 – 356 | 65 | Sushi 1 | ||||||||
| Domain | 357 – 423 | 67 | Sushi 2 | ||||||||
| Domain | 438 – 681 | 244 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 475 | 1 | Charge relay system By similarity | ||||||||
| Active site | 529 | 1 | Charge relay system By similarity | ||||||||
| Active site | 632 | 1 | Charge relay system By similarity | ||||||||
| Metal binding | 60 | 1 | Calcium By similarity | ||||||||
| Metal binding | 68 | 1 | Calcium By similarity | ||||||||
| Metal binding | 113 | 1 | Calcium By similarity | ||||||||
| Metal binding | 131 | 1 | Calcium By similarity | ||||||||
| Metal binding | 132 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 134 | 1 | Calcium By similarity | ||||||||
| Metal binding | 149 | 1 | Calcium By similarity | ||||||||
| Metal binding | 150 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 153 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 149 | 1 | (3R)-3-hydroxyasparagine By similarity | ||||||||
| Glycosylation | 64 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 174 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 406 | 1 | 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 | 628 ↔ 660 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal skin. |
Cross-references
Sequence databases | |
|---|---|
| BC119956 mRNA. Translation: AAI19957.1. Different initiation. | |
| IPI | IPI00695404. |
| RefSeq | NP_001070018.1. |
| UniGene | Bt.1491 |
3D structure databases | |
| SMR | Q0VCX1. Positions 18-174, 357-684. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S01.193. |
Genome annotation databases | |
| Ensembl | ENSBTAG00000004840. Bos taurus. [Contig view] |
| GeneID | 767827. |
| KEGG | bta:767827. |
Phylogenomic databases | |
| HOVERGEN | Q0VCX1. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.42. 251. |
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... |
Entry information
| Entry name | C1S_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q0VCX1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


