Q27083 · CFGB_TACTR
- ProteinClotting factor G beta subunit
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids309 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the heterodimer clotting factor G which may play a role in defense mechanisms against fungi (Probable). Initiates a (1->3)-beta-glucan-sensing clotting pathway whereby the alpha subunit binds to glucans containing (1->3)-beta linkages, which are components of the fungal cell wall, and the beta subunit catalyzes the activation of proclotting enzyme (PubMed:7822328).
Catalytic activity
Activity regulation
Binding to (1->3)-beta-D-glucan to alpha subunit, induces autocatalysis and activation of beta subunit (PubMed:7822328).
Inhibited by intracellular coagulation inhibitor 3/LICI-3 and to a lesser extend by intracellular coagulation inhibitor 2/LICI-2 (PubMed:7822328, PubMed:8798603).
Inhibited by intracellular coagulation inhibitor 3/LICI-3 and to a lesser extend by intracellular coagulation inhibitor 2/LICI-2 (PubMed:7822328, PubMed:8798603).
Biotechnology
Clotting factor G is a component of the Limulus test used to detect bacterial endotoxins in fluids.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 89 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 138 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 242 | Charge relay system | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | serine-type peptidase activity | |
Biological Process | hemolymph coagulation | |
Biological Process | protein processing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameClotting factor G beta subunit
- EC number
- Cleaved into 2 chains
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Merostomata > Xiphosura > Limulidae > Tachypleus
Accessions
- Primary accessionQ27083
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-31 | |||||
Sequence: MDISFLVFITLSMALFSSNVTGTSVTSRVRR | ||||||
Chain | PRO_0000450356 | 32-46 | Clotting factor G beta subunit light chain | |||
Sequence: GINEKHCGFRPVITR | ||||||
Disulfide bond | 38↔158 | |||||
Sequence: CGFRPVITRIIGGGIATPHSWPWMVGIFKVNPHRFLCGGSIINKVSVVTAAHCLVTQFGNRQNYSIFVRVGAHDIDNSGTNYQVDKVIVHQGYKHHSHYYDIGLILLSKPVEYNDKIQPVC | ||||||
Chain | PRO_5004203470 | 47-309 | Clotting factor G beta subunit heavy chain | |||
Sequence: IIGGGIATPHSWPWMVGIFKVNPHRFLCGGSIINKVSVVTAAHCLVTQFGNRQNYSIFVRVGAHDIDNSGTNYQVDKVIVHQGYKHHSHYYDIGLILLSKPVEYNDKIQPVCIPEFNKPHVNLNNIKVVITGWGVTGKATEKRNVLRELELPVVTNEQCNKSYQTLPFSKLNRGITNDMICAGFPEGGKDACQGDSGGPLMYQNPTTGRVKIVGVVSFGFECARPNFPGVYTRLSSYVNWLQEITFGQSLASLFEVVPIFIPE | ||||||
Disulfide bond | 74↔90 | |||||
Sequence: CGGSIINKVSVVTAAHC | ||||||
Glycosylation | 100 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 205↔227 | |||||
Sequence: CNKSYQTLPFSKLNRGITNDMIC | ||||||
Glycosylation | 206 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 238↔268 | |||||
Sequence: CQGDSGGPLMYQNPTTGRVKIVGVVSFGFEC |
Keywords
- PTM
Expression
Tissue specificity
Expressed in the hemocytes (at protein level).
Interaction
Subunit
Clotting factor G is a heterodimer composed of two non-covalently associated subunits, alpha and beta (PubMed:7822328).
Upon activation, converted to a two-chain active form linked by a disulfide bond (PubMed:7822328).
Forms a covalent heterodimer with intracellular coagulation inhibitor 3/LICI-3 (PubMed:8798603).
Upon activation, converted to a two-chain active form linked by a disulfide bond (PubMed:7822328).
Forms a covalent heterodimer with intracellular coagulation inhibitor 3/LICI-3 (PubMed:8798603).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 47-292 | Peptidase S1 | ||||
Sequence: IIGGGIATPHSWPWMVGIFKVNPHRFLCGGSIINKVSVVTAAHCLVTQFGNRQNYSIFVRVGAHDIDNSGTNYQVDKVIVHQGYKHHSHYYDIGLILLSKPVEYNDKIQPVCIPEFNKPHVNLNNIKVVITGWGVTGKATEKRNVLRELELPVVTNEQCNKSYQTLPFSKLNRGITNDMICAGFPEGGKDACQGDSGGPLMYQNPTTGRVKIVGVVSFGFECARPNFPGVYTRLSSYVNWLQEITF |
Sequence similarities
Belongs to the peptidase S1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length309
- Mass (Da)34,265
- Last updated1996-11-01 v1
- Checksum014F0B5F2BD56FDB
Keywords
- Technical term