Q7LZ61 · VM3CX_DABSI
- ProteinCoagulation factor X-activating enzyme heavy chain
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids619 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.
Catalytic activity
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 333 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 334 | |||||
Sequence: E | ||||||
Binding site | 337 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 343 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 403 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 406 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 408 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 410 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 413 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 416 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 467 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 468 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 470 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 482 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 483 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | toxin activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCoagulation factor X-activating enzyme heavy chain
- EC number
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Viperinae > Daboia
Accessions
- Primary accessionQ7LZ61
- Secondary accessions
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MMQVLLVTISLAVFPYQGSS | ||||||
Propeptide | PRO_0000355226 | 21-188 | ||||
Sequence: IILESGNVNDYEVVYPQKVTALPKGAVQQPEQKYEDTMQYEFEVNGEPVVLHLEKNKILFSEDYSETHYYPDGREITTNPPVEDHCYYHGRIQNDAHSSASISACNGLKGHFKLRGEMYFIEPLKLSNSEAHAVYKYENIEKEDEIPKMCGVTQTNWESDKPIKKASQ | ||||||
Chain | PRO_0000078204 | 189-619 | Coagulation factor X-activating enzyme heavy chain | |||
Sequence: LVSTSAQFNKIFIELVIIVDHSMAKKCNSTATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDLMTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVEIVQEQGNRNFKTAVIMAHELSHNLGMYHDGKNCICNDSSCVMSPVLSDQPSKLFSNCSIHDYQRYLTRYKPKCIFNPPLRKDIVSPPVCGNEIWEEGEECDCGSPANCQNPCCDAATCKLKPGAECGNGLCCYQCKIKTAGTVCRRARDECDVPEHCTGQSAECPRDQLQQNGKPCQNNRGYCYNGDCPIMRNQCISLFGSRANVAKDSCFQENLKGSYYGYCRKENGRKIPCAPQDVKCGRLFCLNNSPRNKNPCNMHYSCMDQHKGMVDPGTKCEDGKVCNNKRQCVDVNTAYQSTTGFSQI | ||||||
Disulfide bond | 215↔251 | |||||
Sequence: CNSTATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWC | ||||||
Glycosylation | 216 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 257 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 308↔388 | |||||
Sequence: CQAYRSVEIVQEQGNRNFKTAVIMAHELSHNLGMYHDGKNCICNDSSCVMSPVLSDQPSKLFSNCSIHDYQRYLTRYKPKC | ||||||
Disulfide bond | 348↔372 | |||||
Sequence: CICNDSSCVMSPVLSDQPSKLFSNC | ||||||
Disulfide bond | 350↔355 | |||||
Sequence: CNDSSC | ||||||
Glycosylation | 351 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 371 | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 404↔433 | |||||
Sequence: CGNEIWEEGEECDCGSPANCQNPCCDAATC | ||||||
Disulfide bond | 415↔428 | |||||
Sequence: CDCGSPANCQNPCC | ||||||
Disulfide bond | 417↔423 | |||||
Sequence: CGSPANC | ||||||
Disulfide bond | 427↔450 | |||||
Sequence: CCDAATCKLKPGAECGNGLCCYQC | ||||||
Disulfide bond | 441↔447 | |||||
Sequence: CGNGLCC | ||||||
Disulfide bond | 446↔472 | |||||
Sequence: CCYQCKIKTAGTVCRRARDECDVPEHC | ||||||
Disulfide bond | 459↔479 | |||||
Sequence: CRRARDECDVPEHCTGQSAEC | ||||||
Disulfide bond | 466↔498 | |||||
Sequence: CDVPEHCTGQSAECPRDQLQQNGKPCQNNRGYC | ||||||
Disulfide bond | 491↔503 | |||||
Sequence: CQNNRGYCYNGDC | ||||||
Disulfide bond | 510↔560 | |||||
Sequence: CISLFGSRANVAKDSCFQENLKGSYYGYCRKENGRKIPCAPQDVKCGRLFC | ||||||
Disulfide bond | 525↔571 | |||||
Sequence: CFQENLKGSYYGYCRKENGRKIPCAPQDVKCGRLFCLNNSPRNKNPC | ||||||
Disulfide bond | 538↔548 | |||||
Sequence: CRKENGRKIPC | ||||||
Disulfide bond | 555↔597 | |||||
Sequence: CGRLFCLNNSPRNKNPCNMHYSCMDQHKGMVDPGTKCEDGKVC | ||||||
Disulfide bond | 577 | Interchain (with C-158 in coagulation factor X-activating enzyme light chain LC2) | ||||
Sequence: C | ||||||
Disulfide bond | 591↔603 | |||||
Sequence: CEDGKVCNNKRQC |
Post-translational modification
N-glycosylated; probably required for conformation. Removal of easily accessible sugars does not change its functional capacity, but removal of the core sugars with N-glycanase causes a virtually complete loss of enzyme activity, apparently as a result of major conformational changes in the molecule. Not O-glycosylated.
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Heterotrimer; disulfide-linked. The heterotrimer consists of 1 heavy chain and 2 light chains (lectins): LC1 and LC2.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 199-393 | Peptidase M12B | ||||
Sequence: IFIELVIIVDHSMAKKCNSTATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDLMTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVEIVQEQGNRNFKTAVIMAHELSHNLGMYHDGKNCICNDSSCVMSPVLSDQPSKLFSNCSIHDYQRYLTRYKPKCIFNPP | ||||||
Domain | 401-487 | Disintegrin | ||||
Sequence: PPVCGNEIWEEGEECDCGSPANCQNPCCDAATCKLKPGAECGNGLCCYQCKIKTAGTVCRRARDECDVPEHCTGQSAECPRDQLQQN | ||||||
Motif | 465-467 | D/ECD-tripeptide | ||||
Sequence: ECD |
Sequence similarities
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length619
- Mass (Da)69,648
- Last updated2008-11-25 v2
- Checksum71084A3B46338797
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 191 | in Ref. 3; AA sequence | ||||
Sequence: S → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ137799 EMBL· GenBank· DDBJ | AAZ39881.1 EMBL· GenBank· DDBJ | mRNA |