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P09872 (VSPCA_AGKCO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine protease protac
EC=3.4.21.-
Alternative name(s):
ACC-C
Protein C activator
OrganismAgkistrodon contortrix contortrix (Southern copperhead)
Taxonomic identifier8713 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Agkistrodon

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Anticoagulant serine protease that acts by quickly activating protein C (PC). This activation is thrombomodulin-independent. Ref.2

Subunit structure

Monomer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Biotechnological use

Is used in diagnostic practice for the determination of disorders in the PC pathway. Functional assays are either clotting assays or based on determinations using chromogenic assays. Sold under the name Protac by Pentapharm. Ref.4

Sequence similarities

Belongs to the peptidase S1 family. Snake venom subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processBlood coagulation
   Cellular componentSecreted
   Molecular functionHydrolase
Protease
Serine protease
Toxin
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 231231Serine protease protac
PRO_0000088726

Regions

Domain1 – 222222Peptidase S1

Sites

Active site401Charge relay system Ref.3
Active site851Charge relay system Ref.3
Active site1771Charge relay system Ref.3

Amino acid modifications

Glycosylation211N-linked (GlcNAc...) Ref.1 Ref.3
Glycosylation781N-linked (GlcNAc...) Ref.1 Ref.3
Glycosylation1291N-linked (GlcNAc...) Ref.1 Ref.3
Disulfide bond7 ↔ 138 Ref.3
Disulfide bond25 ↔ 41 Ref.3
Disulfide bond73 ↔ 229 Ref.3
Disulfide bond117 ↔ 183 Ref.3
Disulfide bond149 ↔ 162 Ref.3
Disulfide bond173 ↔ 198 Ref.3

Secondary structure

1 ...................................... 231
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09872 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: DC3D7CBE601EC52B

FASTA23125,106
        10         20         30         40         50         60 
VIGGDECNIN EHRFLALVYA NGSLCGGTLI NQEWVLTARH CDRGNMRIYL GMHNLKVLNK 

        70         80         90        100        110        120 
DALRRFPKEK YFCLNTRNDT IWDKDIMLIR LNRPVRNSAH IAPLSLPSNP PSVGSVCRIM 

       130        140        150        160        170        180 
GWGTITSPNA TLPDVPHCAN INILDYAVCQ AAYKGLAATT LCAGILEGGK DTCKGDSGGP 

       190        200        210        220        230 
LICNGQFQGI LSVGGNPCAQ PRKPGIYTKV FDYTDWIQSI ISGNTDATCP P

« Hide

References

[1]"Primary structure of a protein C activator from Agkistrodon contortrix contortrix venom."
McMullen B.A., Fujikawa K., Kisiel W.
Biochemistry 28:674-679(1989) [PubMed: 2653426] [Abstract]
Cited for: PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-21; ASN-78 AND ASN-129.
Tissue: Venom.
[2]"Characterization of a protein C activator from Agkistrodon contortrix contortrix venom."
Kisiel W., Kondo S., Smith K.J., McMullen B.A., Smith L.F.
J. Biol. Chem. 262:12607-12613(1987) [PubMed: 3624272] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-63, FUNCTION.
Tissue: Venom.
[3]"Thrombomodulin-independent activation of protein C and specificity of hemostatically active snake venom serine proteinases: crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator."
Murakami M.T., Arni R.K.
J. Biol. Chem. 280:39309-39315(2005) [PubMed: 16162508] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), ACTIVE SITE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-21; ASN-78 AND ASN-129.
[4]"Protein C activators from snake venoms and their diagnostic use."
Gempeler-Messina P.M., Volz K., Buhler B., Muller C.
Haemostasis 31:266-272(2001) [PubMed: 11910194] [Abstract]
Cited for: BIOTECHNOLOGY.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA60468.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AIPX-ray1.65A1-231[»]
2AIQX-ray1.54A1-231[»]
ProteinModelPortalP09872.
SMRP09872. Positions 1-231.
ModBaseSearch...

Protein family/group databases

MEROPSS01.466.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013304.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. False negative.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVSPCA_AGKCO
AccessionPrimary (citable) accession number: P09872
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1994
Last modified: November 16, 2011
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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