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P47797 (VSPF2_CALRH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine protease ancrod-2

EC=3.4.21.74
Alternative name(s):
Venombin A
OrganismCalloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Taxonomic identifier8717 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeCalloselasma

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Thrombin-like snake venom serine protease. Cleaves fibrinopeptides AM, AO, and AY; the aberrant fibrinogen is then incapable of being cross-linked, forming easily dispersible clots.

Catalytic activity

Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the peptidase S1 family. Snake venom subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
Toxin
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

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

Signal peptide1 – 1818 By similarity
Propeptide19 – 246 By similarity
PRO_0000028377
Chain25 – 258234Serine protease ancrod-2
PRO_0000028378

Regions

Domain25 – 251227Peptidase S1

Sites

Active site671Charge relay system By similarity
Active site1121Charge relay system By similarity
Active site2061Charge relay system By similarity

Amino acid modifications

Glycosylation1231N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 165 By similarity
Disulfide bond52 ↔ 68 By similarity
Disulfide bond102 ↔ 256 By similarity
Disulfide bond144 ↔ 212 By similarity
Disulfide bond176 ↔ 191 By similarity
Disulfide bond202 ↔ 227 By similarity

Sequences

Sequence LengthMass (Da)Tools
P47797 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9181C7D1F2D689F4

FASTA25829,145
        10         20         30         40         50         60 
MVLIRVLANL VILQLSYAQK SSELVIGGDE CNINEHRFLV ALYDSTTRNF LCGGVLIHPE 

        70         80         90        100        110        120 
WVITAKHCNK KSMVLYLGKH KQSVKFDDEQ ERFPKEKHFI RCNKPRTRWG EDIMLIRLNK 

       130        140        150        160        170        180 
PVNNSEHIAP LSLPSNPPIV GSVCRVMGWG SINKYIDVLP DEPRCANINL YNYTVCRGVF 

       190        200        210        220        230        240 
PRIPKKSKIL CAGDLQGRLD SCHCDSGGPL ICSEEFHGIV YRGPNPCAQP DKPALYTNIF 

       250 
DHLHWILSIM AGNATCYP 

« Hide

References

[1]"Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from the venom of Calloselasma rhodostoma."
Au L.-C., Lin S.-B., Chou J.-S., Teh G.-W., Chang K.-J., Shih C.-M.
Biochem. J. 294:387-390(1993) [PubMed: 8373353] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07308 mRNA. Translation: AAA49195.1.
PIRS36783.

3D structure databases

ProteinModelPortalP47797.
SMRP47797. Positions 25-255.
ModBaseSearch...

Protein family/group databases

MEROPSS01.178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013304.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVSPF2_CALRH
AccessionPrimary (citable) accession number: P47797
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families