Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P83370 (FA10V_HOPST)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Hopsarin-D
    EC=3.4.21.6
Cleaved into the following 2 chains:
    1- Recommended name:
            Hopsarin-D light chain
    2- Recommended name:
            Hopsarin-D heavy chain
OrganismHoplocephalus stephensii (Stephens' banded snake)
Taxonomic identifier196418 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Notechinae › Hoplocephalus

Hide | Top

Protein attributes

Sequence length376 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Act as a toxin in venom by activating thrombin. It is a procoagulant protein functionally similar to blood coagulation factor Xa. Ref.1

Catalytic activity

Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. Ref.1

Subunit structure

The two chains are formed from a single-chain precursor and are held together by a disulfide bond. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium By similarity. UniProtKB P00742

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 EGF-like domains.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Contains 1 peptidase S1 domain.

Hide | Top

Ontologies

Keywords
   Biological processBlood coagulation
   Cellular componentSecreted
   DomainEGF-like domain
Repeat
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
Toxin
   PTMDisulfide bond
Gamma-carboxyglutamic acid
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processblood coagulation

Non-traceable author statement. Source: UniProtKB

pathogenesis

Non-traceable author statement. Source: UniProtKB

proteolysis

Non-traceable author statement. Source: UniProtKB

   Cellular componentextracellular region

Non-traceable author statement. Source: UniProtKB

   Molecular functioncalcium ion binding

Non-traceable author statement. Source: UniProtKB

serine-type endopeptidase activity

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 141141Hopsarin-D light chain
PRO_0000027816
Chain142 – 376235Hopsarin-D heavy chain
PRO_0000027817

Regions

Domain1 – 4646Gla
Domain50 – 8132EGF-like 1; calcium-binding Potential UniProtKB P00742
Domain89 – 12436EGF-like 2
Domain142 – 374233Peptidase S1

Sites

Active site1831Charge relay system By similarity UniProtKB P00742
Active site2291Charge relay system By similarity UniProtKB P00742
Active site3261Charge relay system By similarity UniProtKB P00742
Site631Not modified

Amino acid modifications

Modified residue614-carboxyglutamate
Modified residue714-carboxyglutamate
Modified residue1414-carboxyglutamate
Modified residue1614-carboxyglutamate
Modified residue1914-carboxyglutamate
Modified residue2014-carboxyglutamate
Modified residue2514-carboxyglutamate
Modified residue2614-carboxyglutamate
Modified residue2914-carboxyglutamate
Modified residue3214-carboxyglutamate
Modified residue3514-carboxyglutamate
Glycosylation521O-linked (Hex...) Probable
Glycosylation1861N-linked (GlcNAc...) Probable
Disulfide bond17 ↔ 22 By similarity UniProtKB P00742
Disulfide bond50 ↔ 61 By similarity UniProtKB P00742
Disulfide bond55 ↔ 70 By similarity UniProtKB P00742
Disulfide bond72 ↔ 81 By similarity UniProtKB P00742
Disulfide bond89 ↔ 100 By similarity UniProtKB P00742
Disulfide bond96 ↔ 109 By similarity UniProtKB P00742
Disulfide bond111 ↔ 124 By similarity UniProtKB P00742
Disulfide bond132 ↔ 249Interchain (between light and heavy chains) By similarity UniProtKB P00742
Disulfide bond168 ↔ 184 By similarity UniProtKB P00742
Disulfide bond297 ↔ 311 By similarity UniProtKB P00742
Disulfide bond322 ↔ 350 By similarity UniProtKB P00742

Experimental info

Non-adjacent residues141 – 1422

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P83370-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 8484F03ADB6BBE17

FASTA37642,301
        10         20         30         40         50         60 
SNSLFEEIRP GNIERECIEE KCSKEEAREV FEDNEKTTTF WNVYVDGDQC SSNPCHYRGT 

        70         80         90        100        110        120 
CKDGIGSYTC TCLPNYEGKN CEKVLFKSCR AFNGNCWHFC KRVQSETQCS CAESYRLGVD 

       130        140        150        160        170        180 
GHSCVAEGDF SCGRNIKARN KIVNGMDSKL GECPWQAVLI NEKGEVFCGG TILSPIHVLT 

       190        200        210        220        230        240 
AAHCINQTKS VKETRRLLSV DKIYVHTKFV PPNYYYGHQN FDRVAYDYDI AIIRMKTPIQ 

       250        260        270        280        290        300 
FSENVVPACL PTADFANEVL MKQDSGIVSG FGRIRFKEPT SNTLKVITVP YVDRHTCMLS 

       310        320        330        340        350        360 
SDFRITQNMF CAGYDTLPQD ACQGDSGGPH ITAYGDTHFI TGIVSWGEGC ARKGKYGVYT 

       370 
KVSRFIPWIK KIMSLK

« Hide

Hide | Top

References

[1]"Group D prothrombin activators from snake venom are structural homologues of mammalian blood coagulation factor Xa."
Rao V.S., Joseph J.S., Kini R.M.
Biochem. J. 369:635-642(2003) [PubMed: 12403650] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MASS SPECTROMETRY.
Tissue: Venom gland.

Hide | Top

Cross-references

3D structure databases

HSSPHSSP built from PDB template 1HCG based on UniProtKB P00742.
ModBaseSearch...

Protein family/group databases

MEROPSS01.426.

Phylogenomic databases

HOVERGENP83370.

Enzyme and pathway databases

BRENDA3.4.21.6. 310322.

Family and domain databases

InterProIPR002383. Coagulation_factor_Gla.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR001438. EGF_2.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR018097. EGF_Ca_bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00010. EGFBLOOD.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameFA10V_HOPST
AccessionPrimary (citable) accession number: P83370
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

Hide | Top

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents