Trocarin precursor - Tropidechis carinatus (Australian rough-scaled snake)

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Reviewed, UniProtKB/Swiss-Prot P81428 (FA10V_TROCA)

Last modified June 16, 2009. Version 72. History...

Clusters with 100%, 90%, 50% identity |

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

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Names and origin

Protein names	Recommended name: Trocarin EC=3.4.21.6 Alternative name(s): Venom coagulation factor Xa-like protease Cleaved into the following 2 chains: 1- Recommended name: Trocarin light chain 2- Recommended name: Trocarin heavy chain
Organism	Tropidechis carinatus (Australian rough-scaled snake)
Taxonomic identifier	100989 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Notechinae › Tropidechis

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Protein attributes

Sequence length	455 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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. Induces cyanosis and death in mice at 1 mg/kg body weight during blood clotting.
Catalytic activity	Selective cleavage of Arg-\|-Thr and then Arg-\|-Ile bonds in prothrombin to form thrombin.
Enzyme regulation	Activated by calcium and phospholipids.
Subunit structure	The two chains are formed from a single-chain precursor and are held together by a disulfide bond.
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. The O-linked saccharides at Ser-92 are a mixture of Xyl-Glc, and Glc along with smaller amounts of Xyl-GlcNAc, GlcNAc, Gal, GalNAc, Xyl-Gal, and Xyl-GalNAc, suggesting that the glycosyl transferases responsible for this modification are nonspecific.
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.

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Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease Toxin
PTM	Cleavage on pair of basic residues Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Potential

Propeptide

21 – 40

Ref.2

PRO_0000043207

Chain

41 – 181

141

Trocarin light chain

PRO_0000027822

Propeptide

182 – 209

PRO_0000043208

Chain

210 – 455

246

Trocarin heavy chain

PRO_0000027823

Regions

Domain

41 – 86

Gla

Domain

90 – 121

EGF-like 1; calcium-binding

Domain

129 – 164

EGF-like 2

Domain

210 – 453

244

Peptidase S1

Sites

Active site

251

Charge relay system By similarity

Active site

308

Charge relay system By similarity

Active site

405

Charge relay system By similarity

Site

103

Not modified

Amino acid modifications

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Glycosylation

O-linked (Hex...) Ref.3

Glycosylation

254

N-linked (GlcNAc...)

Disulfide bond

57 ↔ 62

By similarity

Disulfide bond

90 ↔ 101

By similarity

Disulfide bond

95 ↔ 110

By similarity

Disulfide bond

112 ↔ 121

By similarity

Disulfide bond

129 ↔ 140

By similarity

Disulfide bond

136 ↔ 149

By similarity

Disulfide bond

151 ↔ 164

By similarity

Disulfide bond

172 ↔ 328

Interchain (between light and heavy chains) By similarity

Disulfide bond

216 ↔ 221

By similarity

Disulfide bond

236 ↔ 252

By similarity

Disulfide bond

376 ↔ 390

By similarity

Disulfide bond

401 ↔ 429

By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P81428-1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 65C8571B662782DC
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FASTA

455

51,407

        10         20         30         40         50         60 
MAPQLLLCLI LTFLWSLPEA ESNVFLKSKV ANRFLQRTKR SNSLFEEIRP GNIERECIEE 

        70         80         90        100        110        120 
KCSKEEAREV FEDNEKTETF WNVYVDGDQC SSNPCHYRGT CKDGIGSYTC TCLPNYEGKN 

       130        140        150        160        170        180 
CEKVLYQSCR VDNGNCWHFC KRVQSETQCS CAESYRLGVD GHSCVAEGDF SCGRNIKARN 

       190        200        210        220        230        240 
KREASLPDFV QSQKATLLKK SDNPSPDIRI VNGMDCKLGE CPWQAVLINE KGEVFCGGTI 

       250        260        270        280        290        300 
LSPIHVLTAA HCINQTKSVS VIVGEIDISR KETRRLLSVD KIYVHTKFVP PNYYYVHQNF 

       310        320        330        340        350        360 
DRVAYDYDIA IIRMKTPIQF SENVVPACLP TADFANEVLM KQDSGIVSGF GRIQFKQPTS 

       370        380        390        400        410        420 
NTLKVITVPY VDRHTCMLSS DFRITQNMFC AGYDTLPQDA CQGDSGGPHI TAYRDTHFIT 

       430        440        450 
GIISWGEGCA RKGKYGVYTK VSKFIPWIKK IMSLK

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References

[1]	"Comparative analysis of prothrombin activators from the venom of Australian elapids." St Pierre L., Masci P.P., Filippovich I., Sorokina N., Marsh N., Miller D.J., Lavin M.F. Mol. Biol. Evol. 22:1853-1864(2005) [PubMed: 15930152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Amino acid sequence of trocarin, a prothrombin activator from Tropidechis carinatus venom: its structural similarity to coagulation factor Xa." Joseph J.S., Chung M.C.M., Jeyaseelan K., Kini R.M. Blood 94:621-631(1999) [PubMed: 10397729] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-181; 210-259 AND 271-455, CHARACTERIZATION. Tissue: Venom.
[3]	"Occurrence of O-linked Xyl-GlcNAc and Xyl-Glc disaccharides in trocarin, a factor Xa homolog from snake venom." Joseph J.S., Valiyaveettil M., Gowda D.C., Kini R.M. J. Thromb. Haemost. 1:545-550(2003) [PubMed: 12871464] [Abstract] Cited for: GLYCOSYLATION AT SER-92, MASS SPECTROMETRY.

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Cross-references

Sequence databases
	AY769963 mRNA. Translation: AAV34695.1.
3D structure databases
HSSP	HSSP built from PDB template 1HCG based on UniProtKB P00742.
ModBase	Search...
Protein family/group databases
MEROPS	S01.425.
Phylogenomic databases
HOVERGEN	P81428.
Enzyme and pathway databases
BRENDA	3.4.21.6. 295067.
Family and domain databases
InterPro	IPR002383. Coagulation_factor_Gla. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_CS. 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]
Pfam	PF00008. EGF. 1 hit. PF00594. Gla. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001143. Factor_X. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN. PR00001. GLABLOOD.
SMART	SM00181. EGF. 1 hit. SM00179. EGF_CA. 1 hit. SM00069. GLA. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS00010. 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]
ProtoNet	Search...

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Entry information

Entry name

FA10V_TROCA

Accession

Primary (citable) accession number: P81428
Secondary accession number(s): Q5UAE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 6, 2005
Last modified:	June 16, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)

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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)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents