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

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P81428 (FAXD_TROCA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 87. History...

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

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	Recommended name: Trocarin-D EC=3.4.21.6 Alternative name(s): Venom coagulation factor Xa-like protease Venom prothrombin activator trocarin-D Short name=vPA trocarin-D Cleaved into the following 2 chains: Trocarin-D light chain Trocarin-D 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

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

General annotation (Comments)

Function	Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa. Induces cyanosis and death in mice at 1 mg/kg body weight during blood clotting. Ref.3
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	Heterodimer of a light chain and a heavy chain; disulfide-linked.
Subcellular location	Secreted Ref.3 Ref.5.
Tissue specificity	Expressed by the venom gland. Ref.3 Ref.5
Post-translational modification	Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium. 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 non-specific.
Miscellaneous	Is classified in the group D of snake venom prothrombin activators, since it requires the mammalian factor Va for maximal activity for the cleavage of prothrombin. In contrast to blood coagulation factors that circulate as inactive zymogen in plasma, venom prothrombin activators are always found in the active form in the venom.
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.

Ontologies

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Potential

Propeptide

21 – 40

PRO_0000043207

Chain

41 – 181

141

Trocarin-D light chain

PRO_0000027822

Propeptide

182 – 209

Activation peptide

PRO_0000043208

Chain

210 – 455

246

Trocarin-D heavy chain

PRO_0000027823

Regions

Domain

41 – 86

Gla

Domain

86 – 122

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 Ref.3

Modified residue

4-carboxyglutamate Ref.3

Modified residue

4-carboxyglutamate Ref.3

Modified residue

4-carboxyglutamate Ref.3

Modified residue

4-carboxyglutamate Ref.3

Modified residue

4-carboxyglutamate Ref.3

Modified residue

4-carboxyglutamate Ref.3

Modified residue

4-carboxyglutamate Ref.3

Modified residue

4-carboxyglutamate Ref.3

Modified residue

4-carboxyglutamate Ref.3

Modified residue

4-carboxyglutamate Ref.3

Glycosylation

O-linked (Hex...) Ref.3 Ref.5

Glycosylation

254

N-linked (GlcNAc...) Ref.3 Ref.5

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

Experimental info

Sequence conflict

260 – 270

Missing AA sequence Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P81428 [UniParc].

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

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]	"Structure of two genes encoding parallel prothrombin activators in Tropidechis carinatus snake: gene duplication and recruitment of factor X gene to the venom gland." Reza M.A., Swarup S., Kini R.M. J. Thromb. Haemost. 5:117-126(2007) [PubMed: 17239167] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Venom gland.
[3]	"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 AND 210-455, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47; GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-72 AND GLU-75, GLYCOSYLATION AT SER-92 AND ASN-254. Tissue: Venom.
[4]	"Classification and nomenclature of prothrombin activators isolated from snake venoms." Manjunatha Kini R., Morita T., Rosing J. Thromb. Haemost. 86:710-711(2001) [PubMed: 11522026] [Abstract] Cited for: NOMENCLATURE.
[5]	"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: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION AT SER-92 AND ASN-254, SIALIC ACID CONTENT, MASS SPECTROMETRY. Tissue: Venom.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY769963 mRNA. Translation: AAV34695.1. DQ017707 mRNA. Translation: AAY85309.1. DQ533832 Genomic DNA. Translation: ABG02404.1.
3D structure databases
ProteinModelPortal	P81428.
SMR	P81428. Positions 42-86, 210-453.
ModBase	Search...
Protein family/group databases
MEROPS	S01.425.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG013304.
Family and domain databases
InterPro	IPR017857. Coagulation_fac_subgr_Gla_dom. IPR006209. EGF. IPR006210. EGF-like. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR000742. EGF_3. IPR018097. EGF_Ca-bd_CS. IPR000294. GLA_domain. IPR009003. Pept_cys/ser_Trypsin-like. IPR012224. Pept_S1A_FX. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Gene3D	G3DSA:4.10.740.10. Coagulation_factor_Gla. 1 hit.
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]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit. SSF57630. VitK_dep_GLA. 1 hit.
PROSITE	PS00010. ASX_HYDROXYL. 1 hit. PS00022. EGF_1. 1 hit. PS01186. EGF_2. False negative. 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...

Entry information

Entry name

FAXD_TROCA

Accession

Primary (citable) accession number: P81428
Secondary accession number(s): Q1L657, Q5UAE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 6, 2005
Last modified:	November 16, 2011
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents