P83654 (ERVC_TABDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ervatamin-C Short name=ERV-C EC=3.4.22.-
Organism	Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria)
Taxonomic identifier	52861 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Rauvolfioideae › Tabermontantaneae › Tabernaemontana

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cysteine proteinase. Hydrolyzes denatured natural substrates such as casein, hemoglobin, azoalbumin and azocasein with a high specific activity. Has little or no activity against synthetic substrates. Ref.3
Enzyme regulation	Activated by thio-specific activators such as cysteine, beta-mercaptoethanol, DTT and glutathione. Inhibited by the thiol-specific inhibitors leupeptin, iodoacetamide, PCMB, NEM, mercuric chloride and sodium tetrathionate. Ref.3
Subunit structure	Monomer. Ref.2
Subcellular location	Secreted Ref.2.
Tissue specificity	Laticifer. Ref.2
Sequence similarities	Belongs to the peptidase C1 family.
Biophysicochemical properties	Kinetic parameters: KM=9.09 µM for azoalbumin pH dependence: Optimum pH is 7.5-8.0 with azoalbumin or hemoglobin as substrate. Active and stable from pH 2.0 to 12.0. Temperature dependence: Optimum temperature is 50 degrees Celsius with azoalbumin as substrate. Thermostable up to 70 degrees Celsius.
Mass spectrometry	Molecular mass is 23000 Da from positions 1 - 208. Determined by MALDI. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from direct assay Ref.3. Source: UniProtKB
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type endopeptidase activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 208

208

Ervatamin-C

PRO_0000050559

Sites

Active site

25

1

By similarity UniProtKB P00785

Active site

157

1

By similarity UniProtKB P00785

Active site

173

1

By similarity UniProtKB P00785

Amino acid modifications

Disulfide bond

22 ↔ 63

Ref.1

Disulfide bond

56 ↔ 96

Ref.1

Disulfide bond

114 ↔ 193

Ref.1

Disulfide bond

151 ↔ 196

Ref.1

Experimental info

Sequence conflict

17

1

K → W AA sequence Ref.3

Sequence conflict

21

1

S → W AA sequence Ref.3

Secondary structure

1

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208

Helix Strand Turn

Details...

Helix

7 – 10

4

Beta strand

21 – 23

3

Helix

25 – 42

18

Helix

50 – 56

7

Helix

68 – 78

11

Turn

84 – 86

3

Beta strand

107 – 110

4

Helix

116 – 125

10

Beta strand

128 – 132

5

Helix

137 – 140

4

Beta strand

144 – 147

4

Beta strand

157 – 164

8

Beta strand

166 – 172

7

Beta strand

184 – 188

5

Helix

195 – 197

3

Beta strand

203 – 206

4

Sequences

	Sequence		Length	Mass (Da)
	P83654 [UniParc]. Last modified April 26, 2004. Version 1. Checksum: 13CD944089802C12	FASTA	208	22,523
	10 20 30 40 50 60 LPEQIDWRKK GAVTPVKNQG SCGSCWAFST VSTVESINQI RTGNLISLSE QELVDCDKKN 70 80 90 100 110 120 HGCLGGAFVF AYQYIINNGG IDTQANYPYK AVQGPCQAAS KVVSIDGYNG VPFCNEXALK 130 140 150 160 170 180 QAVAVQPSTV AIDASSAQFQ QYSSGIFSGP CGTKLNHGVT IVGYQANYWI VRNSWGRYWG 190 200 EKGYIRMLRV GGCGLCGIAR LPYYPTKA

References

[1]	"Structural basis of the unusual stability and substrate specificity of ervatamin C, a plant cysteine protease from Ervatamia coronaria." Guha Thakurta P., Biswas S., Chakrabarti C., Sundd M., Jagannadham M.V., Dattagupta J.K. Biochemistry 43:1532-1540(2004) [PubMed: 14769029] [Abstract] Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MASS SPECTROMETRY, DISULFIDE BONDS.
[2]	Guha Thakurta P., Biswas S., Chakrabarti C., Dattagupta J.K. Submitted (AUG-2003) to UniProtKB Cited for: PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Latex.
[3]	"Purification and characterization of a highly stable cysteine protease from the latex of Ervatamia coronaria." Sundd M., Kundu S., Pal G.P., Medicherla J.V. Biosci. Biotechnol. Biochem. 62:1947-1955(1998) [PubMed: 9836431] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21, FUNCTION, ENZYME REGULATION. Tissue: Latex.
[4]	"Structural characterization of a highly stable cysteine protease ervatamin C." Kundu S., Sundd M., Jagannadham M.V. Biochem. Biophys. Res. Commun. 264:635-642(1999) [PubMed: 10543984] [Abstract] Cited for: STABILITY. Tissue: Latex.
+	Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O0E	X-ray	1.90	A/B	1-208	[»]
2PNS	X-ray	1.90	A/B	1-208	[»]

ModBase

Search...

Protein family/group databases

MEROPS

C01.116.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]

PANTHER

PTHR12411. Peptidase_C1A. 1 hit.

Pfam

PF00112. Peptidase_C1. 1 hit.
[Graphical view]

PRINTS

PR00705. PAPAIN.

SMART

SM00645. Pept_C1. 1 hit.
[Graphical view]

PROSITE

PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ERVC_TABDI

Accession

Primary (citable) accession number: P83654

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	March 2, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program