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P60994 (ERVB_TABDI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cysteine protease.

Subcellular location

Secreted.

Tissue specificity

Laticifer.

Post-translational modification

Not glycosylated.

Miscellaneous

Stable in 8 M urea and 2.5 M GuHCl at neutral pH, in 40% acetonitrile, 70% ethanol and 50% methanol. Unstable in SDS.

Sequence similarities

Belongs to the peptidase C1 family.

Biophysicochemical properties

pH dependence:

Active from pH 3.0 to 10.5.

Temperature dependence:

Active up to 62 degrees Celsius.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Ervatamin-B
PRO_0000050558

Sites

Active site251
Active site1581
Active site1781 By similarity

Amino acid modifications

Disulfide bond22 ↔ 63
Disulfide bond56 ↔ 96
Disulfide bond152 ↔ 203

Secondary structure

................................. 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60994 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: 4DE62E43BA4F4F83

FASTA21523,183
        10         20         30         40         50         60 
LPSFVDWRSK GAVNSIKNQK QCGSCWAFSA VAAVESINKI RTGQLISLSE QELVDCDTAS 

        70         80         90        100        110        120 
HGCNGGWMNN AFQYIITNGG IDTQQNYPYS AVQGSCKPYR LRVVSINGFQ RVTRNNESAL 

       130        140        150        160        170        180 
QSAVASQPVS VTVEAAGAPF QHYSSGIFTG PCGTAQNHGV VIVGYGTQSG KNYWIVRNSW 

       190        200        210 
GQNWGNQGYI WMERNVASSA GLCGIAQLPS YPTKA 

« Hide

References

[1]"Proposed amino acid sequence and the 1.63 A X-ray crystal structure of a plant cysteine protease, ervatamin B: some insights into the structural basis of its stability and substrate specificity."
Biswas S., Chakrabarti C., Kundu S., Jagannadham M.V., Dattagupta J.K.
Proteins 51:489-497(2003) [PubMed: 12784208] [Abstract]
Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[2]"Purification and characterization of a stable cysteine protease ervatamin B, with two disulfide bridges, from the latex of Ervatamia coronaria."
Kundu S., Sundd M., Jagannadham M.V.
J. Agric. Food Chem. 48:171-179(2000) [PubMed: 10691612] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-21, CHARACTERIZATION.
Tissue: Latex.

Cross-references

Sequence databases

PIRA59428.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWDX-ray1.63A1-215[»]
ProteinModelPortalP60994.
SMRP60994. Positions 1-215.
ModBaseSearch...

Protein family/group databases

MEROPSC01.099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameERVB_TABDI
AccessionPrimary (citable) accession number: P60994
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: November 16, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families