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P25803 (CYSEP_PHAVU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 namesRecommended name:
Vignain

EC=3.4.22.-
Alternative name(s):
Bean endopeptidase
Cysteine proteinase EP-C1
OrganismPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifier3885 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Thought to be involved in the hydrolysis of stored seed proteins.

Subunit structure

Monomer.

Subcellular location

Endoplasmic reticulum lumen.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMGlycoprotein
Zymogen
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 131111Activation peptide Potential
PRO_0000026440
Chain132 – 362231Vignain
PRO_0000026441

Regions

Motif359 – 3624Prevents secretion from ER Potential

Sites

Active site1521 By similarity
Active site2881 By similarity
Active site3091 By similarity

Amino acid modifications

Glycosylation3261N-linked (GlcNAc...) Potential
Glycosylation3461N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1071P → H in CAA40073. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P25803 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 9AAF24A557FAF806

FASTA36240,212
        10         20         30         40         50         60 
MATKKLLWVV LSFSLVLGVA NSFDFHDKDL ASEESLWDLY ERWRSHHTVS RSLGEKHKRF 

        70         80         90        100        110        120 
NVFKANLMHV HNTNKMDKPY KLKLNKFADM TNHEFRSTYA GSKVNHPRMF RGTPHENGAF 

       130        140        150        160        170        180 
MYEKVVSVPP SVDWRKKGAV TDVKDQGQCG SCWAFSTVVA VEGINQIKTN KLVALSEQEL 

       190        200        210        220        230        240 
VDCDKEENQG CNGGLMESAF EFIKQKGGIT TESNYPYKAQ EGTCDASKVN DLAVSIDGHE 

       250        260        270        280        290        300 
NVPANDEDAL LKAVANQPVS VAIDAGGSDF QFYSEGVFTG DCSTDLNHGV AIVGYGTTVD 

       310        320        330        340        350        360 
GTNYWIVRNS WGPEWGEHGY IRMQRNISKK EGLCGIAMLP SYPIKNSSDN PTGSFSSPKD 


EL 

« Hide

References

[1]"Nucleotide sequence of a gene for an endopeptidase (EP-C1) from Phaseolus vulgaris."
Ogushi Y., Tanaka T., Yamauchi D., Minamikawa T.
Plant Mol. Biol. 19:705-706(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Saxa.
Tissue: Seedling.
[2]"Nucleotide sequence of cDNA for an endopeptidase (EP-C1) from pods of maturing Phaseolus vulgaris fruits."
Tanaka T., Yamauchi D., Minamikawa T.
Plant Mol. Biol. 16:1083-1084(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-362.
Strain: cv. Goldstar.
Tissue: Fruit.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63102 Genomic DNA. Translation: CAA44816.1.
X56753 mRNA. Translation: CAA40073.1.
PIRS22502.

3D structure databases

ProteinModelPortalP25803.
SMRP25803. Positions 127-352.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC01.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSEP_PHAVU
AccessionPrimary (citable) accession number: P25803
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 1, 1994
Last modified: February 19, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries