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Protein

Vacuolar-processing enzyme

Gene
N/A
Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Asparagine-specific endopeptidase. Probably involved in the degradation of phaseolin during and after germination.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei167 – 1671Sequence analysis
Active sitei209 – 2091Sequence analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.34. 4746.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar-processing enzyme (EC:3.4.22.-)
Short name:
VPE
Alternative name(s):
Legumain-like proteinase
Short name:
LLP
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 484Sequence analysisPRO_0000026519
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Propeptidei25 – 44201 PublicationPRO_0000026517Add
BLAST
Chaini45 – ?Vacuolar-processing enzymePRO_0000026518

Keywords - PTMi

Zymogen

Proteomic databases

ProMEXiO24325.

Expressioni

Developmental stagei

Not expressed in dormant seeds. First detected 2 days after imbibition, reaching a maximum at 5-6 days after imbibition, then declining.1 Publication

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR001096. Peptidase_C13.
[Graphical view]
PANTHERiPTHR12000. PTHR12000. 1 hit.
PfamiPF01650. Peptidase_C13. 1 hit.
[Graphical view]
PIRSFiPIRSF019663. Legumain. 1 hit.
PRINTSiPR00776. HEMOGLOBNASE.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O24325-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTTATTSL LALLLLFLVA LVSAGRDLVG DFLRLPSDSG NGDNVHGTRW
60 70 80 90 100
AILFAGSSGY WNYRHQADIC HAYQLLRKGG LKDENIIVFM YDDIAFNSEN
110 120 130 140 150
PRRGVIINSP NGDEVYKGVP KDYTGEDVTA HNFYAALLGD KSKLTGGSGK
160 170 180 190 200
VVNSGPNDHI FIFYSDHGGP GVLGSPAGPY IYASDLNEVL KKKHASGTYK
210 220 230 240 250
NLVFYLEACE SGSIFEGLLP EDINVYATTA SNADESSWGT YCPGEDPSPP
260 270 280 290 300
PEYSTCLGDL YSVAWMEDSD RHNLRTETLH QQYKLVKERT ISGGLYYGSH
310 320 330 340 350
VMQYGDVGLS KDILFHYLGT DPANENLTFV DENSLWSSSK AVNQRDADLV
360 370 380 390 400
HFWDKFRKAP EGSPKKNEAR KQVLEVMSHR MHIDDSVELV GKLLFGIEKA
410 420 430 440 450
PELLNAVRPA GSALVDDWDC LKTMVRTFET HCGSLSQYGM KHMRSFANMC
460 470 480
NVGIKKEQMR EASAQACVTI PANPWSSLQR GFSA
Length:484
Mass (Da):53,389
Last modified:January 1, 1998 - v1
Checksum:i548DABEB99F7201D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z99956 Genomic DNA. Translation: CAB17078.1.
PIRiT12043.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z99956 Genomic DNA. Translation: CAB17078.1.
PIRiT12043.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

ProMEXiO24325.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.22.34. 4746.

Family and domain databases

InterProiIPR001096. Peptidase_C13.
[Graphical view]
PANTHERiPTHR12000. PTHR12000. 1 hit.
PfamiPF01650. Peptidase_C13. 1 hit.
[Graphical view]
PIRSFiPIRSF019663. Legumain. 1 hit.
PRINTSiPR00776. HEMOGLOBNASE.
ProtoNetiSearch...

Publicationsi

  1. "Does an asparaginyl-specific cysteine endopeptidase trigger phaseolin degradation in cotyledons of kidney bean seedlings?"
    Senyuk V., Rotari V., Becker C., Zakharov A., Horstmann C., Muentz K., Vaintraub I.
    Eur. J. Biochem. 258:546-558(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 45-56, FUNCTION, DEVELOPMENTAL STAGE.
    Strain: cv. Moldavian.
    Tissue: Cotyledon.

Entry informationi

Entry nameiVPE1_PHAVU
AccessioniPrimary (citable) accession number: O24325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: January 1, 1998
Last modified: October 14, 2015
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.