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Protein

Vacuolar-processing enzyme beta-isozyme

Gene

bVPE

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms (By similarity). Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds (PubMed:12417707, PubMed:14688293).By similarity2 Publications

Catalytic activityi

Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa-bonds.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei169 – 1691Sequence analysis
Active sitei211 – 2111Sequence analysis
Sitei258 – 2581Required for post-translational maturation and enzyme activityBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciARA:AT1G62710-MONOMER.

Protein family/group databases

MEROPSiC13.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar-processing enzyme beta-isozyme1 Publication (EC:3.4.22.34By similarity)
Alternative name(s):
Asparaginyl endopeptidase beta-VPECurated
Beta-VPE1 Publication
Gene namesi
Name:bVPE1 Publication
Ordered Locus Names:At1g62710Imported
ORF Names:F23N19.7Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G62710.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Disruption phenotypei

No macroscopic phenotype, probably due to functional redundancy (PubMed:12417707, PubMed:14688293). Slight differences in polypeptide accumulation in seeds with an increased amount of propolypeptide forms of legumin-type globulins (PubMed:12417707). In plants lacking all vacuolar-processing enzyme isozymes (e.g. alpha, beta, gamma and delta) shift of storage protein accumulation from normally processed polypeptides to a finite number of prominent alternatively processed polypeptides cleaved at sites other than the conserved Asn residues targeted by VPE (PubMed:14688293).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 486465Vacuolar-processing enzyme beta-isozymePRO_0000026527Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi309 – 3091N-linked (GlcNAc...)PROSITE-ProRule annotation

Post-translational modificationi

Auto-catalytic activation.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ39044.
PRIDEiQ39044.

Expressioni

Tissue specificityi

Seed specific. Also expressed in the flowers and buds.3 Publications

Gene expression databases

GenevisibleiQ39044. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G62710.1.

Structurei

3D structure databases

ProteinModelPortaliQ39044.
SMRiQ39044. Positions 52-450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1348. Eukaryota.
COG5206. LUCA.
HOGENOMiHOG000236335.
InParanoidiQ39044.
KOiK01369.
OMAiRHRKHLD.
PhylomeDBiQ39044.

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.

Q39044-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKSCYFRPA LLLLLVLLVH AESRGRFEPK ILMPTEEANP ADQDEDGVGT
60 70 80 90 100
RWAVLVAGSS GYGNYRHQAD VCHAYQILRK GGLKEENIVV LMYDDIANHP
110 120 130 140 150
LNPRPGTLIN HPDGDDVYAG VPKDYTGSSV TAANFYAVLL GDQKAVKGGS
160 170 180 190 200
GKVIASKPND HIFVYYADHG GPGVLGMPNT PHIYAADFIE TLKKKHASGT
210 220 230 240 250
YKEMVIYVEA CESGSIFEGI MPKDLNIYVT TASNAQESSY GTYCPGMNPS
260 270 280 290 300
PPSEYITCLG DLYSVAWMED SETHNLKKET IKQQYHTVKM RTSNYNTYSG
310 320 330 340 350
GSHVMEYGNN SIKSEKLYLY QGFDPATVNL PLNELPVKSK IGVVNQRDAD
360 370 380 390 400
LLFLWHMYRT SEDGSRKKDD TLKELTETTR HRKHLDASVE LIATILFGPT
410 420 430 440 450
MNVLNLVREP GLPLVDDWEC LKSMVRVFEE HCGSLTQYGM KHMRAFANVC
460 470 480
NNGVSKELME EASTAACGGY SEARYTVHPS ILGYSA
Length:486
Mass (Da):53,828
Last modified:July 11, 2002 - v3
Checksum:i8B3EFD53CDAEC9C3
GO

Sequence cautioni

The sequence AAF19550.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti288 – 2892Missing in BAA09615 (PubMed:7579169).Curated
Sequence conflicti324 – 3241D → E in BAA09615 (PubMed:7579169).Curated
Sequence conflicti337 – 3371V → A in BAA09615 (PubMed:7579169).Curated
Sequence conflicti358 – 3581Y → H in BAA09615 (PubMed:7579169).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D61394 Genomic DNA. Translation: BAA09615.1.
AC007190 Genomic DNA. Translation: AAF19550.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE33996.1.
AY059156 mRNA. Translation: AAL15381.1.
AF367254 mRNA. Translation: AAK56243.1.
PIRiC96652.
S60050.
RefSeqiNP_176458.1. NM_104948.3.
UniGeneiAt.16374.

Genome annotation databases

EnsemblPlantsiAT1G62710.1; AT1G62710.1; AT1G62710.
GeneIDi842569.
GrameneiAT1G62710.1; AT1G62710.1; AT1G62710.
KEGGiath:AT1G62710.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D61394 Genomic DNA. Translation: BAA09615.1.
AC007190 Genomic DNA. Translation: AAF19550.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE33996.1.
AY059156 mRNA. Translation: AAL15381.1.
AF367254 mRNA. Translation: AAK56243.1.
PIRiC96652.
S60050.
RefSeqiNP_176458.1. NM_104948.3.
UniGeneiAt.16374.

3D structure databases

ProteinModelPortaliQ39044.
SMRiQ39044. Positions 52-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G62710.1.

Protein family/group databases

MEROPSiC13.001.

Proteomic databases

PaxDbiQ39044.
PRIDEiQ39044.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G62710.1; AT1G62710.1; AT1G62710.
GeneIDi842569.
GrameneiAT1G62710.1; AT1G62710.1; AT1G62710.
KEGGiath:AT1G62710.

Organism-specific databases

TAIRiAT1G62710.

Phylogenomic databases

eggNOGiKOG1348. Eukaryota.
COG5206. LUCA.
HOGENOMiHOG000236335.
InParanoidiQ39044.
KOiK01369.
OMAiRHRKHLD.
PhylomeDBiQ39044.

Enzyme and pathway databases

BioCyciARA:AT1G62710-MONOMER.

Miscellaneous databases

PROiQ39044.

Gene expression databases

GenevisibleiQ39044. AT.

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

« Hide 'large scale' publications
  1. "Homologues of a vacuolar processing enzyme that are expressed in different organs in Arabidopsis thaliana."
    Kinoshita T., Nishimura M., Hara-Nishimura I.
    Plant Mol. Biol. 29:81-89(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions."
    Kinoshita T., Yamada K., Hiraiwa N., Kondo M., Nishimura M., Hara-Nishimura I.
    Plant J. 19:43-53(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  6. "Redundant proteolytic mechanisms process seed storage proteins in the absence of seed-type members of the vacuolar processing enzyme family of cysteine proteases."
    Gruis D.F., Selinger D.A., Curran J.M., Jung R.
    Plant Cell 14:2863-2882(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.
  7. "Storage protein accumulation in the absence of the vacuolar processing enzyme family of cysteine proteases."
    Gruis D., Schulze J., Jung R.
    Plant Cell 16:270-290(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiVPEB_ARATH
AccessioniPrimary (citable) accession number: Q39044
Secondary accession number(s): Q93VS7, Q9SI79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: February 17, 2016
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.