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P12412 (CYSEP_VIGMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. 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
Sulfhydryl-endopeptidase
Short name=SH-EP

Cleaved into the following 2 chains:

  1. Vignain-1
  2. Vignain-2
OrganismVigna mungo (Black gram) (Phaseolus mungo)
Taxonomic identifier3915 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

Protein attributes

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

General annotation (Comments)

Function

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

Catalytic activity

Hydrolysis of proteins, such as azocasein. Preferential cleavage: Asn-|-Xaa in small molecule substrates such as Boc-Asn-|-OPHNO2.

Subcellular location

Endoplasmic reticulum lumen. Vacuolealeurone grain Ref.3.

Post-translational modification

The mature protein is not glycosylated.

The precursor stored in the endoplasmic reticulum lumen is processed during the transport to proteins bodies to two dominant mature forms that differ by a single amino acid residue at the N-terminus.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Vacuole
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentaleurone grain

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

vacuole

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 126106Activation peptide
PRO_0000026445
Chain127 – 352226Vignain-1
PRO_0000026446
Chain128 – 352225Vignain-2
PRO_0000026447
Propeptide353 – 36210
PRO_0000026448

Regions

Motif359 – 3624Prevents secretion from ER

Sites

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

Amino acid modifications

Disulfide bond149 ↔ 191 By similarity
Disulfide bond183 ↔ 224 By similarity
Disulfide bond282 ↔ 334 By similarity

Sequences

Sequence LengthMass (Da)Tools
P12412 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: B7C3B92868D5E3C8

FASTA36240,222
        10         20         30         40         50         60 
MAMKKLLWVV LSLSLVLGVA NSFDFHEKDL ESEESLWDLY ERWRSHHTVS RSLGEKHKRF 

        70         80         90        100        110        120 
NVFKANVMHV HNTNKMDKPY KLKLNKFADM TNHEFRSTYA GSKVNHHKMF RGSQHGSGTF 

       130        140        150        160        170        180 
MYEKVGSVPA SVDWRKKGAV TDVKDQGQCG SCWAFSTIVA VEGINQIKTN KLVSLSEQEL 

       190        200        210        220        230        240 
VDCDKEENQG CNGGLMESAF EFIKQKGGIT TESNYPYTAQ EGTCDESKVN DLAVSIDGHE 

       250        260        270        280        290        300 
NVPVNDENAL LKAVANQPVS VAIDAGGSDF QFYSEGVFTG DCNTDLNHGV AIVGYGTTVD 

       310        320        330        340        350        360 
GTNYWIVRNS WGPEWGEQGY IRMQRNISKK EGLCGIAMMA SYPIKNSSDN PTGSLSSPKD 


EL 

« Hide

References

[1]"Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds."
Akasofu H., Yamauchi D., Mitsuhashi W., Minamikawa T.
Nucleic Acids Res. 17:6733-6733(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 132-140.
Tissue: Seed cotyledon.
[2]"Nucleotide sequence of the gene for the Vigna mungo sulfhydryl-endopeptidase (SH-EP)."
Akasofu H., Yamauchi D., Minamikawa T.
Nucleic Acids Res. 18:1892-1892(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leaf.
[3]"Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP)."
Okamoto T., Nakayama H., Seta K., Isobe T., Minamikawa T.
FEBS Lett. 351:31-34(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 127-140; 197-216; 324-333 AND 339-352, SUBCELLULAR LOCATION.
[4]Erratum
Okamoto T., Nakayama H., Seta K., Isobe T., Minamikawa T.
FEBS Lett. 356:152-152(1994)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15732 mRNA. Translation: CAA33753.1.
X51900 Genomic DNA. Translation: CAA36181.1.
PIRS12581.

3D structure databases

ProteinModelPortalP12412.
SMRP12412. 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_VIGMU
AccessionPrimary (citable) accession number: P12412
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 19, 2014
This is version 93 of the entry and version 1 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