P12412 (CYSEP_VIGMU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended 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: Vignain-1 Vignain-2
Organism	Vigna mungo (Black gram) (Phaseolus mungo)
Taxonomic identifier	3915 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Vigna

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Vacuole › aleurone 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 component	Endoplasmic reticulum Vacuole
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	aleurone 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_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 126	106	Activation peptide		PRO_0000026445
	Chain	127 – 352	226	Vignain-1		PRO_0000026446
	Chain	128 – 352	225	Vignain-2		PRO_0000026447
	Propeptide	353 – 362	10			PRO_0000026448
Regions
	Motif	359 – 362	4	Prevents secretion from ER
Sites
	Active site	152	1	By similarity
	Active site	288	1	By similarity
	Active site	309	1	By similarity
Amino acid modifications
	Disulfide bond	149 ↔ 191		By similarity
	Disulfide bond	183 ↔ 224		By similarity
	Disulfide bond	282 ↔ 334		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P12412 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: B7C3B92868D5E3C8	FASTA	362	40,222
	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

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.
PIR	S12581.
3D structure databases
ProteinModelPortal	P12412.
SMR	P12412. Positions 127-352.
ModBase	Search...
Protein family/group databases
MEROPS	I29.003.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR025661. Pept_asp_AS. IPR000169. Pept_cys_AS. IPR025660. Pept_his_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view]
PANTHER	PTHR12411. PTHR12411. 1 hit.
Pfam	PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view]
PRINTS	PR00705. PAPAIN.
SMART	SM00848. Inhibitor_I29. 1 hit. SM00645. Pept_C1. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. PS00640. THIOL_PROTEASE_ASN. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSEP_VIGMU

Accession

Primary (citable) accession number: P12412

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program