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P12412

- CYSEP_VIGMU

UniProt

P12412 - CYSEP_VIGMU

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Protein

Vignain

Gene
N/A
Organism
Vigna mungo (Black gram) (Phaseolus mungo)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521By similarity
Active sitei288 – 2881By similarity
Active sitei309 – 3091By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiC01.010.

Names & Taxonomyi

Protein namesi
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:
OrganismiVigna mungo (Black gram) (Phaseolus mungo)
Taxonomic identifieri3915 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

Subcellular locationi

Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation. Vacuolealeurone grain 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. vacuole Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 126106Activation peptide1 PublicationPRO_0000026445Add
BLAST
Chaini127 – 352226Vignain-1PRO_0000026446Add
BLAST
Chaini128 – 352225Vignain-2PRO_0000026447Add
BLAST
Propeptidei353 – 36210PRO_0000026448

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi149 ↔ 191By similarity
Disulfide bondi183 ↔ 224By similarity
Disulfide bondi282 ↔ 334By similarity

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliP12412.
SMRiP12412. Positions 127-352.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi359 – 3624Prevents secretion from ER

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12412-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAMKKLLWVV LSLSLVLGVA NSFDFHEKDL ESEESLWDLY ERWRSHHTVS
60 70 80 90 100
RSLGEKHKRF NVFKANVMHV HNTNKMDKPY KLKLNKFADM TNHEFRSTYA
110 120 130 140 150
GSKVNHHKMF RGSQHGSGTF MYEKVGSVPA SVDWRKKGAV TDVKDQGQCG
160 170 180 190 200
SCWAFSTIVA VEGINQIKTN KLVSLSEQEL VDCDKEENQG CNGGLMESAF
210 220 230 240 250
EFIKQKGGIT TESNYPYTAQ EGTCDESKVN DLAVSIDGHE NVPVNDENAL
260 270 280 290 300
LKAVANQPVS VAIDAGGSDF QFYSEGVFTG DCNTDLNHGV AIVGYGTTVD
310 320 330 340 350
GTNYWIVRNS WGPEWGEQGY IRMQRNISKK EGLCGIAMMA SYPIKNSSDN
360
PTGSLSSPKD EL
Length:362
Mass (Da):40,222
Last modified:October 1, 1989 - v1
Checksum:iB7C3B92868D5E3C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15732 mRNA. Translation: CAA33753.1.
X51900 Genomic DNA. Translation: CAA36181.1.
PIRiS12581.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15732 mRNA. Translation: CAA33753.1 .
X51900 Genomic DNA. Translation: CAA36181.1 .
PIRi S12581.

3D structure databases

ProteinModelPortali P12412.
SMRi P12412. Positions 127-352.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C01.010.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi 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 ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

  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)

Entry informationi

Entry nameiCYSEP_VIGMU
AccessioniPrimary (citable) accession number: P12412
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 29, 2014
This is version 96 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

External Data

Dasty 3