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Protein

Zingipain-2

Gene
N/A
Organism
Zingiber officinale (Ginger) (Amomum zingiber)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Preferential cleavage of peptides with a proline residue at the P2 position.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei27 – 271By similarity
Active sitei161 – 1611By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.67. 6754.

Protein family/group databases

MEROPSiC01.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Zingipain-2 (EC:3.4.22.67)
Alternative name(s):
Cysteine proteinase GP-II
OrganismiZingiber officinale (Ginger) (Amomum zingiber)
Taxonomic identifieri94328 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaZingiberalesZingiberaceaeZingiber

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 221221Zingipain-2PRO_0000050569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 651 Publication
Disulfide bondi58 ↔ 981 Publication
Glycosylationi99 – 991N-linked (GlcNAc...)1 PublicationCAR_000190
Disulfide bondi155 ↔ 2061 Publication
Glycosylationi156 – 1561N-linked (GlcNAc...)1 PublicationCAR_000200

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP82474.

Structurei

Secondary structure

1
221
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni9 – 135Combined sources
Helixi27 – 4418Combined sources
Helixi52 – 587Combined sources
Helixi70 – 8011Combined sources
Turni86 – 883Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi110 – 1145Combined sources
Helixi120 – 1278Combined sources
Beta strandi132 – 1365Combined sources
Helixi141 – 1444Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi161 – 17111Combined sources
Beta strandi174 – 1807Combined sources
Beta strandi192 – 1965Combined sources
Helixi205 – 2073Combined sources
Beta strandi213 – 2164Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQDX-ray2.10A/B/C/D1-221[»]
ProteinModelPortaliP82474.
SMRiP82474. Positions 3-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP82474.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P82474-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DDLPDSIDWR ENGAVVPVKN QGGCGSCWAF STVAAVEGIN QIVTGDLISL
60 70 80 90 100
SEQQLVDCTT ANHGCRGGWM NPAFQFIVNN GGINSEETYP YRGQDGICNS
110 120 130 140 150
TVNAPVVSID SYENVPSHNE QSLQKAVANQ PVSVTMDAAG RDFQLYRSGI
160 170 180 190 200
FTGSCNISAN HALTVVGYGT ENDKDFWIVK NSWGKNWGES GYIRAERNIE
210 220
NPDGKCGITR FASYPVKKGT N
Length:221
Mass (Da):23,922
Last modified:May 30, 2000 - v1
Checksum:i909A312BD8632D42
GO

Sequence databases

PIRiA59041.

Cross-referencesi

Sequence databases

PIRiA59041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQDX-ray2.10A/B/C/D1-221[»]
ProteinModelPortaliP82474.
SMRiP82474. Positions 3-218.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC01.017.

PTM databases

UniCarbKBiP82474.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.22.67. 6754.

Miscellaneous databases

EvolutionaryTraceiP82474.

Family and domain databases

InterProiIPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale."
    Choi K.H., Laursen R.A.
    Eur. J. Biochem. 267:1516-1526(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Root.
  2. "The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale."
    Choi K.H., Laursen R.A., Allen K.N.
    Biochemistry 38:11624-11633(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION.

Entry informationi

Entry nameiCPGP2_ZINOF
AccessioniPrimary (citable) accession number: P82474
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: October 14, 2015
This is version 68 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.