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Protein

Subtilisin-chymotrypsin inhibitor-2A

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits both subtilisin and chymotrypsin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei60 – 612Reactive bond

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI13.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Subtilisin-chymotrypsin inhibitor-2A
Short name:
CI-2A
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 8483Subtilisin-chymotrypsin inhibitor-2APRO_0000217649Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiP01053. 1 interaction.
MINTiMINT-242935.

Structurei

Secondary structure

1
84
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 283Combined sources
Helixi33 – 4311Combined sources
Beta strandi48 – 536Combined sources
Beta strandi57 – 593Combined sources
Beta strandi66 – 716Combined sources
Beta strandi75 – 773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CIQX-ray2.20A22-60[»]
B61-84[»]
1CIRNMR-A22-59[»]
B61-84[»]
1CISNMR-A22-84[»]
1COAX-ray2.20I22-84[»]
1CQ4X-ray1.80A21-59[»]
B61-84[»]
1LW6X-ray1.50I22-84[»]
1YPAX-ray2.00I22-84[»]
1YPBX-ray2.00I22-84[»]
1YPCX-ray1.70I22-84[»]
2CI2X-ray2.00I2-84[»]
2SNIX-ray2.10I2-84[»]
3CI2NMR-A19-84[»]
5FBZX-ray1.90B/D13-84[»]
5FFNX-ray1.80I13-84[»]
ProteinModelPortaliP01053.
SMRiP01053. Positions 22-84.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01053.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR000864. Prot_inh_pot1.
[Graphical view]
PfamiPF00280. potato_inhibit. 1 hit.
[Graphical view]
PRINTSiPR00292. POTATOINHBTR.
ProDomiPD002604. Prot_inh_pot1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54654. SSF54654. 1 hit.
PROSITEiPS00285. POTATO_INHIBITOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSVEKKPEG VNTGAGDRHN LKTEWPELVG KSVEEAKKVI LQDKPEAQII
60 70 80
VLPVGTIVTM EYRIDRVRLF VDKLDNIAQV PRVG
Length:84
Mass (Da):9,381
Last modified:January 23, 2007 - v2
Checksum:i594849D2B837F0E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791Q → E AA sequence (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05404 mRNA. Translation: CAA28988.1.
PIRiA01292. EIBH2A.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05404 mRNA. Translation: CAA28988.1.
PIRiA01292. EIBH2A.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CIQX-ray2.20A22-60[»]
B61-84[»]
1CIRNMR-A22-59[»]
B61-84[»]
1CISNMR-A22-84[»]
1COAX-ray2.20I22-84[»]
1CQ4X-ray1.80A21-59[»]
B61-84[»]
1LW6X-ray1.50I22-84[»]
1YPAX-ray2.00I22-84[»]
1YPBX-ray2.00I22-84[»]
1YPCX-ray1.70I22-84[»]
2CI2X-ray2.00I2-84[»]
2SNIX-ray2.10I2-84[»]
3CI2NMR-A19-84[»]
5FBZX-ray1.90B/D13-84[»]
5FFNX-ray1.80I13-84[»]
ProteinModelPortaliP01053.
SMRiP01053. Positions 22-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01053. 1 interaction.
MINTiMINT-242935.

Protein family/group databases

MEROPSiI13.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP01053.

Family and domain databases

InterProiIPR000864. Prot_inh_pot1.
[Graphical view]
PfamiPF00280. potato_inhibit. 1 hit.
[Graphical view]
PRINTSiPR00292. POTATOINHBTR.
ProDomiPD002604. Prot_inh_pot1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54654. SSF54654. 1 hit.
PROSITEiPS00285. POTATO_INHIBITOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of barley chymotrypsin inhibitor-2 (CI-2) and its expression in normal and high-lysine barley."
    Williamson M.S., Forde J., Buxton B., Kreis M.
    Eur. J. Biochem. 165:99-106(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Hiproly and cv. Sundance.
  2. "Characteristics of Hiproly barley III. Amino acid sequences of two lysine-rich proteins."
    Svendsen I., Martin B., Jonassen I.
    Carlsberg Res. Commun. 45:79-85(1980)
    Cited for: PROTEIN SEQUENCE OF 2-84.
    Strain: cv. Hiproly.
  3. "Identification of the reactive sites in two homologous serine proteinase inhibitors isolated from barley."
    Jonassen I., Svendsen I.
    Carlsberg Res. Commun. 47:199-203(1982)
    Cited for: REACTIVE SITE.
  4. "Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds."
    McPhalen C.A., James M.N.G.
    Biochemistry 26:261-269(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  5. "Direct observation of better hydration at the N terminus of an alpha-helix with glycine rather than alanine as the N-cap residue."
    Harpaz Y., Elmasry N., Fersht A.R., Henrick K.
    Proc. Natl. Acad. Sci. U.S.A. 91:311-315(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-84.
  6. "Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor. 2. Direct evidence for a nucleation-condensation mechanism."
    Neira J.L., Davis B., Ladurner A.G., Buckle A.M., de Prat G., Fersht A.R.
    Fold. Des. 1:189-208(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  7. "Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals."
    Ludvigsen S., Shen H.Y., Kjaer M., Madsen J.C., Poulsen F.M.
    J. Mol. Biol. 222:621-635(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiICI2_HORVU
AccessioniPrimary (citable) accession number: P01053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 110 of the entry and version 2 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. 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.