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Protein

Eglin C

Gene
N/A
Organism
Hirudo medicinalis (Medicinal leech)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits both elastase and cathepsin G.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei45 – 462Reactive bond

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI13.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Eglin C
OrganismiHirudo medicinalis (Medicinal leech)
Taxonomic identifieri6421 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaArhynchobdellidaHirudiniformesHirudinidaeHirudo

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7070Eglin CPRO_0000217645Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-6069N.
MINTiMINT-1345724.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 133Combined sources
Helixi18 – 2811Combined sources
Beta strandi32 – 387Combined sources
Beta strandi42 – 443Combined sources
Beta strandi48 – 5710Combined sources
Turni58 – 614Combined sources
Beta strandi68 – 703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACBX-ray2.00I1-70[»]
1CSEX-ray1.20I1-70[»]
1EGLNMR-A1-70[»]
1EGPX-ray2.00A1-45[»]
B46-70[»]
1MEEX-ray2.00I7-70[»]
1SBNX-ray2.10I1-70[»]
1SIBX-ray2.40I1-70[»]
1TECX-ray2.20I1-70[»]
2SECX-ray1.80I1-70[»]
2TECX-ray1.98I1-70[»]
3TECX-ray2.00I1-70[»]
4B1TX-ray1.78B/D1-70[»]
4B2AX-ray1.89B/D5-70[»]
4B2BX-ray1.36B/D1-70[»]
4B2CX-ray1.43B/D1-70[»]
4H4FX-ray1.90B8-70[»]
ProteinModelPortaliP01051.
SMRiP01051. Positions 1-70.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01051.

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.

P01051-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
TEFGSELKSF PEVVGKTVDQ AREYFTLHYP QYDVYFLPEG SPVTLDLRYN
60 70
RVRVFYNPGT NVVNHVPHVG
Length:70
Mass (Da):8,091
Last modified:July 21, 1986 - v1
Checksum:i7E5C5BBD39DC3C11
GO

Sequence databases

PIRiA94592. EILXCH.

Cross-referencesi

Sequence databases

PIRiA94592. EILXCH.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACBX-ray2.00I1-70[»]
1CSEX-ray1.20I1-70[»]
1EGLNMR-A1-70[»]
1EGPX-ray2.00A1-45[»]
B46-70[»]
1MEEX-ray2.00I7-70[»]
1SBNX-ray2.10I1-70[»]
1SIBX-ray2.40I1-70[»]
1TECX-ray2.20I1-70[»]
2SECX-ray1.80I1-70[»]
2TECX-ray1.98I1-70[»]
3TECX-ray2.00I1-70[»]
4B1TX-ray1.78B/D1-70[»]
4B2AX-ray1.89B/D5-70[»]
4B2BX-ray1.36B/D1-70[»]
4B2CX-ray1.43B/D1-70[»]
4H4FX-ray1.90B8-70[»]
ProteinModelPortaliP01051.
SMRiP01051. Positions 1-70.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6069N.
MINTiMINT-1345724.

Protein family/group databases

MEROPSiI13.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP01051.

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. "Structure of the elastase-cathepsin G inhibitor of the leech Hirudo medicinalis."
    Seemueller U., Eulitz M., Fritz H., Strobl A.
    Hoppe-Seyler's Z. Physiol. Chem. 361:1841-1846(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. Fritz H., Seemuller U.
    Submitted (MAR-1982) to the PIR data bank
    Cited for: SEQUENCE REVISION TO 33.
  3. "Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin."
    Bode W., Papamokos E., Musil D., Seemueller U., Fritz H.
    EMBO J. 5:813-818(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH SUBTILISIN.
  4. "Sequence-specific 1H NMR assignments and secondary structure of eglin c."
    Hyberts S.G., Wagner G.
    Biochemistry 29:1465-1474(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  5. "X-ray crystal structure of the serine proteinase inhibitor eglin c at 1.95-A resolution."
    Hipler K., Priestle J.P., Rahuel J., Gruetter M.G.
    FEBS Lett. 309:139-145(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
  6. "Structure of the proteinase inhibitor eglin c with hydrolysed reactive centre at 2.0-A resolution."
    Betzel C., Dauter Z., Genov N., Lamzin V., Navaza J., Schnebli H.P., Visanji M., Wilson K.S.
    FEBS Lett. 317:185-188(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  7. "Long-range electrostatic complementarity governs substrate recognition by human chymotrypsin C, a key regulator of digestive enzyme activation."
    Batra J., Szabo A., Caulfield T.R., Soares A.S., Sahin-Toth M., Radisky E.S.
    J. Biol. Chem. 288:9848-9859(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 4-70 IN COMPLEX WITH HUMAN CTRC.

Entry informationi

Entry nameiICIC_HIRME
AccessioniPrimary (citable) accession number: P01051
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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

External Data

Dasty 3

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 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.