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P01051 (ICIC_HIRME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eglin C
OrganismHirudo medicinalis (Medicinal leech)
Taxonomic identifier6421 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaArhynchobdellidaHirudiniformesHirudinidaeHirudo

Protein attributes

Sequence length70 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits both elastase and cathepsin G.

Sequence similarities

Belongs to the protease inhibitor I13 (potato type I serine protease inhibitor) family. [View classification]

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7070Eglin C
PRO_0000217645

Sites

Site45 – 462Reactive bond

Secondary structure

............. 70
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01051 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 7E5C5BBD39DC3C11

FASTA708,091
        10         20         30         40         50         60 
TEFGSELKSF PEVVGKTVDQ AREYFTLHYP QYDVYFLPEG SPVTLDLRYN RVRVFYNPGT 

        70 
NVVNHVPHVG 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIREILXCH. A94592.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP01051.
SMRP01051. Positions 1-70.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6069N.
MINTMINT-1345724.

Protein family/group databases

MEROPSI13.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000864. Prot_inh_pot1.
[Graphical view]
PfamPF00280. potato_inhibit. 1 hit.
[Graphical view]
PRINTSPR00292. POTATOINHBTR.
ProDomPD002604. Prot_inh_pot1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF54654. SSF54654. 1 hit.
PROSITEPS00285. POTATO_INHIBITOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01051.

Entry information

Entry nameICIC_HIRME
AccessionPrimary (citable) accession number: P01051
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references