Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Leech-derived tryptase inhibitor C

Gene
N/A
Organism
Hirudo medicinalis (Medicinal leech)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Acts as an inhibitor of human tryptase, trypsin and chymotrypsin. Probably acts to block host defense mechanisms.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei8 – 92Reactive bond (tryptase)

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI01.021.

Names & Taxonomyi

Protein namesi
Recommended name:
Leech-derived tryptase inhibitor C
Short name:
LDTI-C
Cleaved into the following 2 chains:
OrganismiHirudo medicinalis (Medicinal leech)
Taxonomic identifieri6421 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaArhynchobdellidaHirudiniformesHirudinidaeHirudo

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4646Leech-derived tryptase inhibitor CPRO_0000045882Add
BLAST
Chaini1 – 4343Leech-derived tryptase inhibitor BPRO_0000045883Add
BLAST
Chaini1 – 4242Leech-derived tryptase inhibitor APRO_0000045884Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 29
Disulfide bondi6 ↔ 25
Disulfide bondi14 ↔ 40

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

DIPiDIP-6084N.
MINTiMINT-1526663.

Structurei

Secondary structure

1
46
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi13 – 153Combined sources
Beta strandi20 – 234Combined sources
Helixi24 – 307Combined sources
Beta strandi36 – 383Combined sources
Beta strandi41 – 433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AN1X-ray2.03I1-46[»]
1LDTX-ray1.90L1-46[»]
2KMONMR-A1-44[»]
2KMPNMR-A1-44[»]
2KMQNMR-A1-44[»]
2KMRNMR-A1-44[»]
ProteinModelPortaliP80424.
SMRiP80424. Positions 1-46.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80424.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4242Kazal-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Kazal-like domain.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR002350. Kazal_dom.
[Graphical view]
PfamiPF00050. Kazal_1. 1 hit.
[Graphical view]
SMARTiSM00280. KAZAL. 1 hit.
[Graphical view]
PROSITEiPS00282. KAZAL_1. 1 hit.
PS51465. KAZAL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P80424-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
KKVCACPKIL KPVCGSDGRT YANSCIARCN GVSIKSEGSC PTGILN
Length:46
Mass (Da):4,744
Last modified:February 1, 1995 - v1
Checksum:i9FC4383FF5C009A1
GO

Sequence databases

PIRiS50015.

Cross-referencesi

Sequence databases

PIRiS50015.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AN1X-ray2.03I1-46[»]
1LDTX-ray1.90L1-46[»]
2KMONMR-A1-44[»]
2KMPNMR-A1-44[»]
2KMQNMR-A1-44[»]
2KMRNMR-A1-44[»]
ProteinModelPortaliP80424.
SMRiP80424. Positions 1-46.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6084N.
MINTiMINT-1526663.

Protein family/group databases

MEROPSiI01.021.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP80424.

Family and domain databases

InterProiIPR002350. Kazal_dom.
[Graphical view]
PfamiPF00050. Kazal_1. 1 hit.
[Graphical view]
SMARTiSM00280. KAZAL. 1 hit.
[Graphical view]
PROSITEiPS00282. KAZAL_1. 1 hit.
PS51465. KAZAL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A Kazal-type inhibitor of human mast cell tryptase: isolation from the medical leech Hirudo medicinalis, characterization, and sequence analysis."
    Sommerhoff C.P., Soellner C., Mentele R., Piechottka G.P., Auerswald E.A., Fritz H.
    Biol. Chem. Hoppe-Seyler 375:685-694(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. Cited for: STRUCTURE BY NMR.
  3. "The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition."
    Stubbs M.T., Morenweiser R., Stuerzebecher J., Bauer M., Bode W., Huber R., Piechottka G.P., Matschiner G., Sommerhoff C.P., Fritz H., Auerswald E.A.
    J. Biol. Chem. 272:19931-19937(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH TRYPSIN.
  4. "Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LDTI-tryptase system."
    di Marco S., Priestle J.P.
    Structure 5:1465-1474(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF COMPLEX WITH TRYPSIN.

Entry informationi

Entry nameiLDTI_HIRME
AccessioniPrimary (citable) accession number: P80424
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
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

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.