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Protein

Hirustasin

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 tissue kallikrein, trypsin, chymotrypsin and neutrophil cathepsin G.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei30 – 312Reactive bond

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Ligandi

Heparin-binding

Protein family/group databases

MEROPSiI15.001.

Names & Taxonomyi

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5555HirustasinPRO_0000155194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 171 Publication
Disulfide bondi11 ↔ 221 Publication
Disulfide bondi24 ↔ 441 Publication
Disulfide bondi29 ↔ 481 Publication
Disulfide bondi33 ↔ 501 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
55
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Beta strandi15 – 184Combined sources
Beta strandi21 – 244Combined sources
Beta strandi27 – 304Combined sources
Beta strandi37 – 393Combined sources
Beta strandi45 – 506Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BX7X-ray1.20A1-55[»]
1BX8X-ray1.40A1-55[»]
1HIAX-ray2.40I/J5-52[»]
ProteinModelPortaliP80302.
SMRiP80302. Positions 3-53.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80302.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 5027Antistasin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 antistasin-like domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.10.22.10. 1 hit.
InterProiIPR004094. Antistasin-like.
IPR011061. Hirudin/antistatin.
IPR008086. Prot_inh_I15_antistasin_leech.
[Graphical view]
PfamiPF02822. Antistasin. 1 hit.
[Graphical view]
PRINTSiPR01706. ANTISTASIN.
SUPFAMiSSF57262. SSF57262. 1 hit.
PROSITEiPS51252. ANTISTASIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80302-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
TQGNTCGGET CSAAQVCLKG KCVCNEVHCR IRCKYGLKKD ENGCEYPCSC

AKASQ
Length:55
Mass (Da):5,878
Last modified:February 1, 1994 - v1
Checksum:i234226BEE3CC532E
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BX7X-ray1.20A1-55[»]
1BX8X-ray1.40A1-55[»]
1HIAX-ray2.40I/J5-52[»]
ProteinModelPortaliP80302.
SMRiP80302. Positions 3-53.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI15.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP80302.

Family and domain databases

Gene3Di2.10.22.10. 1 hit.
InterProiIPR004094. Antistasin-like.
IPR011061. Hirudin/antistatin.
IPR008086. Prot_inh_I15_antistasin_leech.
[Graphical view]
PfamiPF02822. Antistasin. 1 hit.
[Graphical view]
PRINTSiPR01706. ANTISTASIN.
SUPFAMiSSF57262. SSF57262. 1 hit.
PROSITEiPS51252. ANTISTASIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and characterization of hirustasin, an antistasin-type serine-proteinase inhibitor from the medical leech Hirudo medicinalis."
    Soellner C., Mentele R., Eckerskorn C., Fritz H., Sommerhoff C.P.
    Eur. J. Biochem. 219:937-943(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex."
    Mittl P.R.E., di Marco S., Fendrich G., Pohlig G., Heim J., Sommerhoff C., Fritz H., Priestle J.P., Gruetter M.G.
    Structure 5:253-264(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH KALLIKREIN.
  3. "The 1.2 A crystal structure of hirustasin reveals the intrinsic flexibility of a family of highly disulphide-bridged inhibitors."
    Uson I., Sheldrick G.M., de La Fortelle E., Bricogne G., Di Marco S., Priestle J.P., Gruetter M.G., Mittl P.R.
    Structure 7:55-63(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), DISULFIDE BONDS.

Entry informationi

Entry nameiANTA_HIRME
AccessioniPrimary (citable) accession number: P80302
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: December 9, 2015
This is version 84 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.