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P09945 (HIRV2_HIRME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. Feed History...

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

Names and origin

Protein namesRecommended name:
Hirudin variant-2
OrganismHirudo medicinalis (Medicinal leech)
Taxonomic identifier6421 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Lophotrochozoa › Annelida › Clitellata › Hirudinida › Hirudinea › Arhynchobdellida › Hirudiniformes › Hirudinidae › Hirudo

Protein attributes

Sequence length72 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hirudin is a potent thrombin-specific protease inhibitor. It forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen.

Subcellular location

Secreted.

Sequence similarities

Belongs to the protease inhibitor I14 (hirudin) family. [View classification]

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
Glycoprotein
Sulfation
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 7›7
Chain8 – 7265Hirudin variant-2
PRO_0000013441

Regions

Region8 – 103Interaction with thrombin active site
Region62 – 7211Interaction with fibrinogen-binding exosite of thrombin

Amino acid modifications

Modified residue701Sulfotyrosine
Glycosylation521O-linked (GalNAc...) By similarity
Disulfide bond13 ↔ 21 Ref.2
Disulfide bond23 ↔ 35 Ref.2
Disulfide bond29 ↔ 46 Ref.2

Experimental info

Non-terminal residue11

Secondary structure

1 ........... 72
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09945 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: C6EF2F28E9C45A5B

FASTA727,571
        10         20         30         40         50         60 
AICVSQAITY TDCTESGQNL CLCEGSNVCG KGNKCILGSN GKGNQCVTGE GTPNPESHNN 

        70 
GDFEEIPEEY LQ

« Hide

References

[1]"Cloning and expression of a cDNA coding for the anticoagulant hirudin from the bloodsucking leech, Hirudo medicinalis."
Harvey R.P., Degryse E., Stefani L., Schamber F., Cazenave J.-P., Courtney M., Tolstoshev P., Lecocq J.-P.
Proc. Natl. Acad. Sci. U.S.A. 83:1084-1088(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The structure of a complex of recombinant hirudin and human alpha-thrombin."
Rydel T.J., Ravichandran K.G., Tulinsky A., Bode W., Huber R., Roitsch C., Fenton J.W. II
Science 249:277-280(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 8-72 OF MUTANT LYS-54 IN COMPLEX WITH THROMBIN, DISULFIDE BONDS.
[3]"Refined structure of the hirudin-thrombin complex."
Rydel T.J., Tulinsky A., Bode W., Huber R.
J. Mol. Biol. 221:583-601(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 8-72 IN COMPLEX WITH THROMBIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M12693 mRNA. Translation: AAA29195.1.
PIRA37417.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2CX-ray2.10I60-71[»]
1A46X-ray2.12I60-71[»]
1A5GX-ray2.06I60-71[»]
1A61X-ray2.20I60-71[»]
1B5GX-ray2.07I60-71[»]
1DOJX-ray1.70B62-72[»]
1K21X-ray1.86I60-71[»]
1K22X-ray1.93I60-71[»]
1NRSX-ray2.40I60-71[»]
1VZQX-ray1.54I62-72[»]
1W7GX-ray1.65I62-71[»]
1WAYX-ray2.02I62-71[»]
2C8WX-ray1.96I61-72[»]
2C8XX-ray2.17I61-72[»]
2C8YX-ray2.20I61-72[»]
2C8ZX-ray2.14I61-72[»]
2C90X-ray2.25I61-72[»]
2C93X-ray2.20I61-72[»]
2R2MX-ray2.10H62-72[»]
2ZFQX-ray1.80I60-71[»]
2ZFRX-ray1.85I60-71[»]
2ZG0X-ray1.75I60-71[»]
2ZHEX-ray2.10I60-71[»]
2ZHFX-ray1.98I60-71[»]
2ZHWX-ray2.02I60-71[»]
3BIUX-ray2.30I60-71[»]
3BIVX-ray1.80I60-71[»]
3F68X-ray1.75I61-71[»]
3HTCX-ray2.30I8-72[»]
3P17X-ray1.43I60-71[»]
3QTOX-ray1.52I60-72[»]
3QTVX-ray1.63I60-72[»]
3QWCX-ray1.75I60-72[»]
3QX5X-ray1.35I60-72[»]
3RLWX-ray1.69I60-72[»]
3RLYX-ray1.51I60-72[»]
3RM0X-ray1.34I60-72[»]
3RM2X-ray1.23I60-72[»]
3RMLX-ray1.53I60-72[»]
3RMMX-ray1.58I60-72[»]
3RMNX-ray1.78I60-72[»]
3RMOX-ray1.40I60-72[»]
3SHAX-ray1.52I60-72[»]
3SHCX-ray1.90I60-72[»]
3SI3X-ray1.55I60-72[»]
3SI4X-ray1.27I60-72[»]
3SV2X-ray1.30I60-72[»]
3T5FX-ray1.45I60-72[»]
3TU7X-ray2.49I61-72[»]
3U98X-ray1.45I60-72[»]
3U9AX-ray1.58I60-72[»]
3UWJX-ray1.50I60-72[»]
4BAOX-ray1.87D62-71[»]
4E7RX-ray2.25I/J62-72[»]
4HTCX-ray2.30I8-72[»]
ProteinModelPortalP09945.
SMRP09945. Positions 8-72.
ModBaseSearch...

Protein family/group databases

Allergome9843. Hir me Hirudin.
MEROPSI14.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.70.10.10. 1 hit.
InterProIPR024793. Hirudin.
IPR000429. Prot_inh_hirudin.
IPR011061. Prot_inh_I14/15_hirudin/antisn.
[Graphical view]
PfamPF00713. Hirudin. 1 hit.
[Graphical view]
PIRSFPIRSF001640. Hirudin. 1 hit.
PRINTSPR00777. HIRUDIN.
ProDomPD004216. Prot_inh_hirudin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF57262. Antihaemostatic. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP09945.

Entry information

Entry nameHIRV2_HIRME
AccessionPrimary (citable) accession number: P09945
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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