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Reviewed, UniProtKB/Swiss-Prot P09944 (HIRPA_HIRME)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Hirudin-PA
OrganismHirudo medicinalis (Medicinal leech)
Taxonomic identifier6421 [NCBI]
Taxonomic lineageEukaryotaMetazoaAnnelidaClitellataHirudinidaHirudineaArhynchobdellidaHirudiniformesHirudinidaeHirudo

Protein attributes

Sequence length66 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
Glycoprotein
Sulfation
   Technical termDirect protein sequencing
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

Chain1 – 6666Hirudin-PA
PRO_0000195640

Regions

Region1 – 33Interaction with thrombin active site By similarity
Region55 – 6612Interaction with fibrinogen-binding exosite of thrombin By similarity

Amino acid modifications

Modified residue641Sulfotyrosine
Glycosylation451O-linked (GalNAc...) By similarity
Disulfide bond6 ↔ 14 By similarity
Disulfide bond16 ↔ 28 By similarity
Disulfide bond22 ↔ 39 By similarity

Sequences

Sequence LengthMass (Da)Tools
P09944-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: FA1B80B7F4FEA317

FASTA667,026
        10         20         30         40         50         60 
ITYTDCTESG QNLCLCEGSN VCGKGNKCIL GSQGKDNQCV TGEGTPKPQS HNQGDFEPIP 


EDAYDE 

« Hide

References

[1]"Isolation and characterization of hirudin isoinhibitors and sequence analysis of hirudin PA."
Dodt J., Machleidt W., Seemueller U., Maschler R., Fritz H.
Biol. Chem. Hoppe-Seyler 367:803-811(1986) [PubMed: 3768144] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRA24350.

3D structure databases

SMRP09944. Positions 1-62.
ModBaseSearch...

Protein family/group databases

MEROPSI14.001.

Family and domain databases

InterProIPR000429. Prot_inh_hirudin.
[Graphical view]
Gene3DG3DSA:2.70.10.10. Prot_inh_hirudin. 1 hit.
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]
ProtoNetSearch...

Entry information

Entry nameHIRPA_HIRME
AccessionPrimary (citable) accession number: P09944
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 16, 2009
This is version 61 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents