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Protein

Hirudin variant-1

Gene
N/A
Organism
Hirudo medicinalis (Medicinal leech)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • serine-type endopeptidase inhibitor activity Source: CAFA

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionProtease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPS protease database

More...
MEROPSi
I14.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Hirudin variant-1
Alternative name(s):
Hirudin-1
Hirudin-I
INN: Lepirudin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHirudo medicinalis (Medicinal leech)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri6421 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudineaHirudinidaHirudiniformesHirudinidaeHirudo

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

Available under the name Refludan (Hoechst Marion Roussel). Used to treat heparin-induced thrombocytopenia (HIT).

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1V → E or K: Strongly decreased affinity for thrombin. 1 Publication1
Mutagenesisi1V → G or S: Decreased affinity for thrombin. 1 Publication1
Mutagenesisi1V → L or R: No effect. 1 Publication1
Mutagenesisi2V → E or G: Strongly decreased affinity for thrombin. 1 Publication1
Mutagenesisi2V → L: Decreased affinity for thrombin. 1 Publication1
Mutagenesisi3Y → A: Strongly decreased affinity for thrombin. 1 Publication1
Mutagenesisi4T → A: Decreased affinity for thrombin. 1 Publication1
Mutagenesisi5D → A or E: Decreased affinity for thrombin. 1 Publication1
Mutagenesisi15L → A: Strongly decreased affinity for thrombin. 1 Publication1
Mutagenesisi17E → A: Slightly decreased affinity for thrombin. 1
Mutagenesisi20N → A: Decreased affinity for thrombin. 1 Publication1
Mutagenesisi21V → A: Slightly decreased affinity for thrombin. 1 Publication1
Mutagenesisi56F → A or W: Slightly decreased affinity for thrombin. 1 Publication1
Mutagenesisi56F → I, L, T or V: Strongly decreased affinity for thrombin. 1 Publication1
Mutagenesisi56F → Y: No effect. 1 Publication1
Mutagenesisi60P → A or G: Decreased affinity for thrombin. 1 Publication1
Mutagenesisi63Y → A, E or L: Slightly decreased affinity for thrombin. 1 Publication1
Mutagenesisi63Y → F: No effect. 1 Publication1
Mutagenesisi63Y → V: Decreased affinity for thrombin. 1 Publication1

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
9843 Hir me Hirudin

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001956391 – 65Hirudin variant-1Add BLAST65

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi6 ↔ 14
Disulfide bondi16 ↔ 28
Disulfide bondi22 ↔ 39
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi45O-linked (GalNAc...) threonineBy similarity1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei63Sulfotyrosine2 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

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DisProti
DP00137

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P01050

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P01050

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P01050

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 3Interaction with thrombin active site3
Regioni55 – 65Interaction with fibrinogen-binding exosite of thrombinAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011061 Hirudin/antistatin
IPR000429 Prot_inh_hirudin

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00713 Hirudin, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001640 Hirudin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00777 HIRUDIN

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD004216 Prot_inh_hirudin, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57262 SSF57262, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P01050-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
VVYTDCTESG QNLCLCEGSN VCGQGNKCIL GSDGEKNQCV TGEGTPKPQS
60
HNDGDFEEIP EEYLQ
Length:65
Mass (Da):6,970
Last modified:July 21, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9085A5876E3DE9FF
GO

Sequence databases

Protein sequence database of the Protein Information Resource

More...
PIRi
A91318 HULXH
S05672

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Refludan

Clinical information on Refludan

Sequence databases

PIRiA91318 HULXH
S05672

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AD8X-ray2.00I55-64[»]
1AE8X-ray2.00I55-64[»]
1AFEX-ray2.00I55-64[»]
1AHTX-ray1.60I55-64[»]
1AI8X-ray1.85I55-64[»]
1AWFX-ray2.20I55-64[»]
1AY6X-ray1.80I55-64[»]
1BA8X-ray1.80C53-64[»]
1BB0X-ray2.10C53-64[»]
1BCUX-ray2.00I54-65[»]
1CA8X-ray2.10C53-64[»]
1D3DX-ray2.04H54-65[»]
1D3PX-ray2.10H54-65[»]
1D3QX-ray2.90H54-65[»]
1D3TX-ray3.00H54-65[»]
1D4PX-ray2.07H54-65[»]
1H8DX-ray1.40I55-64[»]
1H8IX-ray1.75I55-64[»]
1HICNMR-A1-51[»]
1HRTX-ray2.80I1-65[»]
1HXEX-ray2.10I55-64[»]
1HXFX-ray2.10I55-64[»]
1NO9X-ray1.90I55-65[»]
1QHRX-ray2.20I55-64[»]
1QJ1X-ray2.00I55-64[»]
1QJ6X-ray2.20I55-64[»]
1QJ7X-ray2.20I55-64[»]
1TMTX-ray2.20I53-65[»]
1TMUX-ray2.50I55-65[»]
1UMAX-ray2.00I55-64[»]
1WBGX-ray2.20I55-64[»]
2HIRNMR-A1-65[»]
2JOONMR-A1-65[»]
2PW8X-ray1.84I3-65[»]
2UUFX-ray1.26H55-64[»]
2UUJX-ray1.32H55-64[»]
2UUKX-ray1.39H55-64[»]
2V3OX-ray1.79I56-65[»]
2ZC9X-ray1.58I54-64[»]
2ZDAX-ray1.73I54-64[»]
2ZDVX-ray1.72I54-64[»]
2ZF0X-ray2.20I54-64[»]
2ZFFX-ray1.47I54-64[»]
2ZFPX-ray2.25I54-64[»]
2ZGBX-ray1.60I54-64[»]
2ZGXX-ray1.80I54-64[»]
2ZHQX-ray1.96I54-64[»]
2ZI2X-ray1.65I54-64[»]
2ZIQX-ray1.65I54-64[»]
2ZNKX-ray1.80I54-64[»]
2ZO3X-ray1.70I54-64[»]
3D49X-ray1.50I54-64[»]
3DHKX-ray1.73I54-64[»]
3DT0X-ray2.40I54-64[»]
3DUXX-ray1.60I54-64[»]
3EGKX-ray2.20I54-64[»]
3EQ0X-ray1.53I54-64[»]
3LDXX-ray2.25I55-65[»]
3UTUX-ray1.55I54-64[»]
4AX9X-ray1.90I55-65[»]
4BAHX-ray1.94D53-64[»]
4BAKX-ray1.94D53-64[»]
4BAMX-ray1.88D53-64[»]
4BANX-ray1.87D53-64[»]
4BAQX-ray1.89D53-64[»]
4HIRNMR-A1-65[»]
4LXBX-ray1.61I53-65[»]
4MLFX-ray2.20D1-65[»]
4YESX-ray1.50H54-65[»]
5HIRNMR-A1-65[»]
6HIRNMR-A1-65[»]
DisProtiDP00137
ProteinModelPortaliP01050
SMRiP01050
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei9843 Hir me Hirudin
MEROPSiI14.001

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP01050

Family and domain databases

InterProiView protein in InterPro
IPR011061 Hirudin/antistatin
IPR000429 Prot_inh_hirudin
PfamiView protein in Pfam
PF00713 Hirudin, 1 hit
PIRSFiPIRSF001640 Hirudin, 1 hit
PRINTSiPR00777 HIRUDIN
ProDomiView protein in ProDom or Entries sharing at least one domain
PD004216 Prot_inh_hirudin, 1 hit
SUPFAMiSSF57262 SSF57262, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHIRV1_HIRME
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P01050
Secondary accession number(s): P28501
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 12, 2018
This is version 124 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Pharmaceutical

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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