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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-Experimental evidence at protein leveli

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI14.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Hirudin variant-1
Alternative name(s):
Hirudin-1
Hirudin-I
Lepirudin
OrganismiHirudo medicinalis (Medicinal leech)
Taxonomic identifieri6421 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaArhynchobdellidaHirudiniformesHirudinidaeHirudo

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Allergomei9843. Hir me Hirudin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001956391 – 65Hirudin variant-1Add BLAST65

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi6 ↔ 14
Disulfide bondi16 ↔ 28
Disulfide bondi22 ↔ 39
Glycosylationi45O-linked (GalNAc...)By similarity1
Modified residuei63Sulfotyrosine2 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Structurei

Secondary structure

165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 15Combined sources5
Beta strandi17 – 19Combined sources3
Beta strandi20 – 22Combined sources3
Beta strandi26 – 29Combined sources4
Beta strandi32 – 34Combined sources3
Beta strandi38 – 42Combined sources5
Helixi61 – 63Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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...

Miscellaneous databases

EvolutionaryTraceiP01050.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 3Interaction with thrombin active site3
Regioni55 – 65Interaction with fibrinogen-binding exosite of thrombinAdd BLAST11

Sequence similaritiesi

Family and domain databases

Gene3Di2.70.10.10. 1 hit.
InterProiIPR024793. Hirudin.
IPR011061. Hirudin/antistatin.
IPR000429. Prot_inh_hirudin.
[Graphical view]
PfamiPF00713. Hirudin. 1 hit.
[Graphical view]
PIRSFiPIRSF001640. Hirudin. 1 hit.
PRINTSiPR00777. HIRUDIN.
ProDomiPD004216. Prot_inh_hirudin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57262. SSF57262. 1 hit.

Sequencei

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
Checksum:i9085A5876E3DE9FF
GO

Sequence databases

PIRiA91318. HULXH.
S05672.

Cross-referencesi

Web resourcesi

Refludan

Clinical information on Refludan

Sequence databases

PIRiA91318. HULXH.
S05672.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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

Gene3Di2.70.10.10. 1 hit.
InterProiIPR024793. Hirudin.
IPR011061. Hirudin/antistatin.
IPR000429. Prot_inh_hirudin.
[Graphical view]
PfamiPF00713. Hirudin. 1 hit.
[Graphical view]
PIRSFiPIRSF001640. Hirudin. 1 hit.
PRINTSiPR00777. HIRUDIN.
ProDomiPD004216. Prot_inh_hirudin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57262. SSF57262. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHIRV1_HIRME
AccessioniPrimary (citable) accession number: P01050
Secondary accession number(s): P28501
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 120 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, Pharmaceutical

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.