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Protein

Hirudin variant-2

Gene
N/A
Organism
Hirudo medicinalis (Medicinal leech)
Status
Reviewed-Annotation score: Annotation score: 3 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.

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW
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-2
OrganismiHirudo medicinalis (Medicinal leech)
Taxonomic identifieri6421 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaArhynchobdellidaHirudiniformesHirudinidaeHirudo

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei9843. Hir me Hirudin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 7›7
Chaini8 – 7265Hirudin variant-2PRO_0000013441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi13 ↔ 211 Publication
Disulfide bondi23 ↔ 351 Publication
Disulfide bondi29 ↔ 461 Publication
Glycosylationi52 – 521O-linked (GalNAc...)By similarity
Modified residuei70 – 701Sulfotyrosine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Structurei

Secondary structure

1
72
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 225Combined sources
Beta strandi24 – 263Combined sources
Beta strandi33 – 364Combined sources
Beta strandi45 – 495Combined sources
Helixi68 – 703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2CX-ray2.10I60-71[»]
1A46X-ray2.12I60-71[»]
1A4WX-ray1.80I60-71[»]
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[»]
1TMBX-ray2.30I60-71[»]
1TMUX-ray2.50J62-72[»]
1VZQX-ray1.54I62-72[»]
1W7GX-ray1.65I60-71[»]
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[»]
3HATX-ray2.50I60-71[»]
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[»]
4LOYX-ray1.77I62-71[»]
4N3LX-ray1.94I60-71[»]
4NZEX-ray1.98I60-71[»]
ProteinModelPortaliP09945.
SMRiP09945. Positions 8-72.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09945.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 103Interaction with thrombin active site
Regioni62 – 7211Interaction with fibrinogen-binding exosite of thrombinAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

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: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09945-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AICVSQAITY TDCTESGQNL CLCEGSNVCG KGNKCILGSN GKGNQCVTGE
60 70
GTPNPESHNN GDFEEIPEEY LQ
Length:72
Mass (Da):7,571
Last modified:July 1, 1989 - v1
Checksum:iC6EF2F28E9C45A5B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12693 mRNA. Translation: AAA29195.1.
PIRiA37417.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12693 mRNA. Translation: AAA29195.1.
PIRiA37417.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2CX-ray2.10I60-71[»]
1A46X-ray2.12I60-71[»]
1A4WX-ray1.80I60-71[»]
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[»]
1TMBX-ray2.30I60-71[»]
1TMUX-ray2.50J62-72[»]
1VZQX-ray1.54I62-72[»]
1W7GX-ray1.65I60-71[»]
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[»]
3HATX-ray2.50I60-71[»]
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[»]
4LOYX-ray1.77I62-71[»]
4N3LX-ray1.94I60-71[»]
4NZEX-ray1.98I60-71[»]
ProteinModelPortaliP09945.
SMRiP09945. Positions 8-72.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei9843. Hir me Hirudin.
MEROPSiI14.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP09945.

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...

Publicationsi

  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], SULFATION AT TYR-70.
  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.

Entry informationi

Entry nameiHIRV2_HIRME
AccessioniPrimary (citable) accession number: P09945
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 7, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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

External Data

Dasty 3

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 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.