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Protein

Hementerin

Gene
N/A
Organism
Haementeria depressa (Leech)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves fibrinogen Aalpha (FGA), gamma (FGG) and Bbeta (FGB) chains. Degrades cross-linked fibrin. Has no amidolytic, plasminogenolytic or caseinolytic activity. Inhibits platelet aggregation induced by collagen (IC50=7.5ug/ml) and various other agonists, presumably via activation of a nitridergic pathway. Inhibition is accompanied by reduced ATP release from and surface expression of SELP and CD63 on platelets as well as increased intracellular levels of Ca2+, cGMP and nitric oxide synthase activity.2 Publications

Cofactori

Ca2+1 Publication

Enzyme regulationi

Fibrino(geno)lytic activity inhibited by EDTA but not by PMSF, E-64, 6-AHA and aprotinin.1 Publication

GO - Molecular functioni

  1. metallopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. blood coagulation Source: UniProtKB-KW
  2. fibrinolysis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Hementerin1 Publication (EC:3.4.-.-)
OrganismiHaementeria depressa (Leech)
Taxonomic identifieri279730 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaRhynchobdellidaGlossiphoniidaeHaementeria

Subcellular locationi

Secreted Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›30›30HementerinPRO_0000397938Add
BLAST

Sequencei

Sequence statusi: Fragments.

P86682-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30
XTLSEPEPTC SIEYFRYQAI EDCEYSISVK
Length:30
Mass (Da):3,513
Last modified:October 5, 2010 - v1
Checksum:i5A492FA070690DD1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi9 – 1021 Publication
Non-adjacent residuesi16 – 1721 Publication
Non-terminal residuei30 – 3011 Publication

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Fibrino(geno)lytic properties of purified hementerin, a metalloproteinase from the leech Haementeria depressa."
    Chudzinski-Tavassi A.M., Kelen E.M., de Paula Rosa A.P., Loyau S., Sampaio C.A., Bon C., Angles-Cano E.
    Thromb. Haemost. 80:155-160(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, COFACTOR, ENZYME REGULATION.
    Tissue: Salivary gland1 Publication.
  2. "Nitridergic platelet pathway activation by hementerin, a metalloprotease from the leech Haementeria depressa."
    Chudzinski-Tavassi A.M., Bermej E., Rosenstein R.E., Faria F., Sarmiento M.I., Alberto F., Sampaio M.U., Lazzari M.A.
    Biol. Chem. 384:1333-1339(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiHETN_HAEDE
AccessioniPrimary (citable) accession number: P86682
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 5, 2010
Last modified: January 7, 2015
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Caution

The order of the peptides shown is unknown.1 Publication

Keywords - Technical termi

Direct protein sequencing

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.