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P07584 (ASTA_ASTAS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Astacin

EC=3.4.24.21
Alternative name(s):
Crayfish small molecule proteinase
OrganismAstacus astacus (Noble crayfish) (Astacus fluviatilis)
Taxonomic identifier6715 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAstacideaAstacoideaAstacidaeAstacus

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protease prefers to cleave in front of small aliphatic residues (P1'). The presence of Lys or Arg in the P1 and P2 position yields high-turnover substrates. In the P3 position the enzyme prefers Pro > Val > Leu > Ala > Gly.

Catalytic activity

Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'. Ref.3

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Monomer.

Sequence similarities

Belongs to the peptidase M12A family.

Ontologies

Keywords
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from sequence or structural similarity PubMed 22206759. Source: UniProtKB

fertilization

Inferred from sequence or structural similarity PubMed 22206759. Source: UniProtKB

negative regulation of binding of sperm to zona pellucida

Inferred from sequence or structural similarity PubMed 22472438. Source: UniProtKB

positive regulation of protein processing

Inferred from sequence or structural similarity PubMed 22472438. Source: UniProtKB

prevention of polyspermy

Inferred from sequence or structural similarity PubMed 22472438. Source: UniProtKB

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcortical granule

Inferred from sequence or structural similarity PubMed 22472438. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity PubMed 22206759. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity PubMed 22206759. Source: UniProtKB

   Molecular_functionaspartic-type peptidase activity

Inferred from sequence or structural similarity PubMed 22472438. Source: UniProtKB

glutamic-type peptidase activity

Inferred from sequence or structural similarity PubMed 22472438. Source: UniProtKB

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

peptidase activity

Inferred from sequence or structural similarity PubMed 22206759. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Propeptide16 – 4934Activation peptide
PRO_0000028872
Chain50 – 249200Astacin Ref.6
PRO_0000028873
Propeptide250 – 2512
PRO_0000028874

Sites

Active site1421
Metal binding1411Zinc; catalytic Ref.5
Metal binding1451Zinc; catalytic Ref.5
Metal binding1511Zinc; catalytic Ref.5

Amino acid modifications

Disulfide bond91 ↔ 247 Ref.2
Disulfide bond113 ↔ 133 Ref.2

Secondary structure

.................................................. 251
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07584 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 00E76C704334343B

FASTA25128,093
        10         20         30         40         50         60 
MQCAVLLVLL GVVAASPIIP EAARALYYND GMFEGDIKLR AGRQPARVGA AILGDEYLWS 

        70         80         90        100        110        120 
GGVIPYTFAG VSGADQSAIL SGMQELEEKT CIRFVPRTTE SDYVEIFTSG SGCWSYVGRI 

       130        140        150        160        170        180 
SGAQQVSLQA NGCVYHGTII HELMHAIGFY HEHTRMDRDN YVTINYQNVD PSMTSNFDID 

       190        200        210        220        230        240 
TYSRYVGEDY QYYSIMHYGK YSFSIQWGVL ETIVPLQNGI DLTDPYDKAH MLQTDANQIN 

       250 
NLYTNECSLR H 

« Hide

References

[1]"Genomic organization of the zinc-endopeptidase astacin."
Geier G., Jacob E., Stoecker W., Zwilling R.
Arch. Biochem. Biophys. 337:300-307(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Amino acid sequence of a unique protease from the crayfish Astacus fluviatilis."
Titani K., Torff H.-J., Hormel S., Kumar S., Walsh K.A., Rodl J., Neurath H., Zwilling R.
Biochemistry 26:222-226(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 50-249.
[3]"Astacus protease, a zinc metalloenzyme."
Stoecker W., Wolz R.L., Zwilling R., Strydom D.J., Auld D.S.
Biochemistry 27:5026-5032(1988)
Cited for: ZINC-BINDING, ENZYME ACTIVITY.
[4]"Fluorescent oligopeptide substrates for kinetic characterization of the specificity of Astacus protease."
Stoecker W., Ng M., Auld D.S.
Biochemistry 29:10418-10425(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE SPECIFICITY.
[5]"Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases."
Bode W., Gomis-Rueth F.-X., Huber R., Zwilling R., Stoecker W.
Nature 358:164-167(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[6]"Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin."
Gomis-Rueth F.-X., Stoecker W., Huber R., Zwilling R., Bode W.
J. Mol. Biol. 229:945-968(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[7]"Structure of astacin with a transition-state analogue inhibitor."
Grams F., Dive V., Yiotakis A., Yiallouros I., Vassiliou S., Zwilling R., Bode W., Stoecker W.
Nat. Struct. Biol. 3:671-675(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 50-249.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X95684 Genomic DNA. Translation: CAA64981.1.
PIRHYCY. A58830.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ASTX-ray1.80A50-249[»]
1IAAX-ray1.90A50-249[»]
1IABX-ray1.79A50-249[»]
1IACX-ray2.10A50-249[»]
1IADX-ray2.30A50-249[»]
1IAEX-ray1.83A50-249[»]
1QJIX-ray2.14A50-249[»]
1QJJX-ray1.86A50-249[»]
3LQ0X-ray1.45A16-250[»]
ProteinModelPortalP07584.
SMRP07584. Positions 50-249.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP07584.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]
PfamPF01400. Astacin. 1 hit.
[Graphical view]
PRINTSPR00480. ASTACIN.
SMARTSM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07584.

Entry information

Entry nameASTA_ASTAS
AccessionPrimary (citable) accession number: P07584
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references