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UniProtKB/Swiss-Prot entry P07584


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ASTA_ASTFL
Primary accession number P07584
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 78)
Name and origin of the protein
Protein name Astacin [Precursor]
Synonyms EC 3.4.24.21
Crayfish small molecule proteinase
Gene name None
From
Astacus fluviatilis (Broad-fingered crayfish) (Astacus astacus) [TaxID: 6715] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Crustacea; Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea; Astacoidea; Astacidae; Astacus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/abbi.1996.9759; PubMed=9016826 [NCBI, ExPASy, EBI, Israel, Japan]
Geier G., Jacob E., Stoecker W., Zwilling R.;
"Genomic organization of the zinc-endopeptidase astacin.";
Arch. Biochem. Biophys. 337:300-307(1997).
[2]
PROTEIN SEQUENCE OF 50-249.
DOI=10.1021/bi00375a029; PubMed=3548817 [NCBI, ExPASy, EBI, Israel, Japan]
Titani K., Torff H.-J., Hormel S., Kumar S., Walsh K.A., Rodl J., Neurath H., Zwilling R.;
"Amino acid sequence of a unique protease from the crayfish Astacus fluviatilis.";
Biochemistry 26:222-226(1987).
[3]
ZINC-BINDING, AND ENZYME ACTIVITY.
Stoecker W., Wolz R.L., Zwilling R., Strydom D.J., Auld D.S.;
"Astacus protease, a zinc metalloenzyme.";
Biochemistry 27:5026-5032(1988).
[4]
SUBSTRATE SPECIFICITY.
DOI=10.1021/bi00497a018; PubMed=2261483 [NCBI, ExPASy, EBI, Israel, Japan]
Stoecker W., Ng M., Auld D.S.;
"Fluorescent oligopeptide substrates for kinetic characterization of the specificity of Astacus protease.";
Biochemistry 29:10418-10425(1990).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1038/358164a0; PubMed=1319561 [NCBI, ExPASy, EBI, Israel, Japan]
Bode W., Gomis-Rueth F.-X., Huber R., Zwilling R., Stoecker W.;
"Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases.";
Nature 358:164-167(1992).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1006/jmbi.1993.1098; PubMed=8445658 [NCBI, ExPASy, EBI, Israel, Japan]
Gomis-Rueth F.-X., Stoecker W., Huber R., Zwilling R., Bode W.;
"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.";
J. Mol. Biol. 229:945-968(1993).
[7]
X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 50-249.
DOI=10.1038/nsb0896-671; PubMed=8756323 [NCBI, ExPASy, EBI, Israel, Japan]
Grams F., Dive V., Yiotakis A., Yiallouros I., Vassiliou S., Zwilling R., Bode W., Stoecker W.;
"Structure of astacin with a transition-state analogue inhibitor.";
Nat. Struct. Biol. 3:671-675(1996).
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'.
  • COFACTOR: Binds 1 zinc ion per subunit.
  • SUBUNIT: Monomer.
  • SIMILARITY: Belongs to the peptidase M12A family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X95684; CAA64981.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A58830; HYCY.
3D structure databases
PDB
1AST; X-ray; 1.80 A; A=50-249.[ExPASy / RCSB / EBI]
1IAA; X-ray; 1.90 A; A=50-249.[ExPASy / RCSB / EBI]
1IAB; X-ray; 1.79 A; A=50-249.[ExPASy / RCSB / EBI]
1IAC; X-ray; 2.10 A; A=50-249.[ExPASy / RCSB / EBI]
1IAD; X-ray; 2.30 A; A=50-249.[ExPASy / RCSB / EBI]
1IAE; X-ray; 1.83 A; A=50-249.[ExPASy / RCSB / EBI]
1QJI; X-ray; 2.14 A; A=50-249.[ExPASy / RCSB / EBI]
1QJJ; X-ray; 1.86 A; A=50-249.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AST; -.
1IAA; -.
1IAB; -.
1IAC; -.
1IAD; -.
1IAE; -.
1QJI; -.
1QJJ; -.
ModBase P07584.
Protein family/group databases
MEROPS M12.001; -.
Ontologies
GO
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR001506; Peptidase_M12A.
Graphical view of domain structure.
Pfam PF01400; Astacin; 1.
Pfam graphical view of domain structure.
PRINTS PR00480; ASTACIN.
SMART SM00235; ZnMc; 1.
SMART graphical view of domain structure.
PROSITE PS00142; ZINC_PROTEASE; 1.
BLOCKS P07584.
ProtoNet P07584.
Other
LinkHub P07584; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Protease; Signal; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    15  15     Potential. 
PROPEP   16    49  34     Activation peptide. PRO_0000028872
CHAIN   50   249  200     Astacin. PRO_0000028873
PROPEP   250   251  2      PRO_0000028874
ACT_SITE   142   142         
METAL   141   141        Zinc; catalytic. 
METAL   145   145        Zinc; catalytic. 
METAL   151   151        Zinc; catalytic. 
DISULFID   91   247         
DISULFID   113   133         
STRAND   51    53  3      
HELIX   55    57  3      
HELIX   60    62  3      
STRAND   63    70  8      
HELIX   73    89  17      
STRAND   93    96  4      
STRAND   101   115  15      
STRAND   121   128  8      
TURN   130   133  4      
HELIX   136   147  12      
HELIX   152   154  3      
HELIX   158   160  3      
STRAND   162   164  3      
HELIX   166   168  3      
HELIX   171   177  7      
STRAND   181   184  4      
TURN   200   203  4      
STRAND   204   206  3      
TURN   207   209  3      
STRAND   212   217  6      
HELIX   225   227  3      
HELIX   233   242  10      
TURN   243   248  6      
Sequence information
Length: 251 AA [This is the length of the unprocessed precursor] Molecular weight: 28093 Da [This is the MW of the unprocessed precursor] CRC64: 00E76C704334343B [This is a checksum on the sequence]
        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 

P07584 in FASTA format

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View entry in raw text format (no links)
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