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P07584

- ASTA_ASTAS

UniProt

P07584 - ASTA_ASTAS

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Protein
Astacin
Gene
N/A
Organism
Astacus astacus (Noble crayfish) (Astacus fluviatilis)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.1 Publication

Cofactori

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi141 – 1411Zinc; catalytic1 Publication
Active sitei142 – 1421
Metal bindingi145 – 1451Zinc; catalytic1 Publication
Metal bindingi151 – 1511Zinc; catalytic1 Publication

GO - Molecular functioni

  1. aspartic-type peptidase activity Source: UniProtKB
  2. glutamic-type peptidase activity Source: UniProtKB
  3. metalloendopeptidase activity Source: InterPro
  4. peptidase activity Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB
  2. fertilization Source: UniProtKB
  3. negative regulation of binding of sperm to zona pellucida Source: UniProtKB
  4. positive regulation of protein processing Source: UniProtKB
  5. prevention of polyspermy Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKP07584.

Protein family/group databases

MEROPSiM12.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Astacin (EC:3.4.24.21)
Alternative name(s):
Crayfish small molecule proteinase
OrganismiAstacus astacus (Noble crayfish) (Astacus fluviatilis)
Taxonomic identifieri6715 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAstacideaAstacoideaAstacidaeAstacus

Subcellular locationi

GO - Cellular componenti

  1. cortical granule Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515 Reviewed prediction
Add
BLAST
Propeptidei16 – 4934Activation peptide
PRO_0000028872Add
BLAST
Chaini50 – 249200Astacin1 Publication
PRO_0000028873Add
BLAST
Propeptidei250 – 2512
PRO_0000028874

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 2471 Publication
Disulfide bondi113 ↔ 1331 Publication

Keywords - PTMi

Disulfide bond, Zymogen

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 277
Turni34 – 363
Beta strandi46 – 483
Beta strandi51 – 533
Helixi55 – 573
Helixi60 – 623
Beta strandi63 – 708
Helixi73 – 8917
Beta strandi93 – 964
Beta strandi101 – 11818
Beta strandi121 – 1288
Turni130 – 1334
Helixi136 – 14712
Helixi152 – 1543
Helixi158 – 1603
Beta strandi162 – 1643
Helixi166 – 1683
Helixi174 – 1774
Beta strandi181 – 1844
Turni200 – 2034
Turni205 – 2095
Beta strandi212 – 2176
Helixi225 – 2273
Helixi233 – 24210
Helixi244 – 2496

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP07584.
SMRiP07584. Positions 50-249.

Miscellaneous databases

EvolutionaryTraceiP07584.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M12A family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]
PfamiPF01400. Astacin. 1 hit.
[Graphical view]
PRINTSiPR00480. ASTACIN.
SMARTiSM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07584-1 [UniParc]FASTAAdd to Basket

« Hide

MQCAVLLVLL GVVAASPIIP EAARALYYND GMFEGDIKLR AGRQPARVGA    50
AILGDEYLWS GGVIPYTFAG VSGADQSAIL SGMQELEEKT CIRFVPRTTE 100
SDYVEIFTSG SGCWSYVGRI SGAQQVSLQA NGCVYHGTII HELMHAIGFY 150
HEHTRMDRDN YVTINYQNVD PSMTSNFDID TYSRYVGEDY QYYSIMHYGK 200
YSFSIQWGVL ETIVPLQNGI DLTDPYDKAH MLQTDANQIN NLYTNECSLR 250
H 251
Length:251
Mass (Da):28,093
Last modified:October 1, 1996 - v2
Checksum:i00E76C704334343B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X95684 Genomic DNA. Translation: CAA64981.1.
PIRiA58830. HYCY.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X95684 Genomic DNA. Translation: CAA64981.1 .
PIRi A58830. HYCY.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AST X-ray 1.80 A 50-249 [» ]
1IAA X-ray 1.90 A 50-249 [» ]
1IAB X-ray 1.79 A 50-249 [» ]
1IAC X-ray 2.10 A 50-249 [» ]
1IAD X-ray 2.30 A 50-249 [» ]
1IAE X-ray 1.83 A 50-249 [» ]
1QJI X-ray 2.14 A 50-249 [» ]
1QJJ X-ray 1.86 A 50-249 [» ]
3LQ0 X-ray 1.45 A 16-250 [» ]
ProteinModelPortali P07584.
SMRi P07584. Positions 50-249.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M12.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P07584.

Miscellaneous databases

EvolutionaryTracei P07584.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view ]
Pfami PF01400. Astacin. 1 hit.
[Graphical view ]
PRINTSi PR00480. ASTACIN.
SMARTi SM00235. ZnMc. 1 hit.
[Graphical view ]
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 50-249.

Entry informationi

Entry nameiASTA_ASTAS
AccessioniPrimary (citable) accession number: P07584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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