P07584 (ASTA_ASTFL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Astacin EC=3.4.24.21 Alternative name(s): Crayfish small molecule proteinase
Organism	Astacus fluviatilis (Broad-fingered crayfish) (Astacus astacus)
Taxonomic identifier	6715 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Pleocyemata › Astacidea › Astacoidea › Astacidae › Astacus

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	cell adhesion 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_component	cortical granule Inferred from sequence or structural similarity PubMed 22472438. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity PubMed 22206759. Source: UniProtKB
Molecular_function	aspartic-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 zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

15

Potential

Propeptide

16 – 49

34

Activation peptide

PRO_0000028872

Chain

50 – 249

200

Astacin Ref.6

PRO_0000028873

Propeptide

250 – 251

2

PRO_0000028874

Sites

Active site

142

1

Metal binding

141

1

Zinc; catalytic Ref.5

Metal binding

145

1

Zinc; catalytic Ref.5

Metal binding

151

1

Zinc; catalytic Ref.5

Amino acid modifications

Disulfide bond

91 ↔ 247

Ref.2

Disulfide bond

113 ↔ 133

Ref.2

Secondary structure

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251

Helix Strand Turn

Details...

Helix

21 – 27

7

Turn

34 – 36

3

Beta strand

46 – 48

3

Beta strand

51 – 53

3

Helix

55 – 57

3

Helix

60 – 62

3

Beta strand

63 – 70

8

Helix

73 – 89

17

Beta strand

93 – 96

4

Beta strand

101 – 118

18

Beta strand

121 – 128

8

Turn

130 – 133

4

Helix

136 – 147

12

Helix

152 – 154

3

Helix

158 – 160

3

Beta strand

162 – 164

3

Helix

166 – 168

3

Helix

174 – 177

4

Beta strand

181 – 184

4

Turn

200 – 203

4

Turn

205 – 209

5

Beta strand

212 – 217

6

Helix

225 – 227

3

Helix

233 – 242

10

Helix

244 – 249

6

Sequences

	Sequence		Length	Mass (Da)
	P07584 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 00E76C704334343B	FASTA	251	28,093
	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

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.

PIR

HYCY. A58830.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P07584.

SMR

P07584. Positions 50-249.

ModBase

Search...

Protein family/group databases

MEROPS

M12.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P07584.

Family and domain databases

Gene3D

3.40.390.10. 1 hit.

InterPro

IPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]

Pfam

PF01400. Astacin. 1 hit.
[Graphical view]

PRINTS

PR00480. ASTACIN.

SMART

SM00235. ZnMc. 1 hit.
[Graphical view]

PROSITE

PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07584.

Entry information

Entry name

ASTA_ASTFL

Accession

Primary (citable) accession number: P07584

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)