ASTA_ASTAS
ID ASTA_ASTAS Reviewed; 251 AA.
AC P07584;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Astacin;
DE EC=3.4.24.21 {ECO:0000269|PubMed:2261483, ECO:0000269|Ref.3};
DE AltName: Full=Crayfish small molecule proteinase;
DE Flags: Precursor;
OS Astacus astacus (Noble crayfish) (Astacus fluviatilis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Astacoidea; Astacidae; Astacus.
OX NCBI_TaxID=6715;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9016826; DOI=10.1006/abbi.1996.9759;
RA Geier G., Jacob E., Stoecker W., Zwilling R.;
RT "Genomic organization of the zinc-endopeptidase astacin.";
RL Arch. Biochem. Biophys. 337:300-307(1997).
RN [2]
RP PROTEIN SEQUENCE OF 50-249.
RX PubMed=3548817; DOI=10.1021/bi00375a029;
RA Titani K., Torff H.-J., Hormel S., Kumar S., Walsh K.A., Rodl J.,
RA Neurath H., Zwilling R.;
RT "Amino acid sequence of a unique protease from the crayfish Astacus
RT fluviatilis.";
RL Biochemistry 26:222-226(1987).
RN [3]
RP ZINC-BINDING, COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION.
RA Stoecker W., Wolz R.L., Zwilling R., Strydom D.J., Auld D.S.;
RT "Astacus protease, a zinc metalloenzyme.";
RL Biochemistry 27:5026-5032(1988).
RN [4]
RP SUBSTRATE SPECIFICITY, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2261483; DOI=10.1021/bi00497a018;
RA Stoecker W., Ng M., Auld D.S.;
RT "Fluorescent oligopeptide substrates for kinetic characterization of the
RT specificity of Astacus protease.";
RL Biochemistry 29:10418-10425(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 50-249 IN COMPLEX WITH ZINC,
RP COFACTOR, AND DISULFIDE BONDS.
RX PubMed=1319561; DOI=10.1038/358164a0;
RA Bode W., Gomis-Rueth F.-X., Huber R., Zwilling R., Stoecker W.;
RT "Structure of astacin and implications for activation of astacins and zinc-
RT ligation of collagenases.";
RL Nature 358:164-167(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 50-249, AND DISULFIDE BONDS.
RX PubMed=8445658; DOI=10.1006/jmbi.1993.1098;
RA Gomis-Rueth F.-X., Stoecker W., Huber R., Zwilling R., Bode W.;
RT "Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase
RT from the crayfish Astacus astacus L. Structure determination, refinement,
RT molecular structure and comparison with thermolysin.";
RL J. Mol. Biol. 229:945-968(1993).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 50-249 IN COMPLEX WITH ZINC,
RP COFACTOR, AND DISULFIDE BONDS.
RX PubMed=8756323; DOI=10.1038/nsb0896-671;
RA Grams F., Dive V., Yiotakis A., Yiallouros I., Vassiliou S., Zwilling R.,
RA Bode W., Stoecker W.;
RT "Structure of astacin with a transition-state analogue inhibitor.";
RL Nat. Struct. Biol. 3:671-675(1996).
CC -!- FUNCTION: Metalloprotease. This protease prefers to cleave in front of
CC small aliphatic residues (P1'). The presence of Lys or Arg in the P1
CC and P2 position yields high-turnover substrates. In the P3 position the
CC enzyme prefers Pro > Val > Leu > Ala > Gly.
CC {ECO:0000269|PubMed:2261483}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of peptide bonds in substrates containing five or
CC more amino acids, preferentially with Ala in P1', and Pro in P2'.;
CC EC=3.4.24.21; Evidence={ECO:0000269|PubMed:2261483,
CC ECO:0000269|Ref.3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01211,
CC ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323,
CC ECO:0000269|Ref.3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01211, ECO:0000269|PubMed:1319561,
CC ECO:0000269|PubMed:8756323, ECO:0000269|Ref.3};
CC -!- SUBUNIT: Monomer.
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DR EMBL; X95684; CAA64981.1; -; Genomic_DNA.
DR PIR; A58830; HYCY.
DR PDB; 1AST; X-ray; 1.80 A; A=50-249.
DR PDB; 1IAA; X-ray; 1.90 A; A=50-249.
DR PDB; 1IAB; X-ray; 1.79 A; A=50-249.
DR PDB; 1IAC; X-ray; 2.10 A; A=50-249.
DR PDB; 1IAD; X-ray; 2.30 A; A=50-249.
DR PDB; 1IAE; X-ray; 1.83 A; A=50-249.
DR PDB; 1QJI; X-ray; 2.14 A; A=50-249.
DR PDB; 1QJJ; X-ray; 1.86 A; A=50-249.
DR PDB; 3LQ0; X-ray; 1.45 A; A=16-250.
DR PDB; 6HT9; X-ray; 3.10 A; A/C=1-251.
DR PDB; 6SAZ; X-ray; 3.00 A; A/C=50-251.
DR PDBsum; 1AST; -.
DR PDBsum; 1IAA; -.
DR PDBsum; 1IAB; -.
DR PDBsum; 1IAC; -.
DR PDBsum; 1IAD; -.
DR PDBsum; 1IAE; -.
DR PDBsum; 1QJI; -.
DR PDBsum; 1QJJ; -.
DR PDBsum; 3LQ0; -.
DR PDBsum; 6HT9; -.
DR PDBsum; 6SAZ; -.
DR AlphaFoldDB; P07584; -.
DR SMR; P07584; -.
DR MEROPS; M12.001; -.
DR KEGG; ag:CAA64981; -.
DR BRENDA; 3.4.24.21; 546.
DR SABIO-RK; P07584; -.
DR EvolutionaryTrace; P07584; -.
DR GO; GO:0060473; C:cortical granule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0070001; F:aspartic-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0070002; F:glutamic-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:2000360; P:negative regulation of binding of sperm to zona pellucida; ISS:UniProtKB.
DR GO; GO:0010954; P:positive regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0060468; P:prevention of polyspermy; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR Pfam; PF01400; Astacin; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Signal; Zinc; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..49
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:3548817"
FT /id="PRO_0000028872"
FT CHAIN 50..249
FT /note="Astacin"
FT /evidence="ECO:0000269|PubMed:8445658"
FT /id="PRO_0000028873"
FT PROPEP 250..251
FT /id="PRO_0000028874"
FT DOMAIN 50..248
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT ACT_SITE 142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211,
FT ECO:0000305|PubMed:1319561"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211,
FT ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211,
FT ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211,
FT ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323"
FT DISULFID 91..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211,
FT ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:3548817,
FT ECO:0000269|PubMed:8445658, ECO:0000269|PubMed:8756323"
FT DISULFID 113..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211,
FT ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:3548817,
FT ECO:0000269|PubMed:8445658, ECO:0000269|PubMed:8756323"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:3LQ0"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:3LQ0"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3LQ0"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3LQ0"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:3LQ0"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3LQ0"
FT STRAND 101..118
FT /evidence="ECO:0007829|PDB:3LQ0"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:3LQ0"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:3LQ0"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:3LQ0"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:1IAB"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:3LQ0"
FT TURN 205..209
FT /evidence="ECO:0007829|PDB:3LQ0"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:3LQ0"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:3LQ0"
SQ SEQUENCE 251 AA; 28093 MW; 00E76C704334343B CRC64;
MQCAVLLVLL GVVAASPIIP EAARALYYND GMFEGDIKLR AGRQPARVGA AILGDEYLWS
GGVIPYTFAG VSGADQSAIL SGMQELEEKT CIRFVPRTTE SDYVEIFTSG SGCWSYVGRI
SGAQQVSLQA NGCVYHGTII HELMHAIGFY HEHTRMDRDN YVTINYQNVD PSMTSNFDID
TYSRYVGEDY QYYSIMHYGK YSFSIQWGVL ETIVPLQNGI DLTDPYDKAH MLQTDANQIN
NLYTNECSLR H
