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 27-MAR-2024, entry version 127. 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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU01211, ECO:0000269|PubMed:1319561, CC ECO:0000269|PubMed:8756323, 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; Collagenase (Catalytic Domain); 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 PANTHER; PTHR10127:SF780; ASTACIN-LIKE METALLOENDOPEPTIDASE-RELATED; 1. DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1. DR Pfam; PF01400; Astacin; 1. DR PRINTS; PR00480; ASTACIN. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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 //