ELA1_SALSA
ID ELA1_SALSA Reviewed; 236 AA.
AC Q7SIG3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Elastase-1;
DE EC=3.4.21.36;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1] {ECO:0000305, ECO:0000312|PDB:1ELT}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9628006;
RA Berglund G.I., Smalaas A.O., Outzen H., Willassen N.P.;
RT "Purification and characterization of pancreatic elastase from North
RT Atlantic salmon (Salmo salar).";
RL Mol. Mar. Biol. Biotechnol. 7:105-114(1998).
RN [2] {ECO:0000305}
RP CRYSTALLIZATION, AND X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=15299308; DOI=10.1107/s0907444994011066;
RA Berglund G.I., Smalaas A.O., Hansen L.K., Willassen N.P.;
RT "Crystallization and preliminary X-ray crystallographic studies of native
RT elastase from North Atlantic salmon (Salmo salar).";
RL Acta Crystallogr. D 51:393-394(1995).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS), COFACTOR, AND DISULFIDE BONDS.
RX PubMed=15299762; DOI=10.1107/s0907444995004835;
RA Berglund G.I., Willassen N.P., Hordvik A., Smalaas A.O.;
RT "Structure of native pancreatic elastase from North Atlantic salmon at 1.61
RT A resolution.";
RL Acta Crystallogr. D 51:925-937(1995).
CC -!- FUNCTION: Acts upon elastin. {ECO:0000269|PubMed:9628006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, including elastin. Preferential
CC cleavage: Ala-|-Xaa.; EC=3.4.21.36;
CC Evidence={ECO:0000269|PubMed:9628006};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15299762};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:15299762};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.47 mM for Suc-AAA-pNA (at 22 degrees Celsius)
CC {ECO:0000269|PubMed:9628006};
CC KM=1.34 mM for Suc-AAPL-pNA (at 22 degrees Celsius)
CC {ECO:0000269|PubMed:9628006};
CC KM=0.82 mM for Suc-AAPV-pNA (at 22 degrees Celsius)
CC {ECO:0000269|PubMed:9628006};
CC KM=0.83 mM for Suc-AAPA-pNA (at 22 degrees Celsius)
CC {ECO:0000269|PubMed:9628006};
CC KM=0.15 mM for Suc-AAPI-pNA (at 22 degrees Celsius)
CC {ECO:0000269|PubMed:9628006};
CC pH dependence:
CC Optimum pH is 8.1 at 22 degrees Celsius with Suc-AAA-pNA as the
CC substrate. {ECO:0000269|PubMed:9628006};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9628006}.
CC -!- TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:9628006}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR PDB; 1ELT; X-ray; 1.61 A; A=1-236.
DR PDBsum; 1ELT; -.
DR AlphaFoldDB; Q7SIG3; -.
DR SMR; Q7SIG3; -.
DR STRING; 8030.ENSSSAP00000058502; -.
DR EvolutionaryTrace; Q7SIG3; -.
DR Proteomes; UP000087266; Genome assembly.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Serine protease.
FT CHAIN 1..236
FT /note="Elastase-1"
FT /id="PRO_0000248261"
FT DOMAIN 1..236
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 45
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:15299762"
FT ACT_SITE 93
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:15299762"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:15299762"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15299762"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15299762"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15299762"
FT DISULFID 30..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15299762"
FT DISULFID 127..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15299762"
FT DISULFID 158..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15299762"
FT DISULFID 183..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15299762"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1ELT"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1ELT"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1ELT"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1ELT"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:1ELT"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:1ELT"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1ELT"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:1ELT"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:1ELT"
SQ SEQUENCE 236 AA; 25015 MW; 06CF7DB4E1397E97 CRC64;
VVGGRVAQPN SWPWQISLQY KSGSSYYHTC GGSLIRQGWV MTAAHCVDSA RTWRVVLGEH
NLNTNEGKEQ IMTVNSVFIH SGWNSDDVAG GYDIALLRLN TQASLNSAVQ LAALPPSNQI
LPNNNPCYIT GWGKTSTGGP LSDSLKQAWL PSVDHATCSS SGWWGSTVKT TMVCAGGGAN
SGCNGDSGGP LNCQVNGSYY VHGVTSFVSS SGCNASKKPT VFTRVSAYIS WMNGIM
