ID TRY3_SALSA Reviewed; 238 AA. AC P35033; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 24-JAN-2024, entry version 118. DE RecName: Full=Trypsin-3; DE EC=3.4.21.4; DE AltName: Full=Trypsin III; DE Flags: Precursor; Fragment; 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] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pancreas; RX PubMed=7556223; DOI=10.1111/j.1432-1033.1995.tb20860.x; RA Male R., Lorens J.B., Smals A.O., Torrissen K.R.; RT "Molecular cloning and characterization of anionic and cationic variants of RT trypsin from Atlantic salmon."; RL Eur. J. Biochem. 232:677-685(1995). CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. 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; X70074; CAA49679.1; -; mRNA. DR PIR; S66657; S31779. DR PDB; 1A0J; X-ray; 1.70 A; A/B/C/D=16-238. DR PDBsum; 1A0J; -. DR AlphaFoldDB; P35033; -. DR SMR; P35033; -. DR STRING; 8030.ENSSSAP00000005761; -. DR MEROPS; S01.126; -. DR PaxDb; 8030-ENSSSAP00000005761; -. DR SABIO-RK; P35033; -. DR EvolutionaryTrace; P35033; -. 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:0007586; P:digestion; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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 PANTHER; PTHR24264:SF15; RIKEN CDNA 2210010C04 GENE; 1. DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Digestion; Disulfide bond; Hydrolase; Metal-binding; KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen. FT SIGNAL <1..7 FT /evidence="ECO:0000255" FT PROPEP 8..15 FT /note="Activation peptide" FT /id="PRO_0000028229" FT CHAIN 16..238 FT /note="Trypsin-3" FT /id="PRO_0000028230" FT DOMAIN 16..236 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 55 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 99 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 192 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT BINDING 67 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 72 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 77 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT SITE 186 FT /note="Required for specificity" FT /evidence="ECO:0000250" FT DISULFID 22..152 FT DISULFID 40..56 FT DISULFID 124..225 FT DISULFID 131..198 FT DISULFID 163..177 FT DISULFID 188..212 FT NON_TER 1 FT TURN 26..29 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 30..35 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 38..52 FT /evidence="ECO:0007829|PDB:1A0J" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 68..72 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 78..87 FT /evidence="ECO:0007829|PDB:1A0J" FT TURN 93..96 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 101..107 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 130..137 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 151..157 FT /evidence="ECO:0007829|PDB:1A0J" FT HELIX 160..166 FT /evidence="ECO:0007829|PDB:1A0J" FT TURN 168..170 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 195..198 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 201..208 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 210..213 FT /evidence="ECO:0007829|PDB:1A0J" FT STRAND 219..223 FT /evidence="ECO:0007829|PDB:1A0J" FT HELIX 224..227 FT /evidence="ECO:0007829|PDB:1A0J" FT HELIX 228..237 FT /evidence="ECO:0007829|PDB:1A0J" SQ SEQUENCE 238 AA; 25389 MW; AE799B80E8393023 CRC64; FAVAFAAPID DEDDKIVGGY ECRKNSASYQ ASLQSGYHFC GGSLISSTWV VSAAHCYKSR IQVRLGEHNI AVNEGTEQFI DSVKVIMHPS YNSRNLDNDI MLIKLSKPAS LNSYVSTVAL PSSCASSGTR CLVSGWGNLS GSSSNYPDTL RCLDLPILSS SSCNSAYPGQ ITSNMFCAGF MEGGKDSCQG DSGGPVVCNG QLQGVVSWGY GCAQRNKPGV YTKVCNYRSW ISSTMSSN //