ID TRY1_SALSA Reviewed; 242 AA. AC P35031; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 146. DE RecName: Full=Trypsin-1; DE EC=3.4.21.4; DE AltName: Full=Trypsin I; DE Flags: Precursor; 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). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS). RX PubMed=15299521; DOI=10.1107/s0907444992013118; RA Smalas A.O., Hordvik A.; RT "Structure determination and refinement of benzamidine-inhibited trypsin RT from the North Atlantic salmon (Salmo salar) at 1.82-A resolution."; RL Acta Crystallogr. D 49:318-330(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS). RX PubMed=7846025; DOI=10.1002/prot.340200205; RA Smalas A.O., Heimstad E.S., Hordvik A., Willassen N.P., Male R.; RT "Cold adaption of enzymes: structural comparison between salmon and bovine RT trypsins."; RL Proteins 20:149-166(1994). 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; CC Note=Binds 1 Ca(2+) ion per subunit.; 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; X70075; CAA49680.1; -; mRNA. DR EMBL; X70071; CAA49676.1; -; mRNA. DR EMBL; X70072; CAA49677.1; -; mRNA. DR PIR; S66659; S31776. DR PIR; S66660; S31775. DR RefSeq; NP_001117183.1; NM_001123711.1. DR RefSeq; NP_001119704.1; NM_001126232.1. DR PDB; 1BIT; X-ray; 1.83 A; A=6-242. DR PDB; 1BZX; X-ray; 2.10 A; E=21-242. DR PDB; 1HJ8; X-ray; 1.00 A; A=21-242. DR PDB; 1UTJ; X-ray; 1.83 A; A=1-242. DR PDB; 1UTK; X-ray; 1.53 A; A=1-242. DR PDB; 1UTL; X-ray; 1.70 A; M=1-242. DR PDB; 1UTM; X-ray; 1.50 A; A=1-242. DR PDB; 2STA; X-ray; 1.80 A; E=21-242. DR PDB; 2STB; X-ray; 1.80 A; E=21-242. DR PDB; 2TBS; X-ray; 1.80 A; A=21-242. DR PDBsum; 1BIT; -. DR PDBsum; 1BZX; -. DR PDBsum; 1HJ8; -. DR PDBsum; 1UTJ; -. DR PDBsum; 1UTK; -. DR PDBsum; 1UTL; -. DR PDBsum; 1UTM; -. DR PDBsum; 2STA; -. DR PDBsum; 2STB; -. DR PDBsum; 2TBS; -. DR AlphaFoldDB; P35031; -. DR SMR; P35031; -. DR MINT; P35031; -. DR STRING; 8030.ENSSSAP00000006839; -. DR MEROPS; S01.125; -. DR PaxDb; 8030-ENSSSAP00000006839; -. DR GeneID; 100137021; -. DR GeneID; 100137022; -. DR KEGG; sasa:100137021; -. DR KEGG; sasa:100137022; -. DR CTD; 100137021; -. DR CTD; 100137022; -. DR OrthoDB; 5352724at2759; -. DR SABIO-RK; P35031; -. DR EvolutionaryTrace; P35031; -. DR PRO; PR:P35031; -. DR Proteomes; UP000087266; Unplaced. 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; TRYPSIN-RELATED; 1. DR PANTHER; PTHR24264:SF6; TRYPSINOGEN 1A-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..15 FT /evidence="ECO:0000255" FT PROPEP 16..20 FT /note="Activation peptide" FT /id="PRO_0000028225" FT CHAIN 21..242 FT /note="Trypsin-1" FT /id="PRO_0000028226" FT DOMAIN 21..240 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 60 FT /note="Charge relay system" FT ACT_SITE 104 FT /note="Charge relay system" FT ACT_SITE 196 FT /note="Charge relay system" FT BINDING 72 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 74 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 77 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 82 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT SITE 190 FT /note="Required for specificity" FT /evidence="ECO:0000250" FT DISULFID 27..156 FT DISULFID 45..61 FT DISULFID 129..229 FT DISULFID 136..202 FT DISULFID 167..181 FT DISULFID 192..216 FT VARIANT 33 FT /note="T -> A (in trypsins IA/IB)" FT TURN 29..34 FT /evidence="ECO:0007829|PDB:2TBS" FT STRAND 35..51 FT /evidence="ECO:0007829|PDB:1HJ8" FT STRAND 54..57 FT /evidence="ECO:0007829|PDB:1HJ8" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:1HJ8" FT STRAND 67..71 FT /evidence="ECO:0007829|PDB:1HJ8" FT STRAND 83..92 FT /evidence="ECO:0007829|PDB:1HJ8" FT TURN 98..101 FT /evidence="ECO:0007829|PDB:1HJ8" FT STRAND 106..112 FT /evidence="ECO:0007829|PDB:1HJ8" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:1HJ8" FT STRAND 135..142 FT /evidence="ECO:0007829|PDB:1HJ8" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:1UTL" FT STRAND 155..161 FT /evidence="ECO:0007829|PDB:1HJ8" FT HELIX 164..170 FT /evidence="ECO:0007829|PDB:1HJ8" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:1UTK" FT STRAND 179..183 FT /evidence="ECO:0007829|PDB:1HJ8" FT TURN 193..197 FT /evidence="ECO:0007829|PDB:2TBS" FT STRAND 199..202 FT /evidence="ECO:0007829|PDB:1HJ8" FT STRAND 205..212 FT /evidence="ECO:0007829|PDB:1HJ8" FT STRAND 214..217 FT /evidence="ECO:0007829|PDB:1HJ8" FT STRAND 223..227 FT /evidence="ECO:0007829|PDB:1HJ8" FT HELIX 228..231 FT /evidence="ECO:0007829|PDB:1HJ8" FT HELIX 232..240 FT /evidence="ECO:0007829|PDB:1HJ8" SQ SEQUENCE 242 AA; 25958 MW; 43F5642498067E5A CRC64; MISLVFVLLI GAAFATEDDK IVGGYECKAY SQTHQVSLNS GYHFCGGSLV NENWVVSAAH CYKSRVEVRL GEHNIKVTEG SEQFISSSRV IRHPNYSSYN IDNDIMLIKL SKPATLNTYV QPVALPTSCA PAGTMCTVSG WGNTMSSTAD SNKLQCLNIP ILSYSDCNNS YPGMITNAMF CAGYLEGGKD SCQGDSGGPV VCNGELQGVV SWGYGCAEPG NPGVYAKVCI FNDWLTSTMA SY //