ID TRY1_GADMO Reviewed; 241 AA. AC P16049; Q91040; Q92156; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAR-2024, entry version 107. DE RecName: Full=Trypsin-1; DE EC=3.4.21.4; DE AltName: Full=Trypsin I; DE Flags: Precursor; OS Gadus morhua (Atlantic cod). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus. OX NCBI_TaxID=8049; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pyloric caecum; RX PubMed=8223632; DOI=10.1111/j.1432-1033.1993.tb18341.x; RA Gudmundsdottir A., Gudmundsdottir E., Oskarsson S., Bjarnason J.B., RA Eakin A.E., Craik C.S.; RT "Isolation and characterization of cDNAs from Atlantic cod encoding two RT different forms of trypsinogen."; RL Eur. J. Biochem. 217:1091-1097(1993). RN [2] RP PROTEIN SEQUENCE OF 20-58. RC TISSUE=Pyloric caecum; RX PubMed=2707266; DOI=10.1111/j.1432-1033.1989.tb14618.x; RA Asgeirsson B., Fox J.W., Bjarnason J.B.; RT "Purification and characterization of trypsin from the poikilotherm Gadus RT morhua."; RL Eur. J. Biochem. 180:85-94(1989). CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; 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; X76886; CAA54214.1; -; mRNA. DR PIR; S39047; S39047. DR PDB; 2EEK; X-ray; 1.85 A; A=20-239. DR PDBsum; 2EEK; -. DR AlphaFoldDB; P16049; -. DR SMR; P16049; -. DR MEROPS; S01.125; -. DR EvolutionaryTrace; P16049; -. DR Proteomes; UP000694546; Unplaced. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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; Digestion; Direct protein sequencing; Disulfide bond; KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal; KW Zymogen. FT SIGNAL 1..13 FT /evidence="ECO:0000255" FT PROPEP 14..19 FT /note="Activation peptide" FT /evidence="ECO:0000269|PubMed:2707266" FT /id="PRO_0000028309" FT CHAIN 20..241 FT /note="Trypsin-1" FT /id="PRO_0000028310" FT DOMAIN 20..239 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 59 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 103 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 195 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT SITE 189 FT /note="Required for specificity" FT /evidence="ECO:0000250" FT DISULFID 26..155 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 44..60 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 128..228 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 135..201 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 166..180 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 191..215 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT CONFLICT 25 FT /note="E -> Q (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 27..28 FT /note="TK -> EA (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 43 FT /note="F -> Y (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 49..52 FT /note="VSKD -> IN (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT TURN 28..33 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 34..48 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 50..56 FT /evidence="ECO:0007829|PDB:2EEK" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 66..70 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 82..91 FT /evidence="ECO:0007829|PDB:2EEK" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 105..111 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 134..141 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 154..160 FT /evidence="ECO:0007829|PDB:2EEK" FT HELIX 163..169 FT /evidence="ECO:0007829|PDB:2EEK" FT TURN 171..173 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 204..211 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:2EEK" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:2EEK" FT HELIX 227..238 FT /evidence="ECO:0007829|PDB:2EEK" SQ SEQUENCE 241 AA; 25941 MW; 44EC9A0106AD1A68 CRC64; MKSLIFVLLL GAVFAEEDKI VGGYECTKHS QAHQVSLNSG YHFCGGSLVS KDWVVSAAHC YKSVLRVRLG EHHIRVNEGT EQYISSSSVI RHPNYSSYNI NNDIMLIKLT KPATLNQYVH AVALPTECAA DATMCTVSGW GNTMSSVADG DKLQCLSLPI LSHADCANSY PGMITQSMFC AGYLEGGKDS CQGDSGGPVV CNGVLQGVVS WGYGCAERDH PGVYAKVCVL SGWVRDTMAN Y //