TRY3_SALSA
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 03-AUG-2022, entry version 114.
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}.
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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 SABIO-RK; P35033; -.
DR EvolutionaryTrace; P35033; -.
DR Proteomes; UP000087266; Genome assembly.
DR GO; GO:0005615; C:extracellular space; 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; -; 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; 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
