TRY1_SALSA
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 03-AUG-2022, entry version 141.
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}.
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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 GeneID; 100137021; -.
DR GeneID; 100137022; -.
DR KEGG; sasa:100137021; -.
DR KEGG; sasa:100137022; -.
DR CTD; 100137021; -.
DR CTD; 100137022; -.
DR OrthoDB; 1314811at2759; -.
DR SABIO-RK; P35031; -.
DR EvolutionaryTrace; P35031; -.
DR PRO; PR:P35031; -.
DR Proteomes; UP000087266; Unplaced.
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..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
