TRYP_PIG
ID TRYP_PIG Reviewed; 231 AA.
AC P00761;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Trypsin;
DE EC=3.4.21.4;
DE Flags: Precursor;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE OF 1-10.
RX PubMed=14020231; DOI=10.1016/0006-3002(63)91231-9;
RA Charles M., Rovery M., Guidoni A.A., Desnuelle P.;
RT "On trypsinogen and trypsin of pig.";
RL Biochim. Biophys. Acta 69:115-129(1963).
RN [2]
RP PROTEIN SEQUENCE OF 9-231.
RX PubMed=4738933; DOI=10.1021/bi00741a002;
RA Hermodson M.A., Ericsson L.H., Neurath H., Walsh K.A.;
RT "Determination of the amino acid sequence of porcine trypsin by sequenator
RT analysis.";
RL Biochemistry 12:3146-3153(1973).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=8445634; DOI=10.1006/jmbi.1993.1102;
RA Huang Q., Liu S., Tang Y.;
RT "Refined 1.6-A resolution crystal structure of the complex formed between
RT porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family.
RT Detailed comparison with bovine beta-trypsin and its complex.";
RL J. Mol. Biol. 229:1022-1036(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=1551419; DOI=10.1016/0014-5793(92)80346-i;
RA Huang Q., Liu S., Tang Y., Zeng F., Qian R.;
RT "Amino acid sequencing of a trypsin inhibitor by refined 1.6 A X-ray
RT crystal structure of its complex with porcine beta-trypsin.";
RL FEBS Lett. 297:143-146(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=7947985; DOI=10.1016/0167-4838(94)90139-2;
RA Huang Q., Wang Z., Li Y., Liu S., Tang Y.;
RT "Refined 1.8-A resolution crystal structure of the porcine epsilon-
RT trypsin.";
RL Biochim. Biophys. Acta 1209:77-82(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH LDTI.
RX PubMed=9242660; DOI=10.1074/jbc.272.32.19931;
RA Stubbs M.T., Morenweiser R., Stuerzebecher J., Bauer M., Bode W., Huber R.,
RA Piechottka G.P., Matschiner G., Sommerhoff C.P., Fritz H., Auerswald E.A.;
RT "The three-dimensional structure of recombinant leech-derived tryptase
RT inhibitor in complex with trypsin. Implications for the structure of human
RT mast cell tryptase and its inhibition.";
RL J. Biol. Chem. 272:19931-19937(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF COMPLEX WITH LDTI.
RX PubMed=9384562; DOI=10.1016/s0969-2126(97)00296-7;
RA di Marco S., Priestle J.P.;
RT "Structure of the complex of leech-derived tryptase inhibitor (LDTI) with
RT trypsin and modeling of the LDTI-tryptase system.";
RL Structure 5:1465-1474(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH BDELLASTASIN.
RX PubMed=10771427; DOI=10.1107/s0907444900003048;
RA Rester U., Moser M., Huber R., Bode W.;
RT "L-isoaspartate 115 of porcine beta-trypsin promotes crystallization of its
RT complex with bdellastasin.";
RL Acta Crystallogr. D 56:581-588(2000).
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 PIR; A90641; TRPGTR.
DR PDB; 1AKS; X-ray; 1.80 A; A=9-133, B=134-231.
DR PDB; 1AN1; X-ray; 2.03 A; E=9-231.
DR PDB; 1AVW; X-ray; 1.75 A; A=9-231.
DR PDB; 1AVX; X-ray; 1.90 A; A=9-231.
DR PDB; 1C9P; X-ray; 2.80 A; A=9-231.
DR PDB; 1EJA; X-ray; 2.70 A; A=9-231.
DR PDB; 1EPT; X-ray; 1.80 A; A=9-51, B=52-133, C=134-231.
DR PDB; 1FMG; X-ray; 1.90 A; A=9-231.
DR PDB; 1FN6; X-ray; 1.80 A; A=9-231.
DR PDB; 1FNI; X-ray; 1.60 A; A=9-231.
DR PDB; 1H9H; X-ray; 1.50 A; E=9-231.
DR PDB; 1H9I; X-ray; 1.90 A; E=9-231.
DR PDB; 1LDT; X-ray; 1.90 A; T=9-231.
DR PDB; 1MCT; X-ray; 1.60 A; A=9-231.
DR PDB; 1QQU; X-ray; 1.63 A; A=9-231.
DR PDB; 1S5S; X-ray; 1.40 A; A=9-231.
DR PDB; 1S6F; X-ray; 1.80 A; A=9-231.
DR PDB; 1S6H; X-ray; 1.45 A; A=9-231.
DR PDB; 1S81; X-ray; 1.70 A; A=9-231.
DR PDB; 1S82; X-ray; 1.85 A; A=9-231.
DR PDB; 1S83; X-ray; 1.25 A; A=9-231.
DR PDB; 1S84; X-ray; 1.85 A; A=9-231.
DR PDB; 1S85; X-ray; 2.20 A; A=9-231.
DR PDB; 1TFX; X-ray; 2.60 A; A/B=9-231.
DR PDB; 1TX6; X-ray; 2.20 A; A/B/C/D=9-231.
DR PDB; 1UHB; X-ray; 2.15 A; A=9-133, B=134-231, P=177-185.
DR PDB; 1V6D; X-ray; 1.90 A; A=9-231.
DR PDB; 1YF4; X-ray; 1.98 A; A=9-231.
DR PDB; 1Z7K; X-ray; 1.90 A; A=9-231.
DR PDB; 2A31; X-ray; 1.25 A; A=9-231.
DR PDB; 2A32; X-ray; 1.50 A; A=9-231.
DR PDB; 3MYW; X-ray; 2.50 A; A/B=9-231.
DR PDB; 4AN7; X-ray; 2.23 A; A=1-231.
DR PDB; 4DOQ; X-ray; 2.00 A; A/C/E=9-231.
DR PDB; 5XWJ; X-ray; 1.80 A; A/B=1-231.
DR PDB; 5XWL; X-ray; 2.10 A; A/B=1-231.
DR PDBsum; 1AKS; -.
DR PDBsum; 1AN1; -.
DR PDBsum; 1AVW; -.
DR PDBsum; 1AVX; -.
DR PDBsum; 1C9P; -.
DR PDBsum; 1EJA; -.
DR PDBsum; 1EPT; -.
DR PDBsum; 1FMG; -.
DR PDBsum; 1FN6; -.
DR PDBsum; 1FNI; -.
DR PDBsum; 1H9H; -.
DR PDBsum; 1H9I; -.
DR PDBsum; 1LDT; -.
DR PDBsum; 1MCT; -.
DR PDBsum; 1QQU; -.
DR PDBsum; 1S5S; -.
DR PDBsum; 1S6F; -.
DR PDBsum; 1S6H; -.
DR PDBsum; 1S81; -.
DR PDBsum; 1S82; -.
DR PDBsum; 1S83; -.
DR PDBsum; 1S84; -.
DR PDBsum; 1S85; -.
DR PDBsum; 1TFX; -.
DR PDBsum; 1TX6; -.
DR PDBsum; 1UHB; -.
DR PDBsum; 1V6D; -.
DR PDBsum; 1YF4; -.
DR PDBsum; 1Z7K; -.
DR PDBsum; 2A31; -.
DR PDBsum; 2A32; -.
DR PDBsum; 3MYW; -.
DR PDBsum; 4AN7; -.
DR PDBsum; 4DOQ; -.
DR PDBsum; 5XWJ; -.
DR PDBsum; 5XWL; -.
DR AlphaFoldDB; P00761; -.
DR SMR; P00761; -.
DR DIP; DIP-6083N; -.
DR IntAct; P00761; 5.
DR MINT; P00761; -.
DR STRING; 9823.ENSSSCP00000017465; -.
DR BindingDB; P00761; -.
DR ChEMBL; CHEMBL2366; -.
DR DrugCentral; P00761; -.
DR PaxDb; P00761; -.
DR PeptideAtlas; P00761; -.
DR PRIDE; P00761; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_0_1; -.
DR BRENDA; 3.4.21.4; 6170.
DR SABIO-RK; P00761; -.
DR EvolutionaryTrace; P00761; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P00761; SS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:CAFA.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Metal-binding; Protease; Reference proteome;
KW Secreted; Serine protease; Zymogen.
FT PROPEP 1..8
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:4738933"
FT /id="PRO_0000028205"
FT CHAIN 9..231
FT /note="Trypsin"
FT /id="PRO_0000028206"
FT DOMAIN 9..229
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 48
FT /note="Charge relay system"
FT ACT_SITE 92
FT /note="Charge relay system"
FT ACT_SITE 185
FT /note="Charge relay system"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT SITE 179
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 15..145
FT DISULFID 33..49
FT DISULFID 117..218
FT DISULFID 124..191
FT DISULFID 156..170
FT DISULFID 181..205
FT VARIANT 20
FT /note="I -> V"
FT STRAND 23..39
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1S83"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:3MYW"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:1S83"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1S83"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:1S83"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2A31"
FT TURN 182..186
FT /evidence="ECO:0007829|PDB:1S6H"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1S83"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1S83"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1S83"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:1S83"
SQ SEQUENCE 231 AA; 24409 MW; A0A125CF7FC138C2 CRC64;
FPTDDDDKIV GGYTCAANSI PYQVSLNSGS HFCGGSLINS QWVVSAAHCY KSRIQVRLGE
HNIDVLEGNE QFINAAKIIT HPNFNGNTLD NDIMLIKLSS PATLNSRVAT VSLPRSCAAA
GTECLISGWG NTKSSGSSYP SLLQCLKAPV LSDSSCKSSY PGQITGNMIC VGFLEGGKDS
CQGDSGGPVV CNGQLQGIVS WGYGCAQKNK PGVYTKVCNY VNWIQQTIAA N
