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Database: UniProt
Entry: P00761
LinkDB: P00761
Original site: P00761 
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   07-NOV-2018, entry version 148.
DE   RecName: Full=Trypsin;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   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
RT   sequenator 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
RT   between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the
RT   squash family. Detailed comparison with bovine beta-trypsin and its
RT   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.,
RA   Huber R., Piechottka G.P., Matschiner G., Sommerhoff C.P., Fritz H.,
RA   Auerswald E.A.;
RT   "The three-dimensional structure of recombinant leech-derived tryptase
RT   inhibitor in complex with trypsin. Implications for the structure of
RT   human 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)
RT   with 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
RT   of its complex with bdellastasin.";
RL   Acta Crystallogr. D 56:581-588(2000).
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
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.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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; 1D3O; Model; -; A=9-231.
DR   PDB; 1DF2; Model; -; 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; 1EWU; Model; -; A=9-231.
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; 1LT2; Model; -; A=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; 1D3O; -.
DR   PDBsum; 1DF2; -.
DR   PDBsum; 1EJA; -.
DR   PDBsum; 1EPT; -.
DR   PDBsum; 1EWU; -.
DR   PDBsum; 1FMG; -.
DR   PDBsum; 1FN6; -.
DR   PDBsum; 1FNI; -.
DR   PDBsum; 1H9H; -.
DR   PDBsum; 1H9I; -.
DR   PDBsum; 1LDT; -.
DR   PDBsum; 1LT2; -.
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   ProteinModelPortal; P00761; -.
DR   SMR; P00761; -.
DR   DIP; DIP-6083N; -.
DR   IntAct; P00761; 3.
DR   MINT; P00761; -.
DR   STRING; 9823.ENSSSCP00000017465; -.
DR   BindingDB; P00761; -.
DR   ChEMBL; CHEMBL2366; -.
DR   PaxDb; P00761; -.
DR   PeptideAtlas; P00761; -.
DR   PRIDE; P00761; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251820; -.
DR   HOVERGEN; HBG013304; -.
DR   OrthoDB; EOG091G0DF7; -.
DR   BRENDA; 3.4.21.4; 6170.
DR   SABIO-RK; P00761; -.
DR   EvolutionaryTrace; P00761; -.
DR   Proteomes; UP000008227; 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   InterPro; IPR009003; Peptidase_S1_PA.
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; Complete proteome; Digestion;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
KW   Protease; Reference proteome; Secreted; Serine protease; Zymogen.
FT   PROPEP        1      8       Activation peptide.
FT                                {ECO:0000269|PubMed:4738933}.
FT                                /FTId=PRO_0000028205.
FT   CHAIN         9    231       Trypsin.
FT                                /FTId=PRO_0000028206.
FT   DOMAIN        9    229       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     48     48       Charge relay system.
FT   ACT_SITE     92     92       Charge relay system.
FT   ACT_SITE    185    185       Charge relay system.
FT   METAL        60     60       Calcium.
FT   METAL        62     62       Calcium; via carbonyl oxygen.
FT   METAL        65     65       Calcium; via carbonyl oxygen.
FT   METAL        70     70       Calcium.
FT   SITE        179    179       Required for specificity. {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     20       I -> V.
FT   STRAND       23     39       {ECO:0000244|PDB:1S83}.
FT   STRAND       42     45       {ECO:0000244|PDB:1S83}.
FT   HELIX        47     49       {ECO:0000244|PDB:1S83}.
FT   STRAND       55     59       {ECO:0000244|PDB:1S83}.
FT   STRAND       61     65       {ECO:0000244|PDB:3MYW}.
FT   STRAND       71     80       {ECO:0000244|PDB:1S83}.
FT   TURN         86     88       {ECO:0000244|PDB:1S83}.
FT   STRAND       94    100       {ECO:0000244|PDB:1S83}.
FT   STRAND      105    108       {ECO:0000244|PDB:1S83}.
FT   STRAND      123    130       {ECO:0000244|PDB:1S83}.
FT   STRAND      134    136       {ECO:0000244|PDB:1S83}.
FT   STRAND      144    150       {ECO:0000244|PDB:1S83}.
FT   HELIX       153    159       {ECO:0000244|PDB:1S83}.
FT   TURN        161    163       {ECO:0000244|PDB:1S83}.
FT   STRAND      168    172       {ECO:0000244|PDB:1S83}.
FT   STRAND      174    177       {ECO:0000244|PDB:2A31}.
FT   TURN        182    186       {ECO:0000244|PDB:1S6H}.
FT   STRAND      188    191       {ECO:0000244|PDB:1S83}.
FT   STRAND      194    201       {ECO:0000244|PDB:1S83}.
FT   STRAND      203    206       {ECO:0000244|PDB:1S83}.
FT   STRAND      212    216       {ECO:0000244|PDB:1S83}.
FT   HELIX       217    219       {ECO:0000244|PDB:1S83}.
FT   HELIX       221    230       {ECO:0000244|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
//
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