IED ID |
IndEnz0002009574 |
Enzyme Type ID |
protease009574 |
Protein Name |
Serine protease 1
EC 3.4.21.4
Anionic trypsin I
Anionic trypsin-I
Beta-trypsin
Cationic trypsin
Pretrypsinogen I
Trypsin I
Trypsin-I
Cleaved into: Alpha-trypsin chain 1; Alpha-trypsin chain 2
|
Gene Name |
PRSS1 TRP1 TRY1 TRYP1 |
Organism |
Bos taurus (Bovine) |
Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Deuterostomia
Chordata
Craniata
Vertebrata
Gnathostomata (jawed vertebrates)
Teleostomi
Euteleostomi
Sarcopterygii
Dipnotetrapodomorpha
Tetrapoda
Amniota
Mammalia
Theria
Eutheria
Boreoeutheria
Laurasiatheria
Artiodactyla
Ruminantia
Pecora
Bovidae
Bovinae
Bos (oxen
cattle)
Bos taurus (Bovine)
|
Enzyme Sequence |
MKTFIFLALLGAAVAFPVDDDDKIVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN |
Enzyme Length |
246 |
Uniprot Accession Number |
P00760 |
Absorption |
|
Active Site |
ACT_SITE 63; /note=Charge relay system; ACT_SITE 107; /note=Charge relay system; ACT_SITE 200; /note=Charge relay system |
Activity Regulation |
ACTIVITY REGULATION: Is inhibited by scorpion cyclotide trypsin inhibitor TopI1. {ECO:0000269|PubMed:32787139}. |
Binding Site |
BINDING 200; /note=Substrate |
Calcium Binding |
|
catalytic Activity |
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; |
DNA Binding |
|
EC Number |
3.4.21.4 |
Enzyme Function |
|
Temperature Dependency |
|
PH Dependency |
|
Pathway |
|
nucleotide Binding |
|
Features |
Active site (3); Beta strand (17); Binding site (1); Chain (3); Disulfide bond (6); Domain (1); Helix (4); Metal binding (4); Propeptide (1); Region (2); Signal peptide (1); Turn (6) |
Keywords |
3D-structure;Calcium;Digestion;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
Interact With |
P00974; P01009 |
Induction |
|
Subcellular Location |
SUBCELLULAR LOCATION: Secreted, extracellular space. |
Modified Residue |
|
Post Translational Modification |
PTM: Autocatalytic cleavage after Lys-23 leads to beta-trypsin by releasing a terminal hexapeptide. Subsequent cleavage after Lys-148 leads to alpha-trypsin. Further cleavage after Lys-193 yields pseudotrypsin. A cleavage may also occur after Arg-122.; PTM: Not sulfated on tyrosine residue(s). |
Signal Peptide |
SIGNAL 1..17; /evidence=ECO:0000269|PubMed:5967094 |
Structure 3D |
Neutron diffraction (7); Electron microscopy (1); X-ray crystallography (535) |
Cross Reference PDB |
1AQ7;
1AUJ;
1AZ8;
1BJU;
1BJV;
1BTP;
1BTW;
1BTX;
1BTY;
1BTZ;
1C1N;
1C1O;
1C1P;
1C1Q;
1C1R;
1C1S;
1C1T;
1C2D;
1C2E;
1C2F;
1C2G;
1C2H;
1C2I;
1C2J;
1C2K;
1C2L;
1C2M;
1C5P;
1C5Q;
1C5R;
1C5S;
1C5T;
1C5U;
1C5V;
1C9T;
1CE5;
1D6R;
1EB2;
1EJM;
1EZX;
1F0T;
1F0U;
1F2S;
1G36;
1G3B;
1G3C;
1G3D;
1G3E;
1G9I;
1GBT;
1GHZ;
1GI0;
1GI1;
1GI2;
1GI3;
1GI4;
1GI5;
1GI6;
1GJ6;
1HJ9;
1J8A;
1JIR;
1JRS;
1JRT;
1K1I;
1K1J;
1K1L;
1K1M;
1K1N;
1K1O;
1K1P;
1LQE;
1MAX;
1MAY;
1MTS;
1MTU;
1MTV;
1MTW;
1N6X;
1N6Y;
1NC6;
1NTP;
1O2H;
1O2I;
1O2J;
1O2K;
1O2L;
1O2M;
1O2N;
1O2O;
1O2P;
1O2Q;
1O2R;
1O2S;
1O2T;
1O2U;
1O2V;
1O2W;
1O2X;
1O2Y;
1O2Z;
1O30;
1O31;
1O32;
1O33;
1O34;
1O35;
1O36;
1O37;
1O38;
1O39;
1O3A;
1O3B;
1O3C;
1O3D;
1O3E;
1O3F;
1O3G;
1O3H;
1O3I;
1O3J;
1O3K;
1O3L;
1O3M;
1O3N;
1O3O;
1OPH;
1OX1;
1OYQ;
1P2I;
1P2J;
1P2K;
1PPC;
1PPE;
1PPH;
1QA0;
1QB1;
1QB6;
1QB9;
1QBN;
1QBO;
1QCP;
1QL7;
1QL8;
1RXP;
1S0Q;
1S0R;
1SBW;
1SFI;
1SMF;
1TAB;
1TAW;
1TGB;
1TGC;
1TGN;
1TGS;
1TGT;
1TIO;
1TLD;
1TNG;
1TNH;
1TNI;
1TNJ;
1TNK;
1TNL;
1TPA;
1TPO;
1TPP;
1TPS;
1TX7;
1TX8;
1TYN;
1UTN;
1UTO;
1UTP;
1UTQ;
1V2J;
1V2K;
1V2L;
1V2M;
1V2N;
1V2O;
1V2P;
1V2Q;
1V2R;
1V2S;
1V2T;
1V2U;
1V2V;
1V2W;
1XUF;
1XUG;
1XUH;
1XUI;
1XUJ;
1XUK;
1Y3U;
1Y3V;
1Y3W;
1Y3X;
1Y3Y;
1Y59;
1Y5A;
1Y5B;
1Y5U;
1YP9;
1YYY;
1ZR0;
1ZZZ;
2A7H;
2AGE;
2AGG;
2AGI;
2AH4;
2AYW;
2BLV;
2BLW;
2BTC;
2BY5;
2BY6;
2BY7;
2BY8;
2BY9;
2BYA;
2BZA;
2CMY;
2D8W;
2F3C;
2FI3;
2FI4;
2FI5;
2FTL;
2FTM;
2FX4;
2FX6;
2G55;
2G5N;
2G5V;
2G81;
2G8T;
2ILN;
2J9N;
2O9Q;
2OTV;
2OXS;
2PLX;
2PTC;
2PTN;
2QN5;
2QYI;
2TGA;
2TGD;
2TGP;
2TGT;
2TIO;
2TLD;
2TPI;
2UUY;
2XTT;
2ZDK;
2ZDL;
2ZDM;
2ZDN;
2ZFS;
2ZFT;
2ZHD;
2ZQ1;
2ZQ2;
3A7T;
3A7V;
3A7W;
3A7X;
3A7Y;
3A7Z;
3A80;
3A81;
3A82;
3A83;
3A84;
3A85;
3A86;
3A87;
3A88;
3A89;
3A8A;
3A8B;
3A8C;
3A8D;
3AAS;
3AAU;
3AAV;
3ATI;
3ATK;
3ATL;
3ATM;
3BTD;
3BTE;
3BTF;
3BTG;
3BTH;
3BTK;
3BTM;
3BTQ;
3BTT;
3BTW;
3D65;
3E8L;
3GY2;
3GY3;
3GY4;
3GY5;
3GY6;
3GY7;
3GY8;
3I29;
3ITI;
3LJJ;
3LJO;
3M35;
3M7Q;
3MFJ;
3MI4;
3NK8;
3NKK;
3OTJ;
3PLB;
3PLK;
3PLP;
3PM3;
3PMJ;
3PTB;
3PTN;
3PWB;
3PWC;
3PYH;
3Q00;
3QK1;
3RDZ;
3RU4;
3RXA;
3RXB;
3RXC;
3RXD;
3RXE;
3RXF;
3RXG;
3RXH;
3RXI;
3RXJ;
3RXK;
3RXL;
3RXM;
3RXO;
3RXP;
3RXQ;
3RXR;
3RXS;
3RXT;
3RXU;
3RXV;
3T25;
3T26;
3T27;
3T28;
3T29;
3TPI;
3UNQ;
3UNR;
3UNS;
3UOP;
3UPE;
3UQO;
3UQV;
3UUZ;
3UWI;
3UY9;
3V0X;
3V12;
3V13;
3VEQ;
3VPK;
4AB8;
4AB9;
4ABA;
4ABB;
4ABD;
4ABE;
4ABF;
4ABG;
4ABH;
4ABI;
4ABJ;
4AOQ;
4AOR;
4B1T;
4B2A;
4B2B;
4B2C;
4GUX;
4HGC;
4I8G;
4I8H;
4I8J;
4I8K;
4I8L;
4J2Y;
4KTS;
4KTU;
4MTB;
4NCY;
4NIV;
4NIW;
4NIX;
4NIY;
4TPI;
4TPY;
4U2W;
4XOJ;
4Y0Y;
4Y0Z;
4Y10;
4Y11;
4YTA;
5EG4;
5F6M;
5FXL;
5GIB;
5GXP;
5JYI;
5K7R;
5LGO;
5LH4;
5LH8;
5MN1;
5MNA;
5MNB;
5MNC;
5MNE;
5MNF;
5MNG;
5MNH;
5MNK;
5MNL;
5MNM;
5MNN;
5MNO;
5MNP;
5MNQ;
5MNX;
5MNY;
5MNZ;
5MO0;
5MO1;
5MO2;
5MON;
5MOO;
5MOP;
5MOQ;
5MOR;
5MOS;
5PTP;
5T3H;
6AVL;
6B6N;
6B6O;
6B6P;
6B6Q;
6B6R;
6B6S;
6B6T;
6BFP;
6BVH;
6DWF;
6DWH;
6DWR;
6DWU;
6DZF;
6E5M;
6EAT;
6EAU;
6EAV;
6EAW;
6EAX;
6FID;
6MRQ;
6QIH;
6QL0;
6SUX;
6SV0;
6SV6;
6SV8;
6SV9;
6SVB;
6SVD;
6SVG;
6SVI;
6SVJ;
6SVN;
6SVR;
6SVU;
6SVV;
6SVW;
6SVX;
6SVZ;
6SW0;
6SWV;
6SY3;
6T0M;
6T0P;
6T5W;
6T9U;
6T9V;
6U22;
6VXY;
6XYG;
6XYK;
6YDY;
6YIS;
6YIT;
6YIU;
6YIV;
6YIW;
6YIX;
6YIY;
6YZA;
6YZC;
6ZFJ;
6ZFK;
6ZQ2;
7AL8;
7AYS;
7BRV;
7BRW;
7BRX;
7BRY;
7BRZ;
7BS0;
7BS1;
7BS2;
7BS3;
7BS4;
7BS5;
7BS6;
7BS7;
7BS8;
7BS9;
7BSA;
7JR1;
7JR2;
7JWX;
|
Mapped Pubmed ID |
10089404;
10222201;
10390350;
10417407;
10447205;
10497030;
10512718;
10524768;
10531473;
10651279;
10772864;
10779411;
10926503;
10966741;
11152605;
11257512;
11264577;
11292354;
11342132;
11676542;
11731301;
11738605;
11881991;
11921406;
12061878;
12575941;
12742021;
12860985;
12930148;
14568540;
14640539;
14729347;
15044735;
15081015;
15380220;
1557349;
1584773;
15932872;
16081330;
16131756;
16131760;
16321984;
16374786;
16421442;
16510975;
16636277;
16681368;
16754971;
17142058;
17142290;
17157870;
17191291;
17327674;
17372355;
17391695;
18084102;
18692070;
1879520;
19407425;
19461582;
19461845;
19640842;
19822883;
19851024;
20202854;
20356563;
20886466;
21097875;
21111747;
21245536;
21387509;
21698291;
21707922;
22115549;
22187139;
22194335;
2226434;
22374650;
2252895;
22683792;
22709512;
22751665;
22975140;
23161653;
23275169;
23626794;
23897468;
24034223;
24169696;
24520050;
24591244;
24598736;
24798798;
24816088;
25003390;
25003391;
25546528;
26027487;
2614845;
26212347;
27035972;
27280436;
27476144;
27487827;
27841370;
28192420;
28371253;
2914611;
29449928;
29979188;
30177695;
30198901;
3032921;
30644845;
30668585;
30817908;
30876891;
31848402;
32011145;
32270580;
32381789;
33399553;
34094189;
34342281;
6207021;
668890;
6712567;
7169635;
7498454;
7548040;
7599119;
7634078;
7798176;
8605148;
864704;
8845765;
8939944;
9300481;
9341205;
9383379;
9468142;
9724521;
9836602;
9876114;
9920392;
|
Motif |
|
Gene Encoded By |
|
Mass |
25,785 |
Kinetics |
|
Metal Binding |
METAL 75; /note=Calcium; METAL 77; /note=Calcium; via carbonyl oxygen; METAL 80; /note=Calcium; via carbonyl oxygen; METAL 85; /note=Calcium |
Rhea ID |
|
Cross Reference Brenda |
3.4.21.4; |