##gff-version 3 P07477 UniProtKB Signal peptide 1 15 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2598466,ECO:0000269|PubMed:7945238;Dbxref=PMID:2598466,PMID:7945238 P07477 UniProtKB Propeptide 16 23 . . . ID=PRO_0000028197;Note=Activation peptide P07477 UniProtKB Chain 24 247 . . . ID=PRO_0000028198;Note=Serine protease 1 P07477 UniProtKB Chain 24 122 . . . ID=PRO_0000313570;Note=Alpha-trypsin chain 1 P07477 UniProtKB Chain 123 247 . . . ID=PRO_0000313571;Note=Alpha-trypsin chain 2 P07477 UniProtKB Domain 24 244 . . . Note=Peptidase S1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00274 P07477 UniProtKB Active site 63 63 . . . Note=Charge relay system P07477 UniProtKB Active site 107 107 . . . Note=Charge relay system P07477 UniProtKB Active site 200 200 . . . Note=Charge relay system P07477 UniProtKB Binding site 75 75 . . . . P07477 UniProtKB Binding site 77 77 . . . . P07477 UniProtKB Binding site 80 80 . . . . P07477 UniProtKB Binding site 85 85 . . . . P07477 UniProtKB Site 194 194 . . . Note=Required for specificity;Ontology_term=ECO:0000250;evidence=ECO:0000250 P07477 UniProtKB Modified residue 154 154 . . . Note=Sulfotyrosine;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:17087724,ECO:0000305|PubMed:25010489;Dbxref=PMID:17087724,PMID:25010489 P07477 UniProtKB Disulfide bond 30 160 . . . . P07477 UniProtKB Disulfide bond 48 64 . . . . P07477 UniProtKB Disulfide bond 139 206 . . . . P07477 UniProtKB Disulfide bond 171 185 . . . . P07477 UniProtKB Disulfide bond 196 220 . . . . P07477 UniProtKB Natural variant 16 16 . . . ID=VAR_011693;Note=In PCTT%3B disrupts signal sequence cleavage site. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10381903;Dbxref=dbSNP:rs202003805,PMID:10381903 P07477 UniProtKB Natural variant 22 22 . . . ID=VAR_011652;Note=In PCTT%3B increased rate of activation. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10930381;Dbxref=dbSNP:rs397507442,PMID:10930381 P07477 UniProtKB Natural variant 23 23 . . . ID=VAR_011653;Note=In PCTT%3B increased rate of activation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10204851;Dbxref=dbSNP:rs111033567,PMID:10204851 P07477 UniProtKB Natural variant 29 29 . . . ID=VAR_006720;Note=In PCTT. N->I;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11866271,ECO:0000269|PubMed:15776435,ECO:0000269|PubMed:9322498,ECO:0000269|PubMed:9633818;Dbxref=dbSNP:rs111033566,PMID:11866271,PMID:15776435,PMID:9322498,PMID:9633818 P07477 UniProtKB Natural variant 29 29 . . . ID=VAR_012712;Note=In PCTT. N->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11788572;Dbxref=dbSNP:rs111033566,PMID:11788572 P07477 UniProtKB Natural variant 54 54 . . . ID=VAR_037908;Note=In PCTT%3B associated with Ile-29%3B the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15776435;Dbxref=dbSNP:rs144422014,PMID:15776435 P07477 UniProtKB Natural variant 79 79 . . . ID=VAR_037909;Note=In PCTT%3B Lys-79 trypsin activates anionic trypsinogen PRSS2 2-fold while the common pancreatitis-associated mutants His-122 or Ile-29 have no such effect. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14695529;Dbxref=dbSNP:rs111033564,PMID:14695529 P07477 UniProtKB Natural variant 104 104 . . . ID=VAR_011654;Note=In PCTT. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11866271;Dbxref=dbSNP:rs1554499091,PMID:11866271 P07477 UniProtKB Natural variant 116 116 . . . ID=VAR_011655;Note=In PCTT. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11866271;Dbxref=dbSNP:rs387906698,PMID:11866271 P07477 UniProtKB Natural variant 122 122 . . . ID=VAR_012713;Note=In PCTT%3B suppresses an autocleavage site. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11788572;Dbxref=dbSNP:rs111033568,PMID:11788572 P07477 UniProtKB Natural variant 122 122 . . . ID=VAR_006721;Note=In PCTT%3B suppresses an autocleavage site which is probably part of a fail-safe mechanism by which trypsin%2C which is activated within the pancreas%2C may be inactivated%3B loss of this cleavage site would permit autodigestion resulting in pancreatitis. R->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10381903,ECO:0000269|PubMed:11073545,ECO:0000269|PubMed:11866271,ECO:0000269|PubMed:8841182,ECO:0000269|PubMed:9322498;Dbxref=dbSNP:rs267606982,PMID:10381903,PMID:11073545,PMID:11866271,PMID:8841182,PMID:9322498 P07477 UniProtKB Natural variant 137 137 . . . ID=VAR_036299;Note=In a colorectal cancer sample%3B somatic mutation. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=dbSNP:rs117497341,PMID:16959974 P07477 UniProtKB Natural variant 139 139 . . . ID=VAR_011656;Note=In PCTT. C->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11866271;Dbxref=PMID:11866271 P07477 UniProtKB Mutagenesis 154 154 . . . Note=Lack of sulfation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17087724;Dbxref=PMID:17087724 P07477 UniProtKB Sequence conflict 4 4 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 P07477 UniProtKB Beta strand 38 54 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 57 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Helix 62 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 70 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 76 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QE9 P07477 UniProtKB Beta strand 86 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Turn 101 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 109 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 120 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 138 144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 149 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 159 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Helix 168 174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Turn 176 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 183 187 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TRN P07477 UniProtKB Beta strand 203 206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 209 216 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 218 222 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Beta strand 227 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Helix 232 235 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3 P07477 UniProtKB Helix 236 245 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RA3