ID TRY2_RAT Reviewed; 246 AA. AC P00763; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 24-JAN-2024, entry version 208. DE RecName: Full=Anionic trypsin-2; DE EC=3.4.21.4; DE AltName: Full=Anionic trypsin II; DE AltName: Full=Pretrypsinogen II; DE AltName: Full=Serine protease 2; DE Flags: Precursor; GN Name=Prss2; Synonyms=Try2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6094547; DOI=10.1016/s0021-9258(18)89886-6; RA Craik C.S., Choo Q.L., Swift G.H., Quinto C., MacDonald R.J., Rutter W.J.; RT "Structure of two related rat pancreatic trypsin genes."; RL J. Biol. Chem. 259:14255-14264(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 9-246. RC STRAIN=Sprague-Dawley; TISSUE=Pancreas; RX PubMed=6896710; DOI=10.1016/s0021-9258(18)34133-4; RA MacDonald R.J., Stary S.J., Swift G.H.; RT "Two similar but nonallelic rat pancreatic trypsinogens. Nucleotide RT sequences of the cloned cDNAs."; RL J. Biol. Chem. 257:9724-9732(1982). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=3112942; DOI=10.1126/science.3112942; RA Sprang S., Standing T., Fletterick R.J., Stroud R.M., Finer-Moore J., RA Xuong N.-H., Hamlin R., Rutter W.J., Craik C.S.; RT "The three-dimensional structure of Asn102 mutant of trypsin: role of RT Asp102 in serine protease catalysis."; RL Science 237:905-909(1987). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS). RX PubMed=1881877; DOI=10.1002/prot.340100303; RA Earnest T., Fauman E., Craik C.S., Stroud R.; RT "1.59-A structure of trypsin at 120 K: comparison of low temperature and RT room temperature structures."; RL Proteins 10:171-187(1991). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=8634241; DOI=10.1021/bi9530200; RA Brinen L.S., Willett W.S., Craik C.S., Fletterick R.J.; RT "X-ray structures of a designed binding site in trypsin show metal- RT dependent geometry."; RL Biochemistry 35:5999-6009(1996). 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 -!- INTERACTION: CC P00763; P23827: eco; Xeno; NbExp=2; IntAct=EBI-1029166, EBI-1029159; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V01274; CAA24581.1; -; mRNA. DR EMBL; L00131; AAA98517.1; -; mRNA. DR EMBL; L00130; AAA98517.1; JOINED; Genomic_DNA. DR PIR; A22657; TRRT2. DR RefSeq; NP_036861.1; NM_012729.2. DR PDB; 1AMH; X-ray; 2.50 A; A/B=24-246. DR PDB; 1ANB; X-ray; 2.80 A; A=24-246. DR PDB; 1ANC; X-ray; 2.20 A; A=24-246. DR PDB; 1AND; X-ray; 2.30 A; A=24-246. DR PDB; 1ANE; X-ray; 2.20 A; A=24-246. DR PDB; 1BRA; X-ray; 2.20 A; A=24-246. DR PDB; 1BRB; X-ray; 2.10 A; E=24-246. DR PDB; 1BRC; X-ray; 2.50 A; E=24-246. DR PDB; 1CO7; X-ray; 1.90 A; E=2-246. DR PDB; 1DPO; X-ray; 1.59 A; A=24-246. DR PDB; 1EZS; X-ray; 2.30 A; C/D=24-246. DR PDB; 1EZU; X-ray; 2.40 A; C/D=24-246. DR PDB; 1F5R; X-ray; 1.65 A; A=15-246. DR PDB; 1F7Z; X-ray; 1.55 A; A=15-246. DR PDB; 1FY8; X-ray; 1.70 A; E=15-246. DR PDB; 1J14; X-ray; 2.40 A; A=24-246. DR PDB; 1J15; X-ray; 2.00 A; A=24-246. DR PDB; 1J16; X-ray; 1.60 A; A=24-246. DR PDB; 1J17; X-ray; 2.00 A; T=24-246. DR PDB; 1K9O; X-ray; 2.30 A; E=24-246. DR PDB; 1QL9; X-ray; 2.30 A; A=24-246. DR PDB; 1SLU; X-ray; 1.80 A; B=24-246. DR PDB; 1SLV; X-ray; 2.30 A; B=24-246. DR PDB; 1SLW; X-ray; 2.00 A; B=24-246. DR PDB; 1SLX; X-ray; 2.20 A; B=24-246. DR PDB; 1TRM; X-ray; 2.30 A; A/B=24-246. DR PDB; 1YKT; X-ray; 1.70 A; A=24-246. DR PDB; 1YLC; X-ray; 1.70 A; A=24-246. DR PDB; 1YLD; X-ray; 1.70 A; A=24-246. DR PDB; 2TRM; X-ray; 2.80 A; A=24-246. DR PDB; 3FP6; X-ray; 1.49 A; E=24-246. DR PDB; 3FP7; X-ray; 1.46 A; E=24-246. DR PDB; 3FP8; X-ray; 1.46 A; E=24-246. DR PDB; 3TGI; X-ray; 1.80 A; E=24-246. DR PDB; 3TGJ; X-ray; 2.20 A; E=15-246. DR PDB; 3TGK; X-ray; 1.70 A; E=15-246. DR PDBsum; 1AMH; -. DR PDBsum; 1ANB; -. DR PDBsum; 1ANC; -. DR PDBsum; 1AND; -. DR PDBsum; 1ANE; -. DR PDBsum; 1BRA; -. DR PDBsum; 1BRB; -. DR PDBsum; 1BRC; -. DR PDBsum; 1CO7; -. DR PDBsum; 1DPO; -. DR PDBsum; 1EZS; -. DR PDBsum; 1EZU; -. DR PDBsum; 1F5R; -. DR PDBsum; 1F7Z; -. DR PDBsum; 1FY8; -. DR PDBsum; 1J14; -. DR PDBsum; 1J15; -. DR PDBsum; 1J16; -. DR PDBsum; 1J17; -. DR PDBsum; 1K9O; -. DR PDBsum; 1QL9; -. DR PDBsum; 1SLU; -. DR PDBsum; 1SLV; -. DR PDBsum; 1SLW; -. DR PDBsum; 1SLX; -. DR PDBsum; 1TRM; -. DR PDBsum; 1YKT; -. DR PDBsum; 1YLC; -. DR PDBsum; 1YLD; -. DR PDBsum; 2TRM; -. DR PDBsum; 3FP6; -. DR PDBsum; 3FP7; -. DR PDBsum; 3FP8; -. DR PDBsum; 3TGI; -. DR PDBsum; 3TGJ; -. DR PDBsum; 3TGK; -. DR AlphaFoldDB; P00763; -. DR SMR; P00763; -. DR BioGRID; 247129; 1. DR DIP; DIP-6112N; -. DR IntAct; P00763; 2. DR MINT; P00763; -. DR STRING; 10116.ENSRNOP00000018853; -. DR BindingDB; P00763; -. DR ChEMBL; CHEMBL4290; -. DR MEROPS; S01.119; -. DR iPTMnet; P00763; -. DR PhosphoSitePlus; P00763; -. DR PaxDb; 10116-ENSRNOP00000018853; -. DR Ensembl; ENSRNOT00000095908.1; ENSRNOP00000082459.1; ENSRNOG00000064731.1. DR GeneID; 25052; -. DR KEGG; rno:25052; -. DR UCSC; RGD:3418; rat. DR AGR; RGD:3418; -. DR CTD; 5645; -. DR RGD; 3418; Prss2. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT01050000244883; -. DR HOGENOM; CLU_006842_7_0_1; -. DR InParanoid; P00763; -. DR OMA; HPRYSSW; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; P00763; -. DR Reactome; R-RNO-1442490; Collagen degradation. DR Reactome; R-RNO-1462054; Alpha-defensins. DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases. DR Reactome; R-RNO-6798695; Neutrophil degranulation. DR Reactome; R-RNO-6803157; Antimicrobial peptides. DR SABIO-RK; P00763; -. DR EvolutionaryTrace; P00763; -. DR PRO; PR:P00763; -. DR Proteomes; UP000002494; Chromosome 4. DR Bgee; ENSRNOG00000032916; Expressed in pancreas and 10 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB. DR GO; GO:0030574; P:collagen catabolic process; ISS:UniProtKB. DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB. DR GO; GO:0007584; P:response to nutrient; IEP:RGD. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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 PANTHER; PTHR24264:SF10; PROTEASE, SERINE 1 (TRYPSIN 1)-RELATED; 1. DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR Genevisible; P00763; RN. 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 PROPEP 16..23 FT /note="Activation peptide" FT /id="PRO_0000028209" FT CHAIN 24..246 FT /note="Anionic trypsin-2" FT /id="PRO_0000028210" FT DOMAIN 24..244 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 63 FT /note="Charge relay system" FT ACT_SITE 107 FT /note="Charge relay system" FT ACT_SITE 200 FT /note="Charge relay system" FT BINDING 75 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 80 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 85 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT SITE 194 FT /note="Required for specificity" FT /evidence="ECO:0000250" FT DISULFID 30..160 FT DISULFID 48..64 FT DISULFID 132..233 FT DISULFID 139..206 FT DISULFID 171..185 FT DISULFID 196..220 FT CONFLICT 84 FT /note="N -> D (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 88 FT /note="V -> I (in Ref. 1)" FT /evidence="ECO:0000305" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:1SLW" FT STRAND 38..54 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:3FP7" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 70..74 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:1SLU" FT STRAND 86..95 FT /evidence="ECO:0007829|PDB:3FP7" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 109..115 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:3FP8" FT STRAND 138..145 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 159..165 FT /evidence="ECO:0007829|PDB:3FP7" FT HELIX 168..174 FT /evidence="ECO:0007829|PDB:3FP7" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 183..187 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:3FP7" FT TURN 197..201 FT /evidence="ECO:0007829|PDB:1TRM" FT STRAND 203..206 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 209..216 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:3FP7" FT STRAND 227..231 FT /evidence="ECO:0007829|PDB:3FP7" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:3FP7" FT HELIX 236..245 FT /evidence="ECO:0007829|PDB:3FP7" SQ SEQUENCE 246 AA; 26228 MW; A8D3630809AEE606 CRC64; MRALLFLALV GAAVAFPVDD DDKIVGGYTC QENSVPYQVS LNSGYHFCGG SLINDQWVVS AAHCYKSRIQ VRLGEHNINV LEGNEQFVNA AKIIKHPNFD RKTLNNDIML IKLSSPVKLN ARVATVALPS SCAPAGTQCL ISGWGNTLSS GVNEPDLLQC LDAPLLPQAD CEASYPGKIT DNMVCVGFLE GGKDSCQGDS GGPVVCNGEL QGIVSWGYGC ALPDNPGVYT KVCNYVDWIQ DTIAAN //