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Database: UniProt
Entry: P00763
LinkDB: P00763
Original site: P00763 
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   05-DEC-2018, entry version 183.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6094547;
RA   Craik C.S., Choo Q.L., Swift G.H., Quinto C., MacDonald R.J.,
RA   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;
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
RT   and 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.;
CC         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       P23827:eco (xeno); NbExp=2; IntAct=EBI-1029166, EBI-1029159;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   UniGene; Rn.1584; -.
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   ProteinModelPortal; P00763; -.
DR   SMR; P00763; -.
DR   DIP; DIP-6112N; -.
DR   IntAct; P00763; 2.
DR   MINT; P00763; -.
DR   STRING; 10116.ENSRNOP00000060784; -.
DR   BindingDB; P00763; -.
DR   ChEMBL; CHEMBL4290; -.
DR   MEROPS; S01.119; -.
DR   iPTMnet; P00763; -.
DR   PhosphoSitePlus; P00763; -.
DR   PaxDb; P00763; -.
DR   PRIDE; P00763; -.
DR   Ensembl; ENSRNOT00000018852; ENSRNOP00000018853; ENSRNOG00000032916.
DR   GeneID; 25052; -.
DR   KEGG; rno:25052; -.
DR   UCSC; RGD:3418; rat.
DR   CTD; 5645; -.
DR   RGD; 3418; Prss2.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000153485; -.
DR   HOGENOM; HOG000251820; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P00763; -.
DR   KO; K01312; -.
DR   OMA; GGQKVPQ; -.
DR   OrthoDB; EOG091G0DF7; -.
DR   PhylomeDB; P00763; -.
DR   Reactome; R-RNO-1442490; Collagen degradation.
DR   Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-RNO-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
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 1 organ(s), highest expression level in brain.
DR   Genevisible; P00763; RN.
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; TAS:RGD.
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   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; Disulfide bond;
KW   Hydrolase; Metal-binding; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     15
FT   PROPEP       16     23       Activation peptide.
FT                                /FTId=PRO_0000028209.
FT   CHAIN        24    246       Anionic trypsin-2.
FT                                /FTId=PRO_0000028210.
FT   DOMAIN       24    244       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     63     63       Charge relay system.
FT   ACT_SITE    107    107       Charge relay system.
FT   ACT_SITE    200    200       Charge relay system.
FT   METAL        75     75       Calcium.
FT   METAL        77     77       Calcium; via carbonyl oxygen.
FT   METAL        80     80       Calcium; via carbonyl oxygen.
FT   METAL        85     85       Calcium.
FT   SITE        194    194       Required for specificity. {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     84       N -> D (in Ref. 1). {ECO:0000305}.
FT   CONFLICT     88     88       V -> I (in Ref. 1). {ECO:0000305}.
FT   TURN         32     34       {ECO:0000244|PDB:1SLW}.
FT   STRAND       38     54       {ECO:0000244|PDB:3FP7}.
FT   STRAND       57     60       {ECO:0000244|PDB:3FP7}.
FT   HELIX        62     64       {ECO:0000244|PDB:3FP7}.
FT   STRAND       70     74       {ECO:0000244|PDB:3FP7}.
FT   STRAND       76     80       {ECO:0000244|PDB:1SLU}.
FT   STRAND       86     95       {ECO:0000244|PDB:3FP7}.
FT   TURN        101    103       {ECO:0000244|PDB:3FP7}.
FT   STRAND      109    115       {ECO:0000244|PDB:3FP7}.
FT   STRAND      120    123       {ECO:0000244|PDB:3FP8}.
FT   STRAND      138    145       {ECO:0000244|PDB:3FP7}.
FT   STRAND      149    151       {ECO:0000244|PDB:3FP7}.
FT   STRAND      159    165       {ECO:0000244|PDB:3FP7}.
FT   HELIX       168    174       {ECO:0000244|PDB:3FP7}.
FT   TURN        176    178       {ECO:0000244|PDB:3FP7}.
FT   STRAND      183    187       {ECO:0000244|PDB:3FP7}.
FT   STRAND      192    194       {ECO:0000244|PDB:3FP7}.
FT   TURN        197    201       {ECO:0000244|PDB:1TRM}.
FT   STRAND      203    206       {ECO:0000244|PDB:3FP7}.
FT   STRAND      209    216       {ECO:0000244|PDB:3FP7}.
FT   STRAND      218    221       {ECO:0000244|PDB:3FP7}.
FT   STRAND      227    231       {ECO:0000244|PDB:3FP7}.
FT   HELIX       232    234       {ECO:0000244|PDB:3FP7}.
FT   HELIX       236    245       {ECO:0000244|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
//
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