TRY2_RAT
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 03-AUG-2022, entry version 200.
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}.
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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; P00763; -.
DR PRIDE; P00763; -.
DR Ensembl; ENSRNOT00000095908; ENSRNOP00000082459; ENSRNOG00000064731.
DR GeneID; 25052; -.
DR KEGG; rno:25052; -.
DR UCSC; RGD:3418; rat.
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; QCEAAYP; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P00763; -.
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 tissues.
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 Gene3D; 2.40.10.10; -; 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 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; 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
