TRY3_RAT
ID TRY3_RAT Reviewed; 247 AA.
AC P08426;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cationic trypsin-3;
DE EC=3.4.21.4;
DE AltName: Full=Cationic trypsin III;
DE AltName: Full=Pretrypsinogen III;
DE Flags: Precursor;
GN Name=Try3;
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 [MRNA].
RX PubMed=3607011; DOI=10.1021/bi00385a020;
RA Fletcher T.S., Alhadeff M., Craik C.S., Largman C.;
RT "Isolation and characterization of a cDNA encoding rat cationic
RT trypsinogen.";
RL Biochemistry 26:3081-3086(1987).
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; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
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; M16624; AAA41985.1; -; mRNA.
DR PIR; A27547; A27547.
DR RefSeq; NP_775150.1; NM_173127.1.
DR AlphaFoldDB; P08426; -.
DR SMR; P08426; -.
DR BioGRID; 251902; 1.
DR STRING; 10116.ENSRNOP00000018042; -.
DR MEROPS; S01.151; -.
DR PhosphoSitePlus; P08426; -.
DR jPOST; P08426; -.
DR PaxDb; P08426; -.
DR PRIDE; P08426; -.
DR GeneID; 286911; -.
DR KEGG; rno:286911; -.
DR UCSC; RGD:708437; rat.
DR CTD; 286911; -.
DR RGD; 708437; LOC286911.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P08426; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P08426; -.
DR PRO; PR:P08426; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Digestion; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..15
FT PROPEP 16..24
FT /note="Activation peptide"
FT /id="PRO_0000028211"
FT CHAIN 25..247
FT /note="Cationic trypsin-3"
FT /id="PRO_0000028212"
FT DOMAIN 25..245
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 108
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Required for specificity"
FT /evidence="ECO:0000250"
FT DISULFID 31..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 49..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 133..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 140..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 172..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 197..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 247 AA; 26269 MW; D74892BAA584E4A8 CRC64;
MKALIFLAFL GAAVALPLDD DDDKIVGGYT CQKNSLPYQV SLNAGYHFCG GSLINSQWVV
SAAHCYKSRI QVRLGEHNID VVEGGEQFID AAKIIRHPSY NANTFDNDIM LIKLNSPATL
NSRVSTVSLP RSCGSSGTKC LVSGWGNTLS SGTNYPSLLQ CLDAPVLSDS SCKSSYPGKI
TSNMFCLGFL EGGKDSCQGD SGGPVVCNGQ LQGVVSWGYG CAQKGKPGVY TKVCNYVNWI
QQTVAAN
