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Database: UniProt/SWISS-PROT
Entry: TRY3_RAT
LinkDB: TRY3_RAT
Original site: 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   10-OCT-2018, entry version 127.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
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.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; M16624; AAA41985.1; -; mRNA.
DR   PIR; A27547; A27547.
DR   RefSeq; NP_775150.1; NM_173127.1.
DR   UniGene; Rn.9817; -.
DR   ProteinModelPortal; P08426; -.
DR   SMR; P08426; -.
DR   BioGrid; 251902; 1.
DR   STRING; 10116.ENSRNOP00000018042; -.
DR   MEROPS; S01.151; -.
DR   PhosphoSitePlus; P08426; -.
DR   PaxDb; P08426; -.
DR   PRIDE; P08426; -.
DR   GeneID; 286911; -.
DR   KEGG; rno:286911; -.
DR   UCSC; RGD:708437; rat.
DR   CTD; 5646; -.
DR   RGD; 708437; LOC286911.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251820; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P08426; -.
DR   KO; K01312; -.
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   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   2: Evidence at transcript level;
KW   Calcium; Complete proteome; Digestion; Disulfide bond; Hydrolase;
KW   Metal-binding; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     15
FT   PROPEP       16     24       Activation peptide.
FT                                /FTId=PRO_0000028211.
FT   CHAIN        25    247       Cationic trypsin-3.
FT                                /FTId=PRO_0000028212.
FT   DOMAIN       25    245       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     64     64       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    108    108       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    201    201       Charge relay system. {ECO:0000250}.
FT   METAL        76     76       Calcium. {ECO:0000250}.
FT   METAL        78     78       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        81     81       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        86     86       Calcium. {ECO:0000250}.
FT   SITE        195    195       Required for specificity. {ECO:0000250}.
FT   DISULFID     31    161       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID     49     65       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    133    234       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    140    207       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    172    186       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    197    221       {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
//
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