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Database: UniProt/SWISS-PROT
Entry: TRY2_CANLF
LinkDB: TRY2_CANLF
Original site: TRY2_CANLF 
ID   TRY2_CANLF              Reviewed;         247 AA.
AC   P06872;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   07-NOV-2018, entry version 132.
DE   RecName: Full=Anionic trypsin;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3841794; DOI=10.1128/MCB.5.10.2669;
RA   Pinsky S.D., Laforge K.S., Scheele G.;
RT   "Differential regulation of trypsinogen mRNA translation: full-length
RT   mRNA sequences encoding two oppositely charged trypsinogen isoenzymes
RT   in the dog pancreas.";
RL   Mol. Cell. Biol. 5:2669-2676(1985).
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; M11589; AAA30899.1; -; mRNA.
DR   PIR; A26273; TRDG.
DR   RefSeq; XP_003432104.1; XM_003432056.2.
DR   ProteinModelPortal; P06872; -.
DR   SMR; P06872; -.
DR   STRING; 9615.ENSCAFP00000021363; -.
DR   MEROPS; S01.120; -.
DR   PaxDb; P06872; -.
DR   PRIDE; P06872; -.
DR   Ensembl; ENSCAFT00000022998; ENSCAFP00000021363; ENSCAFG00000014481.
DR   GeneID; 100686744; -.
DR   KEGG; cfa:100686744; -.
DR   CTD; 5645; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00760000118862; -.
DR   HOGENOM; HOG000251820; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P06872; -.
DR   KO; K01312; -.
DR   OMA; GGQKVPQ; -.
DR   OrthoDB; EOG091G0DF7; -.
DR   TreeFam; TF331065; -.
DR   Reactome; R-CFA-1442490; Collagen degradation.
DR   Reactome; R-CFA-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-CFA-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
DR   Reactome; R-CFA-6798695; Neutrophil degranulation.
DR   Reactome; R-CFA-6803157; Antimicrobial peptides.
DR   Proteomes; UP000002254; Chromosome 16.
DR   Bgee; ENSCAFG00000014481; Expressed in 1 organ(s), highest expression level in liver.
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   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     23       Activation peptide.
FT                                /FTId=PRO_0000028193.
FT   CHAIN        24    247       Anionic trypsin.
FT                                /FTId=PRO_0000028194.
FT   DOMAIN       24    244       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     63     63       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    107    107       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    200    200       Charge relay system. {ECO:0000250}.
FT   METAL        75     75       Calcium. {ECO:0000250}.
FT   METAL        77     77       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        80     80       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        85     85       Calcium. {ECO:0000250}.
FT   SITE        194    194       Required for specificity. {ECO:0000250}.
FT   DISULFID     30    160       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID     48     64       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    132    233       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    139    206       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    171    185       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    196    220       {ECO:0000255|PROSITE-ProRule:PRU00274}.
SQ   SEQUENCE   247 AA;  26423 MW;  374E9D31D6DB8EAF CRC64;
     MNPLLILAFL GAAVATPTDD DDKIVGGYTC EENSVPYQVS LNAGYHFCGG SLISDQWVVS
     AAHCYKSRIQ VRLGEYNIDV LEGNEQFINS AKVIRHPNYN SWILDNDIML IKLSSPAVLN
     ARVATISLPR ACAAPGTQCL ISGWGNTLSS GTNYPELLQC LDAPILTQAQ CEASYPGQIT
     ENMICAGFLE GGKDSCQGDS GGPVVCNGEL QGIVSWGYGC AQKNKPGVYT KVCNFVDWIQ
     STIAANS
//
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