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   03-AUG-2022, entry version 146.
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; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3841794; DOI=10.1128/mcb.5.10.2669-2676.1985;
RA   Pinsky S.D., Laforge K.S., Scheele G.;
RT   "Differential regulation of trypsinogen mRNA translation: full-length mRNA
RT   sequences encoding two oppositely charged trypsinogen isoenzymes in the dog
RT   pancreas.";
RL   Mol. Cell. Biol. 5:2669-2676(1985).
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}.
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DR   EMBL; M11589; AAA30899.1; -; mRNA.
DR   PIR; A26273; TRDG.
DR   RefSeq; XP_003432104.1; XM_003432056.2.
DR   AlphaFoldDB; P06872; -.
DR   SMR; P06872; -.
DR   STRING; 9612.ENSCAFP00000021363; -.
DR   MEROPS; S01.120; -.
DR   PaxDb; P06872; -.
DR   PRIDE; P06872; -.
DR   GeneID; 100686744; -.
DR   KEGG; cfa:100686744; -.
DR   CTD; 5645; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   InParanoid; P06872; -.
DR   OMA; QCEAAYP; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF331065; -.
DR   Proteomes; UP000002254; Unplaced.
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   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..23
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028193"
FT   CHAIN           24..247
FT                   /note="Anionic trypsin"
FT                   /id="PRO_0000028194"
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                   /evidence="ECO:0000250"
FT   ACT_SITE        107
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        200
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            194
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        48..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        132..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        139..206
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        171..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        196..220
FT                   /evidence="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