TRY1_CANLF
ID TRY1_CANLF Reviewed; 246 AA.
AC P06871;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Serine protease 1 {ECO:0000250|UniProtKB:P07477};
DE EC=3.4.21.4;
DE AltName: Full=Anionic trypsin I {ECO:0000250|UniProtKB:P00762};
DE AltName: Full=Anionic trypsin-1 {ECO:0000250|UniProtKB:P00762};
DE AltName: Full=Beta-trypsin;
DE AltName: Full=Cationic trypsinogen;
DE AltName: Full=Pretrypsinogen I {ECO:0000250|UniProtKB:P00762};
DE AltName: Full=Trypsin I {ECO:0000250|UniProtKB:P07477};
DE AltName: Full=Trypsin-1;
DE Flags: Precursor;
GN Name=PRSS1 {ECO:0000250|UniProtKB:P07477};
GN Synonyms=TRP1, TRY1 {ECO:0000250|UniProtKB:P07477}, TRYP1;
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 -!- SUBUNIT: Interacts with SERPINA1. {ECO:0000250|UniProtKB:P00760}.
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; M11590; AAA30900.1; -; mRNA.
DR PIR; B26273; TRDGC.
DR AlphaFoldDB; P06871; -.
DR SMR; P06871; -.
DR STRING; 9612.ENSCAFP00000005682; -.
DR MEROPS; S01.151; -.
DR PaxDb; P06871; -.
DR PRIDE; P06871; -.
DR eggNOG; KOG3627; Eukaryota.
DR Proteomes; UP000002254; 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..23
FT /note="Activation peptide"
FT /id="PRO_0000028191"
FT CHAIN 24..246
FT /note="Serine protease 1"
FT /id="PRO_0000028192"
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 246 AA; 26170 MW; E9E5A1DE2391BBBB CRC64;
MKTFIFLALL GATVAFPIDD DDKIVGGYTC SRNSVPYQVS LNSGYHFCGG SLINSQWVVS
AAHCYKSRIQ VRLGEYNIAV SEGGEQFINA AKIIRHPRYN ANTIDNDIML IKLSSPATLN
SRVSAIALPK SCPAAGTQCL ISGWGNTQSI GQNYPDVLQC LKAPILSDSV CRNAYPGQIS
SNMMCLGYME GGKDSCQGDS GGPVVCNGEL QGVVSWGAGC AQKGKPGVSP KVCKYVSWIQ
QTIAAN
