TRY2_BOVIN
ID TRY2_BOVIN Reviewed; 247 AA.
AC Q29463;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Anionic trypsin;
DE EC=3.4.21.4;
DE Flags: Precursor;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein-Friesian; TISSUE=Pancreas;
RX PubMed=1701147; DOI=10.1111/j.1432-1033.1990.tb19398.x;
RA le Huerou I., Wicker C., Guilloteau P., Toullec R., Puigserver A.;
RT "Isolation and nucleotide sequence of cDNA clone for bovine pancreatic
RT anionic trypsinogen. Structural identity within the trypsin family.";
RL Eur. J. Biochem. 193:767-773(1990).
RN [2]
RP ABSENCE OF SULFATED TYROSINE.
RX PubMed=17087724; DOI=10.1111/j.1742-4658.2006.05501.x;
RA Sahin-Toth M., Kukor Z., Nemoda Z.;
RT "Human cationic trypsinogen is sulfated on Tyr154.";
RL FEBS J. 273:5044-5050(2006).
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 -!- PTM: Not sulfated on tyrosine residue(s).
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; X54703; CAA38513.1; -; mRNA.
DR PIR; S13813; S13813.
DR AlphaFoldDB; Q29463; -.
DR SMR; Q29463; -.
DR STRING; 9913.ENSBTAP00000028731; -.
DR BindingDB; Q29463; -.
DR ChEMBL; CHEMBL4472; -.
DR MEROPS; S01.120; -.
DR PaxDb; Q29463; -.
DR PRIDE; Q29463; -.
DR eggNOG; KOG3627; Eukaryota.
DR Proteomes; UP000009136; 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 /evidence="ECO:0000255"
FT PROPEP 16..23
FT /note="Activation peptide"
FT /id="PRO_0000028189"
FT CHAIN 24..247
FT /note="Anionic trypsin"
FT /id="PRO_0000028190"
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 ACT_SITE 107
FT /note="Charge relay system"
FT ACT_SITE 200
FT /note="Charge relay system"
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 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; 26290 MW; 50A070495A7731DB CRC64;
MHPLLILAFV GAAVAFPSDD DDKIVGGYTC AENSVPYQVS LNAGYHFCGG SLINDQWVVS
AAHCYQYHIQ VRLGEYNIDV LEGGEQFIDA SKIIRHPKYS SWTLDNDILL IKLSTPAVIN
ARVSTLLLPS ACASAGTECL ISGWGNTLSS GVNYPDLLQC LVAPLLSHAD CEASYPGQIT
NNMICAGFLE GGKDSCQGDS GGPVACNGQL QGIVSWGYGC AQKGKPGVYT KVCNYVDWIQ
ETIAANS
