ID   TRY2_CHICK              Reviewed;         248 AA.
AC   Q90628;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Trypsin I-P38;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=7733885; DOI=10.1042/bj3070471;
RA   Wang K., Gan L., Lee I., Hood L.E.;
RT   "Isolation and characterization of the chicken trypsinogen gene family.";
RL   Biochem. J. 307:471-479(1995).
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   -!- TISSUE SPECIFICITY: High levels are seen in the pancreas while lower
CC       levels are found in the liver, spleen and thymus.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; U15156; AAA79913.1; -; mRNA.
DR   PIR; S55067; S55067.
DR   AlphaFoldDB; Q90628; -.
DR   SMR; Q90628; -.
DR   STRING; 9031.ENSGALP00000016613; -.
DR   VEuPathDB; HostDB:geneid_396345; -.
DR   SABIO-RK; Q90628; -.
DR   Proteomes; UP000000539; 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                   /evidence="ECO:0000250"
FT   PROPEP          16..25
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028221"
FT   CHAIN           26..248
FT                   /note="Trypsin I-P38"
FT                   /id="PRO_0000028222"
FT   DOMAIN          26..246
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        109
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            196
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        134..235
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        141..208
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        173..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        198..222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   248 AA;  26088 MW;  78B79DD6FE15F0CE CRC64;
     MKFLVLVAFL GVAVAFPISD EDDDKIVGGY SCARSAAPYQ VSLNSGYHFC GGSLISSQWV
     LSAAHCYKSS IQVKLGEYNL AAQDGSEQTI SSSKVIRHSG YNANTLNNDI MLIKLSKAAT
     LNSYVNTVPL PTSCVTAGTT CLISGWGNTL SSGSLYPDVL QCLNAPVLSS SQCSSAYPGR
     ITSNMICIGY LNGGKDSCQG DSGGPVVCNG QLQGFVSWGI GCAQKGYPGV YTKVCNYVSW
     IKTTMSSN