ID   TRYP_PROAT              Reviewed;          21 AA.
AC   P35051;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Trypsin;
DE            EC=3.4.21.4;
DE   Flags: Precursor; Fragment;
OS   Protopterus aethiopicus (Marbled lungfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Dipnomorpha; Ceratodontiformes; Lepidosirenoidei; Protopteridae;
OC   Protopterus.
OX   NCBI_TaxID=7886;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=11945763; DOI=10.1016/0014-5793(71)80622-1;
RA   Hermodson M.A., Tye R.W., Reeck G.R., Neurath H., Walsh K.A.;
RT   "Comparison of the amino terminal sequences of bovine, dogfish, and
RT   lungfish trypsinogens.";
RL   FEBS Lett. 14:222-224(1971).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
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   PIR; A27719; A27719.
DR   MEROPS; S01.125; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease;
KW   Zymogen.
FT   PROPEP          1..7
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028313"
FT   CHAIN           8..>21
FT                   /note="Trypsin"
FT                   /id="PRO_0000028314"
FT   DOMAIN          8..>21
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2455 MW;  88E2FB11D130729D CRC64;
     FPIEEDKIVG GYECPKHXVP W
//