ID   TRY2_XENLA              Reviewed;         244 AA.
AC   P70059;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Trypsin;
DE            EC=3.4.21.4;
DE   Flags: Precursor;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang K., Lytle L., Gan L., Hood L.E.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
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; U72330; AAB17274.1; -; mRNA.
DR   RefSeq; XP_018080424.1; XM_018224935.1.
DR   AlphaFoldDB; P70059; -.
DR   SMR; P70059; -.
DR   MEROPS; S01.126; -.
DR   DNASU; 397853; -.
DR   GeneID; 397853; -.
DR   KEGG; xla:397853; -.
DR   AGR; Xenbase:XB-GENE-5776767; -.
DR   CTD; 397853; -.
DR   Xenbase; XB-GENE-5776767; prss1.L.
DR   OMA; QKVIKHP; -.
DR   OrthoDB; 4629979at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 397853; Expressed in pancreas and 8 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24264:SF15; RIKEN CDNA 2210010C04 GENE; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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..21
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028235"
FT   CHAIN           22..244
FT                   /note="Trypsin"
FT                   /id="PRO_0000028236"
FT   DOMAIN          22..242
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        61
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        105
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        198
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            192
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        46..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        130..231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        137..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        169..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        194..218
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   244 AA;  26080 MW;  C63F29CB3300B323 CRC64;
     MKFLVILVLL GAAVAFEDDD KIVGGFTCAK NAVPYQVSLN AGYHFCGGSL INSQWVVSAA
     HCYKSRIQVR LGEHNIALNE GTEQFIDSQK VIKHPNYNSR NLDNDIMLIK LSTTARLSAN
     IQSVPLPSAC ASAGTNCLIS GWGNTLSSGT NYPDLLQCLN APILTDSQCS NSYPGEITKN
     MFCAGFLAGG KDSCQGDSGG PVVCNGQLQG VVSWGYGCAQ RNYPGVYTKV CNFVTWIQST
     ISSN
//