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Database: UniProt/SWISS-PROT
Entry: TRY2_XENLA
LinkDB: TRY2_XENLA
Original site: TRY2_XENLA 
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   05-DEC-2018, entry version 86.
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;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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.;
CC         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.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; U72330; AAB17274.1; -; mRNA.
DR   RefSeq; XP_018080424.1; XM_018224935.1.
DR   UniGene; Xl.1858; -.
DR   ProteinModelPortal; P70059; -.
DR   SMR; P70059; -.
DR   MEROPS; S01.126; -.
DR   PRIDE; P70059; -.
DR   GeneID; 397853; -.
DR   KEGG; xla:397853; -.
DR   CTD; 397853; -.
DR   Xenbase; XB-GENE-5776767; prss1.
DR   HOVERGEN; HBG013304; -.
DR   KO; K01312; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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;
KW   Protease; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     15       {ECO:0000250}.
FT   PROPEP       16     21       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000028235.
FT   CHAIN        22    244       Trypsin.
FT                                /FTId=PRO_0000028236.
FT   DOMAIN       22    242       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     61     61       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    105    105       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    198    198       Charge relay system. {ECO:0000250}.
FT   METAL        73     73       Calcium. {ECO:0000250}.
FT   METAL        75     75       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        83     83       Calcium. {ECO:0000250}.
FT   SITE        192    192       Required for specificity. {ECO:0000250}.
FT   DISULFID     28    158       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID     46     62       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    130    231       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    137    204       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    169    183       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    194    218       {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
//
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