(data stored in ACNUC3659 zone)

HOVERGEN: 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   13-OCT-2009, entry version 56.
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; Mesobatrachia; Pipoidea; Pipidae;
OC   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: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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CC   -!- GENE_FAMILY: HBG013304 [ FAMILY / ALN / TREE ]
DR   EMBL; U72330; AAB17274.1; -; mRNA.
DR   UniGene; Xl.1858; -.
DR   HSSP; P00760; 1EZX.
DR   SMR; P70059; 22-244.
DR   MEROPS; S01.126; -.
DR   Xenbase; XB-FEAT-5776261; prss1.
DR   HOVERGEN; P70059; -.
DR   BRENDA; 3.4.21.4; 648.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium 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   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 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;
DR   PRODOM; P70059.
DR   SWISS-2DPAGE; P70059.
KW   Calcium; Digestion; Disulfide bond; Hydrolase; Metal-binding;
KW   Protease; Secreted; Serine protease; Signal; Zymogen.
FT   DOMAIN        3     61       PRODOM:2005.1:PD474467  1445
FT   DOMAIN       67    110       PRODOM:2005.1:PD331626  438
FT   DOMAIN      111    145       PRODOM:2005.1:PD701657  461
FT   DOMAIN      153    185       PRODOM:2005.1:PD251054  232
FT   DOMAIN      189    239       PRODOM:2005.1:PD000068  1525
FT   SIGNAL        1     15       By similarity.
FT   PROPEP       16     21       Activation peptide (By similarity).
FT                                /FTId=PRO_0000028235.
FT   CHAIN        22    244       Trypsin.
FT                                /FTId=PRO_0000028236.
FT   DOMAIN       22    242       Peptidase S1.
FT   ACT_SITE     61     61       Charge relay system (By similarity).
FT   ACT_SITE    105    105       Charge relay system (By similarity).
FT   ACT_SITE    198    198       Charge relay system (By similarity).
FT   METAL        73     73       Calcium (By similarity).
FT   METAL        75     75       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        83     83       Calcium (By similarity).
FT   SITE        192    192       Required for specificity (By similarity).
FT   DISULFID     28    158       By similarity.
FT   DISULFID     46     62       By similarity.
FT   DISULFID    130    231       By similarity.
FT   DISULFID    137    204       By similarity.
FT   DISULFID    169    183       By similarity.
FT   DISULFID    194    218       By similarity.
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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