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TRP3_PSEAM
ID   TRP3_PSEAM              Reviewed;         256 AA.
AC   O93267;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Trypsinogen-like protein 3;
DE   Flags: Precursor;
GN   Name=trp3;
OS   Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC   Pseudopleuronectes.
OX   NCBI_TaxID=8265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Intestine;
RX   PubMed=9852613;
RA   Douglas S.E., Gallant J.W.;
RT   "Isolation of cDNAs for trypsinogen from the winter flounder, Pleuronectes
RT   americanus.";
RL   J. Mar. Biotechnol. 6:214-219(1998).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- CAUTION: Has lost all three of the essential catalytic residues and so
CC       probably has no enzymatic activity. {ECO:0000305}.
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DR   EMBL; AF012464; AAC32753.1; -; mRNA.
DR   AlphaFoldDB; O93267; -.
DR   SMR; O93267; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Serine protease homolog; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..256
FT                   /note="Trypsinogen-like protein 3"
FT                   /id="PRO_0000028448"
FT   DOMAIN          15..237
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        23..153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        41..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        125..226
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        132..199
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        164..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        189..213
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   256 AA;  28525 MW;  68BA7D9265595587 CRC64;
     MILLLVLALG LAGASPLGEY KECPPHSRPW QVNLHDGKMS CSGALIDRWW IVTSFDCALT
     AHRTIATLGD HDLTVEEGTE QHIPVAEVIV HSPYRSPLHS LTMVRLAQPA QFNQHVQPVP
     LASRCPQPGE ICSVSGWGST RPNHFEPQQR LKCITVPVVD DQTCVNTFPQ YLYWSQHMVC
     AGRADTDNCM SNRGSVMVCG GQLQGVQWFN HGCKDPAHPS VYSKMCLYND WIHQVMARHP
     PFETTTVSTT TRGRKD
 
 
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