ID Q0GYP4_SPAAU Unreviewed; 241 AA. AC Q0GYP4; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 12-AUG-2020, entry version 52. DE SubName: Full=Trypsinogen II {ECO:0000313|EMBL:ABE68639.1}; DE EC=3.4.21.4 {ECO:0000313|EMBL:ABE68639.1}; GN Name=TRPII {ECO:0000313|EMBL:ABE68639.1}; OS Sparus aurata (Gilthead sea bream). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Spariformes; Sparidae; Sparus. OX NCBI_TaxID=8175 {ECO:0000313|EMBL:ABE68639.1}; RN [1] {ECO:0000313|EMBL:ABE68639.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Liver {ECO:0000313|EMBL:ABE68639.1}; RA Psohiou E., Sarropoulou E., Mamuris Z., Moutou K.A.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABE68639.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Liver {ECO:0000313|EMBL:ABE68639.1}; RX PubMed=17341447; DOI=10.1016/j.cbpb.2007.01.020; RA Psochiou E., Sarropoulou E., Mamuris Z., Moutou K.A.; RT "Sequence analysis and tissue expression pattern of Sparus aurata RT chymotrypsinogens and trypsinogen."; RL Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 147:367-377(2007). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space CC {ECO:0000256|ARBA:ARBA00004239}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ443543; ABE68639.1; -; mRNA. DR MEROPS; S01.125; -. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; -; 3. 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 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Hydrolase {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:ABE68639.1}; KW Protease {ECO:0000256|RuleBase:RU363034}; KW Serine protease {ECO:0000256|RuleBase:RU363034}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..15 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 16..241 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5012836321" FT DOMAIN 21..239 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" SQ SEQUENCE 241 AA; 26258 MW; A16A7AFF71CDE151 CRC64; MKCLVFVLLI GAAFALDDDK IVGGYECQAH SQPHQVSLNS GYHFCGGSLV NENWVVSAAH CYKSRVEVRL GEHDIYRNEG TEQFISSSRV IRHPNYNSWN IDNDIMLIKL SKPATLNSYV QPVALPTSCA PAGTMCRVSG WGNTMSSVSG DQLQCLEIPI LSTRDCENSY PGMITDAMFC AGYLEGGKDS CQGDSGGPVV CNGQLQGVVS WGYGCAERDH PGVYAKVCIF NDWLETTMAS Y //