GenomeNet

Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: TRY2_MOUSE Q792Y6_MOUSE
LinkDB: TRY2_MOUSE Q792Y6_MOUSE
Original site: TRY2_MOUSE Q792Y6_MOUSE 
ID   TRY2_MOUSE              Reviewed;         246 AA.
AC   P07146;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   24-JAN-2024, entry version 178.
DE   RecName: Full=Anionic trypsin-2;
DE            EC=3.4.21.4;
DE   AltName: Full=Anionic trypsin II;
DE   AltName: Full=Pretrypsinogen II;
DE   AltName: Full=Serine protease 2;
DE   Flags: Precursor;
GN   Name=Prss2; Synonyms=Try2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=A/J;
RX   PubMed=3641189; DOI=10.1093/nar/14.21.8307;
RA   Stevenson B.J., Hagenbuechle O., Wellauer P.K.;
RT   "Sequence organisation and transcriptional regulation of the mouse elastase
RT   II and trypsin genes.";
RL   Nucleic Acids Res. 14:8307-8330(1986).
RN   [2]
RP   TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=10506205; DOI=10.1074/jbc.274.41.29426;
RA   Ohmura K., Kohno N., Kobayashi Y., Yamagata K., Sato S., Kashiwabara S.,
RA   Baba T.;
RT   "A homologue of pancreatic trypsin is localized in the acrosome of
RT   mammalian sperm and is released during acrosome reaction.";
RL   J. Biol. Chem. 274:29426-29432(1999).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- TISSUE SPECIFICITY: Expressed in the pancreas, lung and kidney.
CC       {ECO:0000269|PubMed:10506205}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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; X04574; CAA28243.1; -; mRNA.
DR   EMBL; X04577; CAA28245.1; -; Genomic_DNA.
DR   CCDS; CCDS20050.1; -.
DR   PIR; B25528; B25528.
DR   RefSeq; NP_033456.1; NM_009430.2.
DR   AlphaFoldDB; P07146; -.
DR   SMR; P07146; -.
DR   BioGRID; 204335; 3.
DR   STRING; 10090.ENSMUSP00000065393; -.
DR   MEROPS; S01.064; -.
DR   PhosphoSitePlus; P07146; -.
DR   jPOST; P07146; -.
DR   PaxDb; 10090-ENSMUSP00000065393; -.
DR   PeptideAtlas; P07146; -.
DR   ProteomicsDB; 300030; -.
DR   DNASU; 22072; -.
DR   Ensembl; ENSMUST00000070380.5; ENSMUSP00000065393.5; ENSMUSG00000057163.4.
DR   GeneID; 22072; -.
DR   KEGG; mmu:22072; -.
DR   UCSC; uc009boz.2; mouse.
DR   AGR; MGI:102759; -.
DR   CTD; 5645; -.
DR   MGI; MGI:102759; Prss2.
DR   VEuPathDB; HostDB:ENSMUSG00000057163; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01050000244883; -.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   InParanoid; P07146; -.
DR   OMA; GCEYQRI; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; P07146; -.
DR   TreeFam; TF331065; -.
DR   Reactome; R-MMU-1442490; Collagen degradation.
DR   Reactome; R-MMU-1462054; Alpha-defensins.
DR   Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-6803157; Antimicrobial peptides.
DR   BioGRID-ORCS; 22072; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Prss2; mouse.
DR   PRO; PR:P07146; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P07146; Protein.
DR   Bgee; ENSMUSG00000057163; Expressed in pyloric antrum and 99 other cell types or tissues.
DR   ExpressionAtlas; P07146; baseline and differential.
DR   Genevisible; P07146; MM.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI.
DR   GO; GO:0030574; P:collagen catabolic process; ISS:UniProtKB.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   GO; GO:0031000; P:response to caffeine; ISO:MGI.
DR   GO; GO:0035094; P:response to nicotine; ISO:MGI.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
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:SF57; TRYPSIN-1; 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   1: Evidence at protein level;
KW   Calcium; Digestion; Disulfide bond; Hydrolase; Metal-binding; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..15
FT   PROPEP          16..23
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028203"
FT   CHAIN           24..246
FT                   /note="Anionic trypsin-2"
FT                   /id="PRO_0000028204"
FT   DOMAIN          24..244
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        63
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        107
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        200
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            194
FT                   /note="Required for specificity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        48..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        132..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        139..206
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        171..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        196..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   246 AA;  26204 MW;  CEF8C97AAC2D07AD CRC64;
     MSALLILALV GAAVAFPVDD DDKIVGGYTC RESSVPYQVS LNAGYHFCGG SLINDQWVVS
     AAHCYKYRIQ VRLGEHNINV LEGNEQFVDS AKIIRHPNYN SWTLDNDIML IKLASPVTLN
     ARVASVPLPS SCAPAGTQCL ISGWGNTLSN GVNNPDLLQC VDAPVLPQAD CEASYPGDIT
     NNMICVGFLE GGKDSCQGDS GGPVVCNGEL QGIVSWGYGC AQPDAPGVYT KVCNYVDWIQ
     NTIADN
//
ID   Q792Y6_MOUSE            Unreviewed;       246 AA.
AC   Q792Y6;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=trypsin {ECO:0000256|ARBA:ARBA00038868};
DE            EC=3.4.21.4 {ECO:0000256|ARBA:ARBA00038868};
GN   Name=Prss2 {ECO:0000313|MGI:MGI:102759};
GN   Synonyms=Ta {ECO:0000313|EMBL:BAA74759.1}, trypsinogen
GN   {ECO:0000313|EMBL:AAB69089.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAB69089.1};
RN   [1] {ECO:0000313|EMBL:BAA74759.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129SVJ {ECO:0000313|EMBL:BAA74759.1};
RX   PubMed=10506205; DOI=10.1074/jbc.274.41.29426;
RA   Ohmura K., Kohno N., Kobayashi Y., Yamagata K., Sato S., Kashiwabara S.,
RA   Baba T.;
RT   "A homologue of pancreatic trypsin is localized in the acrosome of
RT   mammalian sperm and is released during acrosome reaction.";
RL   J. Biol. Chem. 274:29426-29432(1999).
RN   [2] {ECO:0000313|EMBL:BAB22554.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22554.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:BAB22554.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [3] {ECO:0000313|EMBL:BAB22554.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22554.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:BAB22554.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [4] {ECO:0000313|EMBL:BAB22554.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22554.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:BAB22554.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [5] {ECO:0000313|EMBL:BAB22554.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22554.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:BAB22554.1};
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H., Arakawa T.,
RA   Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M., Hanagaki T.,
RA   Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H., Kawai J., Kojima Y.,
RA   Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., Miyazaki A.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Okazaki Y., Okido T., Owa C.,
RA   Saito H., Saito R., Sakai C., Sakai K., Sano H., Sasaki D., Shibata K.,
RA   Shibata Y., Shinagawa A., Shiraki T., Sogabe Y., Suzuki H., Tagami M.,
RA   Tagawa A., Takahashi F., Tanaka T., Tejima Y., Toya T., Yamamura T.,
RA   Yasunishi A., Yoshida K., Yoshino M., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:AAB69089.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11160223;
RA   Chen F., Rowen L., Hood L., Rothenberg E.V.;
RT   "Differential transcriptional regulation of individual TCR V beta segments
RT   before gene rearrangement.";
RL   J. Immunol. 166:1771-1780(2001).
RN   [7] {ECO:0000313|EMBL:BAB22554.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22554.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:BAB22554.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [8] {ECO:0000313|EMBL:BAB22554.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22554.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:BAB22554.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [9] {ECO:0000313|EMBL:BAB22554.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22554.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:BAB22554.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [10] {ECO:0000313|EMBL:BAB22554.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22554.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:BAB22554.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [11] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036320};
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; AE000665; AAB69089.1; -; Genomic_DNA.
DR   EMBL; AB017030; BAA74759.1; -; Genomic_DNA.
DR   EMBL; AK003082; BAB22554.1; -; mRNA.
DR   RefSeq; NP_033456.1; NM_009430.2.
DR   AlphaFoldDB; Q792Y6; -.
DR   SMR; Q792Y6; -.
DR   MEROPS; S01.064; -.
DR   MaxQB; Q792Y6; -.
DR   DNASU; 22072; -.
DR   GeneID; 22072; -.
DR   KEGG; mmu:22072; -.
DR   AGR; MGI:102759; -.
DR   CTD; 5645; -.
DR   MGI; MGI:102759; Prss2.
DR   VEuPathDB; HostDB:ENSMUSG00000057163; -.
DR   HOGENOM; CLU_006842_7_0_1; -.
DR   OMA; GCEYQRI; -.
DR   OrthoDB; 4629979at2759; -.
DR   BioGRID-ORCS; 22072; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Prss2; mouse.
DR   ExpressionAtlas; Q792Y6; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
DR   GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
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:SF57; TRYPSIN-1; 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   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
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..246
FT                   /note="trypsin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011948595"
FT   DOMAIN          24..244
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   246 AA;  26204 MW;  CEF8C97AAC2D07AD CRC64;
     MSALLILALV GAAVAFPVDD DDKIVGGYTC RESSVPYQVS LNAGYHFCGG SLINDQWVVS
     AAHCYKYRIQ VRLGEHNINV LEGNEQFVDS AKIIRHPNYN SWTLDNDIML IKLASPVTLN
     ARVASVPLPS SCAPAGTQCL ISGWGNTLSN GVNNPDLLQC VDAPVLPQAD CEASYPGDIT
     NNMICVGFLE GGKDSCQGDS GGPVVCNGEL QGIVSWGYGC AQPDAPGVYT KVCNYVDWIQ
     NTIADN
//
DBGET integrated database retrieval system