ID   Q792Y6_MOUSE            Unreviewed;       246 AA.
AC   Q792Y6;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 141.
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};
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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; MRETNIY; -.
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-2; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034}; 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
//