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Database: UniProt/SWISS-PROT
Entry: TRY2_MOUSE
LinkDB: TRY2_MOUSE
Original site: TRY2_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   13-FEB-2019, entry version 155.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   elastase II and trypsin genes.";
RL   Nucleic Acids Res. 14:8307-8330(1986).
RN   [2]
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.;
CC         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   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   UniGene; Mm.276926; -.
DR   ProteinModelPortal; P07146; -.
DR   SMR; P07146; -.
DR   BioGrid; 204335; 1.
DR   STRING; 10090.ENSMUSP00000065393; -.
DR   MEROPS; S01.064; -.
DR   PhosphoSitePlus; P07146; -.
DR   jPOST; P07146; -.
DR   PaxDb; P07146; -.
DR   PeptideAtlas; P07146; -.
DR   PRIDE; P07146; -.
DR   DNASU; 22072; -.
DR   Ensembl; ENSMUST00000070380; ENSMUSP00000065393; ENSMUSG00000057163.
DR   GeneID; 22072; -.
DR   KEGG; mmu:22072; -.
DR   UCSC; uc009boz.2; mouse.
DR   CTD; 5645; -.
DR   MGI; MGI:102759; Prss2.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000153485; -.
DR   HOGENOM; HOG000251820; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P07146; -.
DR   KO; K01312; -.
DR   OMA; QNTIADN; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P07146; -.
DR   TreeFam; TF331065; -.
DR   Reactome; R-MMU-1442490; Collagen degradation.
DR   Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-MMU-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-6803157; Antimicrobial peptides.
DR   ChiTaRS; Prss2; mouse.
DR   PRO; PR:P07146; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000057163; Expressed in 161 organ(s), highest expression level in stomach.
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; ISS:UniProtKB.
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   InterPro; IPR009003; Peptidase_S1_PA.
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   1: Evidence at protein level;
KW   Calcium; Complete proteome; Digestion; Disulfide bond; Hydrolase;
KW   Metal-binding; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     15
FT   PROPEP       16     23       Activation peptide.
FT                                /FTId=PRO_0000028203.
FT   CHAIN        24    246       Anionic trypsin-2.
FT                                /FTId=PRO_0000028204.
FT   DOMAIN       24    244       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     63     63       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    107    107       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    200    200       Charge relay system. {ECO:0000250}.
FT   METAL        75     75       Calcium. {ECO:0000250}.
FT   METAL        77     77       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        80     80       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        85     85       Calcium. {ECO:0000250}.
FT   SITE        194    194       Required for specificity. {ECO:0000250}.
FT   DISULFID     30    160       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID     48     64       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    132    233       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    139    206       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    171    185       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    196    220       {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
//
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