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 27-MAR-2024, entry version 179.
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}.
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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 GlyGen; P07146; 1 site, 1 O-linked glycan (1 site).
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; MRETNIY; -.
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-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 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
//
