ID Q792Z0_MOUSE Unreviewed; 246 AA.
AC Q792Z0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE SubName: Full=Protease, serine 3 {ECO:0000313|Ensembl:ENSMUSP00000093702.6};
DE SubName: Full=Trypsinogen 11 {ECO:0000313|EMBL:AAB69059.1};
GN Name=Prss3 {ECO:0000313|Ensembl:ENSMUSP00000093702.6,
GN ECO:0000313|MGI:MGI:102758};
GN Synonyms=Tcrb-V20 {ECO:0000313|MGI:MGI:102758}, trypsinogen
GN {ECO:0000313|EMBL:AAB69059.1};
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:AAB69059.1};
RN [1] {ECO:0000313|EMBL:AAB69059.1}
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 [2] {ECO:0000313|Ensembl:ENSMUSP00000093702.6, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000093702.6,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {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).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000093702.6}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000093702.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AE000664; AAB69059.1; -; Genomic_DNA.
DR RefSeq; NP_035775.1; NM_011645.2.
DR STRING; 10090.ENSMUSP00000093702; -.
DR MEROPS; S01.060; -.
DR MEROPS; S01.062; -.
DR PaxDb; 10090-ENSMUSP00000093702; -.
DR ProteomicsDB; 339270; -.
DR DNASU; 22073; -.
DR Ensembl; ENSMUST00000096003.7; ENSMUSP00000093702.6; ENSMUSG00000071519.7.
DR GeneID; 22073; -.
DR KEGG; mmu:22073; -.
DR UCSC; uc009bov.2; mouse.
DR AGR; MGI:102758; -.
DR CTD; 5646; -.
DR MGI; MGI:102758; Prss3.
DR VEuPathDB; HostDB:ENSMUSG00000071519; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01050000244883; -.
DR HOGENOM; CLU_006842_7_0_1; -.
DR OMA; HNIMELE; -.
DR OrthoDB; 4629979at2759; -.
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; 22073; 2 hits in 41 CRISPR screens.
DR ChiTaRS; Prss3; mouse.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000071519; Expressed in pyloric antrum and 19 other cell types or tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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:SF10; PROTEASE, SERINE 1 (TRYPSIN 1)-RELATED; 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 Proteomics identification {ECO:0007829|MaxQB:Q792Z0,
KW ECO:0007829|PeptideAtlas:Q792Z0};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
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 /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015098646"
FT DOMAIN 24..244
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 246 AA; 26184 MW; 4AEF6314CCBF04EC CRC64;
MNALLILALV GAAVAFPVDD DDKIVGGYTC QENSVPYQVS LNSGYHFCGG SLINDQWVVS
AAHCYKTRIQ VRLGEHNINV LEGNEQFVNA AKIIKHPNFN RKTLNNDIML LKLSSPVTLN
ARVATVALPS SCAPAGTQCL ISGWGNTLSF GVSEPDLLQC LDAPLLPQAD CEASYPGKIT
GNMVCAGFLE GGKDSCQGDS GGPVVCNREL QGIVSWGYGC ALPDNPGVYT KVCNYVDWIQ
DTIAAN
//
