PRS33_MOUSE
ID PRS33_MOUSE Reviewed; 277 AA.
AC Q80WM7; Q3ZB43;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Serine protease 33;
DE EC=3.4.21.-;
DE AltName: Full=Tryptase-6;
DE Short=mT6;
DE Flags: Precursor;
GN Name=Prss33;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=14583634; DOI=10.1074/jbc.m308209200;
RA Wong G.W., Yasuda S., Morokawa N., Li L., Stevens R.L.;
RT "Mouse chromosome 17A3.3 contains 13 genes that encode functional tryptic-
RT like serine proteases with distinct tissue and cell expression patterns.";
RL J. Biol. Chem. 279:2438-2452(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Serine protease that has amidolytic activity, cleaving its
CC substrates before Arg residues. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14583634}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80WM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80WM7-2; Sequence=VSP_027609;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14583634}.
CC -!- PTM: Not glycosylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AY262280; AAP20885.1; -; mRNA.
DR EMBL; BC101950; AAI01951.1; -; mRNA.
DR EMBL; BC103541; AAI03542.1; -; mRNA.
DR EMBL; BC103542; AAI03543.1; -; mRNA.
DR CCDS; CCDS37476.2; -. [Q80WM7-1]
DR RefSeq; NP_001074868.2; NM_001081399.2. [Q80WM7-1]
DR RefSeq; XP_006524514.1; XM_006524451.2. [Q80WM7-2]
DR AlphaFoldDB; Q80WM7; -.
DR SMR; Q80WM7; -.
DR STRING; 10090.ENSMUSP00000059491; -.
DR MEROPS; S01.075; -.
DR PhosphoSitePlus; Q80WM7; -.
DR PaxDb; Q80WM7; -.
DR PRIDE; Q80WM7; -.
DR ProteomicsDB; 291900; -. [Q80WM7-1]
DR ProteomicsDB; 291901; -. [Q80WM7-2]
DR Antibodypedia; 62205; 88 antibodies from 22 providers.
DR DNASU; 353130; -.
DR Ensembl; ENSMUST00000059906; ENSMUSP00000059491; ENSMUSG00000049620. [Q80WM7-1]
DR GeneID; 353130; -.
DR KEGG; mmu:353130; -.
DR UCSC; uc008att.2; mouse. [Q80WM7-1]
DR CTD; 260429; -.
DR MGI; MGI:2661234; Prss33.
DR VEuPathDB; HostDB:ENSMUSG00000049620; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162519; -.
DR HOGENOM; CLU_006842_1_2_1; -.
DR InParanoid; Q80WM7; -.
DR OMA; WIQAHVS; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q80WM7; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 353130; 5 hits in 76 CRISPR screens.
DR PRO; PR:Q80WM7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q80WM7; protein.
DR Bgee; ENSMUSG00000049620; Expressed in morula and 26 other tissues.
DR ExpressionAtlas; Q80WM7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA: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:0070528; P:protein kinase C signaling; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
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 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 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..277
FT /note="Serine protease 33"
FT /id="PRO_0000299317"
FT DOMAIN 34..276
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 74
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 123
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 59..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 157..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 190..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 224..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027609"
SQ SEQUENCE 277 AA; 29888 MW; 3310C067573E5E74 CRC64;
MRGASHLQIL LLLVLGTRMQ ECAACGQPRM SSRIVGGRDA QDGEWPWQTS IQHRGAHVCG
GSLIAPQWVL TAGHCFPRRV WPSEYSVLLG ALSLDVRSSH ELLVPVLRVL LPPDYSEDEA
RGDLALLQLR HPVSLSTRIQ PVCLPAPGSH PPPGSPCWVT GWGSLSPGVP LPKGRPLQGV
RVPLLDSRAC DRLYHVGANV PQGERIVLPG NLCAGYRRGH KDACQGDSGG PLTCMESGHW
VLVGVVSWGK GCALPNRPGV YTNVAKYSPW IQARLSL
