PRS30_MOUSE
ID PRS30_MOUSE Reviewed; 310 AA.
AC Q9QYZ9; Q91XC4;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Serine protease 30;
DE EC=3.4.21.-;
DE AltName: Full=Distal intestinal serine protease;
DE AltName: Full=Transmembrane serine protease 8;
DE Flags: Precursor;
GN Name=Prss30; Synonyms=Disp {ECO:0000312|MGI:MGI:1353645}, Tmprss8;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:10786627};
RC TISSUE=Small intestine {ECO:0000269|PubMed:10786627};
RX PubMed=10786627; DOI=10.1016/s0167-4781(99)00226-2;
RA Shaw-Smith C.J., Coffey A.J., Leversha M., Freeman T.C., Bentley D.R.,
RA Walters J.R.F.;
RT "Characterization of a novel murine intestinal serine protease, DISP.";
RL Biochim. Biophys. Acta 1490:131-136(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH10970.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH10970.1};
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: Selectively cleaves synthetic peptide substrates of trypsin.
CC Activates the epithelial sodium channel ENaC (By similarity).
CC {ECO:0000250|UniProtKB:P83748}.
CC -!- ACTIVITY REGULATION: Inhibited by aprotinin, leupeptin, benzamidine and
CC soybean trypsin inhibitor. Partially inhibited by PMSF and DFP (By
CC similarity). {ECO:0000250|UniProtKB:P83748}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed primarily in distal gut.
CC {ECO:0000269|PubMed:10786627}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AJ243866; CAB56465.1; -; mRNA.
DR EMBL; BC010970; AAH10970.1; -; mRNA.
DR EMBL; BC040348; AAH40348.1; -; mRNA.
DR CCDS; CCDS28470.1; -.
DR RefSeq; NP_038949.2; NM_013921.3.
DR RefSeq; XP_006524445.1; XM_006524382.3.
DR AlphaFoldDB; Q9QYZ9; -.
DR SMR; Q9QYZ9; -.
DR STRING; 10090.ENSMUSP00000024936; -.
DR MEROPS; S01.042; -.
DR GlyGen; Q9QYZ9; 2 sites.
DR PaxDb; Q9QYZ9; -.
DR PRIDE; Q9QYZ9; -.
DR ProteomicsDB; 291674; -.
DR DNASU; 30943; -.
DR Ensembl; ENSMUST00000024936; ENSMUSP00000024936; ENSMUSG00000024124.
DR Ensembl; ENSMUST00000234765; ENSMUSP00000157077; ENSMUSG00000024124.
DR GeneID; 30943; -.
DR KEGG; mmu:30943; -.
DR UCSC; uc008aue.2; mouse.
DR CTD; 30943; -.
DR MGI; MGI:1353645; Prss30.
DR VEuPathDB; HostDB:ENSMUSG00000024124; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000160305; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q9QYZ9; -.
DR OMA; TSEGHIC; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9QYZ9; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 30943; 5 hits in 71 CRISPR screens.
DR PRO; PR:Q9QYZ9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9QYZ9; protein.
DR Bgee; ENSMUSG00000024124; Expressed in right colon and 28 other tissues.
DR ExpressionAtlas; Q9QYZ9; baseline and differential.
DR Genevisible; Q9QYZ9; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; ISA:MGI.
DR GO; GO:0017080; F:sodium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; ISS:UniProtKB.
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 Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase;
KW Ion transport; Lipoprotein; Membrane; Protease; Reference proteome;
KW Serine protease; Signal; Sodium; Sodium transport; Transport; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..36
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P83748, ECO:0000255"
FT /id="PRO_0000027861"
FT CHAIN 37..281
FT /note="Serine protease 30"
FT /id="PRO_0000027862"
FT PROPEP 282..310
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000027863"
FT DOMAIN 37..277
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 78
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P49863"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P49863"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P49863"
FT LIPID 281
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..79
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 161..235
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 191..214
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 225..253
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 221..222
FT /note="QK -> HI (in Ref. 1; CAB56465)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 33707 MW; FA126747DEAE0AB6 CRC64;
MESRARCIFL LLLQILTRAR GDILPSVCGH SRDAGKIVGG QDALEGQWPW QVSLWITEDG
HICGGSLIHE VWVLTAAHCF RRSLNPSFYH VKVGGLTLSL LEPHSTLVAV RNIFVHPTYL
WADASSGDIA LVQLDTPLRP SQFTPVCLPA AQTPLTPGTV CWVTGWGATQ ERDMASVLQE
LAVPLLDSED CEKMYHTQGS SLSGERIIQS DMLCAGYVEG QKDSCQGDSG GPLVCSINSS
WTQVGITSWG IGCARPYRPG VYTRVPTYVD WIQRILAENH SDAYGYHSSA SAAYQMLLPV
LLAVALPGSL
