PRSS8_MOUSE
ID PRSS8_MOUSE Reviewed; 342 AA.
AC Q9ESD1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Prostasin;
DE EC=3.4.21.-;
DE AltName: Full=Channel-activating protease 1;
DE Short=CAP1;
DE AltName: Full=Serine protease 8;
DE Contains:
DE RecName: Full=Prostasin light chain;
DE Contains:
DE RecName: Full=Prostasin heavy chain;
DE Flags: Precursor;
GN Name=Prss8; Synonyms=Cap1;
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], AND FUNCTION.
RX PubMed=10770960; DOI=10.1681/asn.v115828;
RA Vuagniaux G., Vallet V., Jaeger N.F., Pfister C., Bens M., Farman N.,
RA Courtois-Coutry N., Vandewalle A., Rossier B.C., Hummler E.;
RT "Activation of the amiloride-sensitive epithelial sodium channel by the
RT serine protease mCAP1 expressed in a mouse cortical collecting duct cell
RT line.";
RL J. Am. Soc. Nephrol. 11:828-834(2000).
CC -!- FUNCTION: Possesses a trypsin-like cleavage specificity with a
CC preference for poly-basic substrates (By similarity). Stimulates
CC epithelial sodium channel (ENaC) activity through activating cleavage
CC of the gamma subunits (SCNN1G). {ECO:0000250,
CC ECO:0000269|PubMed:10770960}.
CC -!- SUBUNIT: Heterodimer of two chains, light and heavy, held by a
CC disulfide bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Prostasin]: Secreted, extracellular space
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Prostasin light chain]: Secreted, extracellular
CC space {ECO:0000250}. Note=Found in the seminal fluid. Secreted after
CC cleavage of its C-terminus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Prostasin heavy chain]: Secreted, extracellular
CC space {ECO:0000250}. Note=Found in the seminal fluid. Secreted after
CC cleavage of its C-terminus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG17054.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF188613; AAG17054.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q9ESD1; -.
DR SMR; Q9ESD1; -.
DR STRING; 10090.ENSMUSP00000032988; -.
DR MEROPS; S01.159; -.
DR GlyGen; Q9ESD1; 2 sites.
DR PhosphoSitePlus; Q9ESD1; -.
DR MaxQB; Q9ESD1; -.
DR PaxDb; Q9ESD1; -.
DR PRIDE; Q9ESD1; -.
DR ProteomicsDB; 291824; -.
DR MGI; MGI:1923810; Prss8.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q9ESD1; -.
DR PhylomeDB; Q9ESD1; -.
DR BRENDA; 3.4.21.B6; 3474.
DR ChiTaRS; Prss8; mouse.
DR PRO; PR:Q9ESD1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9ESD1; protein.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0017080; F:sodium channel regulator activity; IMP:UniProtKB.
DR GO; GO:1902307; P:positive regulation of sodium ion transmembrane transport; ISO:MGI.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IGI:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0070633; P:transepithelial transport; IMP:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 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 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; Hydrolase; Membrane; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..32
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028031"
FT CHAIN 33..322
FT /note="Prostasin"
FT /id="PRO_0000240512"
FT CHAIN 33..44
FT /note="Prostasin light chain"
FT /id="PRO_0000028032"
FT CHAIN 45..322
FT /note="Prostasin heavy chain"
FT /id="PRO_0000028033"
FT PROPEP 323..342
FT /evidence="ECO:0000250"
FT /id="PRO_0000028034"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 45..286
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..154
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 70..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 168..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 201..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 234..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 342 AA; 36729 MW; 0620DE88ED187D0F CRC64;
MAPRVGLGLG QLEAVTILLL LGLLQSGIRA DGTEASCGAV IQPRITGGGS AKPGQWPWQV
SITYDGNHVC GGSLVSNKWV VSAAHCFPRE HSREAYEVKL GAHQLDSYSN DTVVHTVAQI
ITHSSYREEG SQGDIAFIRL SSPVTFSRYI RPICLPAANA SFPNGLHCTV TGWGHVAPSV
SLQTPRPLQQ LEVPLISRET CSCLYNINAV PEEPHTIQQD MLCAGYVKGG KDACQGDSGG
PLSCPMEGIW YLAGIVSWGD ACGAPNRPGV YTLTSTYASW IHHHVAELQP RVVPQTQESQ
PDGHLCNHHP VFSSAAAPKL LRPVLFLPLG LTLGLLSLWL EH
