PRSS8_RAT
ID PRSS8_RAT Reviewed; 342 AA.
AC Q9ES87; Q6GSY8; Q9ER01;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=11373334; DOI=10.1681/asn.v1261114;
RA Adachi M., Kitamura K., Miyoshi T., Narikiyo T., Iwashita K., Shiraishi N.,
RA Nonoguchi H., Tomita K.;
RT "Activation of epithelial sodium channels by prostasin in Xenopus
RT oocytes.";
RL J. Am. Soc. Nephrol. 12:1114-1121(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang C.;
RT "Molecular cloning and expression of rat prostasin.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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: Possesses a trypsin-like cleavage specificity with a
CC preference for poly-basic substrates. Stimulates epithelial sodium
CC channel (ENaC) activity through activating cleavage of the gamma
CC subunits (SCNN1G) (By similarity). {ECO:0000250}.
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}.
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DR EMBL; AB017638; BAB20281.1; -; mRNA.
DR EMBL; AF202076; AAG32641.1; -; mRNA.
DR EMBL; BC061800; AAH61800.1; -; mRNA.
DR RefSeq; NP_620191.1; NM_138836.1.
DR AlphaFoldDB; Q9ES87; -.
DR SMR; Q9ES87; -.
DR STRING; 10116.ENSRNOP00000026572; -.
DR MEROPS; S01.159; -.
DR GlyGen; Q9ES87; 1 site.
DR PaxDb; Q9ES87; -.
DR GeneID; 192107; -.
DR KEGG; rno:192107; -.
DR UCSC; RGD:619973; rat.
DR CTD; 5652; -.
DR RGD; 619973; Prss8.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q9ES87; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9ES87; -.
DR PRO; PR:Q9ES87; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0017080; F:sodium channel regulator activity; ISO:RGD.
DR GO; GO:0001942; P:hair follicle development; ISO:RGD.
DR GO; GO:1902307; P:positive regulation of sodium ion transmembrane transport; IDA:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0070633; P:transepithelial transport; ISO:RGD.
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_0000028035"
FT CHAIN 33..322
FT /note="Prostasin"
FT /id="PRO_0000240513"
FT CHAIN 33..44
FT /note="Prostasin light chain"
FT /id="PRO_0000028036"
FT CHAIN 45..322
FT /note="Prostasin heavy chain"
FT /id="PRO_0000028037"
FT PROPEP 323..342
FT /evidence="ECO:0000250"
FT /id="PRO_0000028038"
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 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"
FT CONFLICT 17
FT /note="V -> I (in Ref. 1; BAB20281)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="V -> A (in Ref. 1; BAB20281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 36857 MW; F78BCAC8B1268C64 CRC64;
MALRVGLGLG QLEALFVLLL IGLLQSRIGA DGTEASCGAV IQPRITGGGS AKPGQWPWQV
SITYNGVHVC GGSLVSNQWV VSAAHCFPRE HSKEEYEVKL GAHQLDSFSN DIVVHTVAQI
ISHSSYREEG SQGDIALIRL SSPVTFSRYI RPICLPAANA SFPNGLHCTV TGWGHVAPSV
SLQTPRPLQQ LEVPLISRET CSCLYNINAV PEEPHTIQQD MLCAGYVKGG KDACQGDSGG
PLSCPIDGLW YLAGIVSWGD ACGAPNRPGV YTLTSTYASW IHHHVAELQP RVVPQTQESQ
PDGHLCNHHP VFNLAAAQKL SRPILFLPLS LTLGLFSLWL EH
