PRS30_RAT
ID PRS30_RAT Reviewed; 304 AA.
AC P83748;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Serine protease 30;
DE EC=3.4.21.-;
DE AltName: Full=Distal intestinal serine protease;
DE AltName: Full=Transmembrane serine protease 1;
DE Short=TMSP-1;
DE AltName: Full=Transmembrane serine protease 8;
DE Flags: Precursor;
GN Name=Prss30;
GN Synonyms=Disp {ECO:0000250|UniProtKB:Q9QYZ9}, Tmprss8, Tmsp-1,
GN Tmsp1 {ECO:0000303|PubMed:14669991};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GPI-ANCHOR AT
RP SER-275, FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:BAD01655.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:BAD01655.1};
RX PubMed=14669991; DOI=10.1515/bc.2003.164;
RA Okumura Y., Nishikawa M., Cui P., Shiota M., Nakamura Y., Adachi M.,
RA Kitamura K., Tomita K., Kido H.;
RT "Cloning and characterization of a transmembrane-type serine protease from
RT rat kidney, a new sodium channel activator.";
RL Biol. Chem. 384:1483-1495(2003).
CC -!- FUNCTION: Selectively cleaves synthetic peptide substrates of trypsin.
CC Activates the epithelial sodium channel ENaC.
CC {ECO:0000269|PubMed:14669991}.
CC -!- ACTIVITY REGULATION: Inhibited by aprotinin, leupeptin, benzamidine and
CC soybean trypsin inhibitor. Partially inhibited by PMSF and DFP.
CC {ECO:0000269|PubMed:14669991}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0.;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in kidney, small intestine
CC and stomach and moderately in thymus, lung, spleen, testis and skin. In
CC the kidney, expressed mainly in collecting duct of renal medulla and
CC cortex. {ECO:0000269|PubMed:14669991}.
CC -!- INDUCTION: By aldosterone. {ECO:0000269|PubMed:14669991}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB073023; BAD01655.1; -; mRNA.
DR RefSeq; NP_955403.1; NM_199371.1.
DR AlphaFoldDB; P83748; -.
DR SMR; P83748; -.
DR STRING; 10116.ENSRNOP00000037368; -.
DR MEROPS; S01.042; -.
DR CarbonylDB; P83748; -.
DR GlyGen; P83748; 3 sites.
DR PaxDb; P83748; -.
DR GeneID; 287106; -.
DR KEGG; rno:287106; -.
DR UCSC; RGD:735142; rat.
DR CTD; 30943; -.
DR RGD; 735142; Prss30.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P83748; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P83748; -.
DR PRO; PR:P83748; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0046658; C:anchored component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0017080; F:sodium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IDA: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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Ion transport; Lipoprotein; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Sodium; Sodium transport;
KW Transport; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..30
FT /note="Activation peptide"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:14669991"
FT /id="PRO_0000027864"
FT CHAIN 31..275
FT /note="Serine protease 30"
FT /id="PRO_0000027865"
FT PROPEP 276..304
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000027866"
FT DOMAIN 31..271
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 72
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P49863"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P49863"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P49863"
FT LIPID 275
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000305|PubMed:14669991"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..73
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 155..229
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 185..208
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 219..247
FT /evidence="ECO:0000250|UniProtKB:P49863,
FT ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 304 AA; 33086 MW; 825187B7DD70D789 CRC64;
MESWARCIFL LLLQILTGGR GDILHSGAGK IVGGQDAPEG RWPWQVSLRT EKEGHICGGS
LIHEVWVLTA AHCFRRPLNS SFYHVKVGGL TLSLTEPHST LVAVRNIFVY PTYLWEDASS
GDIALLRLDT PLQPSQFSPV CLPQAQAPLT PGTVCWVTGW GATHERELAS VLQELAVPLL
DSEDCERMYH IGETSLSGKR VIQSDMLCAG FVEGQKDSCQ GDSGGPLVCA INSSWIQVGI
TSWGIGCARP NKPGVYTRVP DYVDWIQRTL AENHSDAYGC RSRASGAYPA LLLVLLAFAL
PESL
