PRS57_MOUSE
ID PRS57_MOUSE Reviewed; 284 AA.
AC Q14B24;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Serine protease 57;
DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q6UWY2};
DE AltName: Full=Neutrophil serine protease 4 {ECO:0000250|UniProtKB:Q6UWY2};
DE Short=NSP4 {ECO:0000250|UniProtKB:Q6UWY2};
DE AltName: Full=Serine protease 1-like protein 1;
DE Flags: Precursor;
GN Name=Prss57; Synonyms=Prssl1;
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 [LARGE SCALE MRNA].
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 cleaves preferentially after Arg
CC residues. Can also cleave after citrulline (deimidated arginine) and
CC methylarginine residues. {ECO:0000250|UniProtKB:Q6UWY2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule lumen
CC {ECO:0000250|UniProtKB:Q6UWY2}. Secreted
CC {ECO:0000250|UniProtKB:Q6UWY2}. Note=Stored in cytoplasmic granules and
CC secreted as active enzyme in response to stimulation of neutrophils.
CC {ECO:0000250|UniProtKB:Q6UWY2}.
CC -!- PTM: After cleavage of the signal peptide, the N-terminus is probably
CC further processed by CTSC. Processing by CTSC is probably required for
CC accumulation in cytoplasmic granules; in the absence of CTSC the
CC protein does not accumulate. {ECO:0000250|UniProtKB:Q6UWY2}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6UWY2}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC {ECO:0000305}.
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DR EMBL; BC116380; AAI16381.2; -; mRNA.
DR CCDS; CCDS35968.1; -.
DR RefSeq; NP_001036175.1; NM_001042710.1.
DR RefSeq; XP_006514262.1; XM_006514199.3.
DR RefSeq; XP_011241886.1; XM_011243584.2.
DR AlphaFoldDB; Q14B24; -.
DR SMR; Q14B24; -.
DR STRING; 10090.ENSMUSP00000132215; -.
DR MEROPS; S01.368; -.
DR GlyGen; Q14B24; 1 site.
DR EPD; Q14B24; -.
DR PaxDb; Q14B24; -.
DR PRIDE; Q14B24; -.
DR ProteomicsDB; 291754; -.
DR Antibodypedia; 1455; 56 antibodies from 16 providers.
DR DNASU; 73106; -.
DR Ensembl; ENSMUST00000020573; ENSMUSP00000020573; ENSMUSG00000020323.
DR Ensembl; ENSMUST00000169684; ENSMUSP00000132215; ENSMUSG00000020323.
DR GeneID; 73106; -.
DR KEGG; mmu:73106; -.
DR UCSC; uc007fzu.1; mouse.
DR CTD; 400668; -.
DR MGI; MGI:1920356; Prss57.
DR VEuPathDB; HostDB:ENSMUSG00000020323; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162457; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; Q14B24; -.
DR OMA; VCNSSWR; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q14B24; -.
DR TreeFam; TF333630; -.
DR BioGRID-ORCS; 73106; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Prss57; mouse.
DR PRO; PR:Q14B24; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q14B24; protein.
DR Bgee; ENSMUSG00000020323; Expressed in granulocyte and 31 other tissues.
DR ExpressionAtlas; Q14B24; baseline and differential.
DR GO; GO:0035578; C:azurophil granule lumen; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS: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 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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Heparin-binding; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..284
FT /note="Serine protease 57"
FT /id="PRO_0000295854"
FT DOMAIN 40..269
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 80
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6UWY2"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6UWY2"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6UWY2"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 163..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 194..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 220..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 284 AA; 30341 MW; 228BBC819F0BA98A CRC64;
MPSSTAMVPG TRGGWHCLVL TTAAALTQLM WLPGCCGSYI VGGHEVTPHS RPYMASVSFE
GHHYCGGFLI HTHWVVSAAH CFSDRDPSMG LVVLGAHALL APEPTQQTFS IAAAVSHPDF
QPATQANDIC LLRLNGSAVL GPAVRLLRLP RRNAKPPAAG TRCHVSGWGF VSDFEEPPPG
LMEVEVRILD LSVCNSSWQG QLNPAMLCTH SGDRRRRGFC SADSGGPLVC GRRAHGLVSF
SGLWCGDPKT PDVYTQVSAF VTWIWDVVRA SSSPGSTGRS VRAV
