PRS48_MOUSE
ID PRS48_MOUSE Reviewed; 312 AA.
AC Q14B25; Q7M755;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Serine protease 48;
DE EC=3.4.21.-;
DE AltName: Full=Epidermis-specific serine protease-like protein;
DE Flags: Precursor;
GN Name=Prss48; Synonyms=Esspl, Gm1019;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
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).
RN [3]
RP IDENTIFICATION.
RC STRAIN=C57BL/6J;
RX PubMed=12838346; DOI=10.1038/nrg1111;
RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT "Human and mouse proteases: a comparative genomic approach.";
RL Nat. Rev. Genet. 4:544-558(2003).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AC133508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116378; AAI16379.1; -; mRNA.
DR EMBL; BC116379; AAI16380.1; -; mRNA.
DR EMBL; BN000135; CAD67964.1; -; mRNA.
DR CCDS; CCDS17444.1; -.
DR RefSeq; NP_001001650.1; NM_001001650.1.
DR AlphaFoldDB; Q14B25; -.
DR SMR; Q14B25; -.
DR STRING; 10090.ENSMUSP00000051199; -.
DR MEROPS; S01.325; -.
DR GlyGen; Q14B25; 2 sites.
DR PaxDb; Q14B25; -.
DR PRIDE; Q14B25; -.
DR ProteomicsDB; 291752; -.
DR Antibodypedia; 53070; 85 antibodies from 17 providers.
DR DNASU; 368202; -.
DR Ensembl; ENSMUST00000061343; ENSMUSP00000051199; ENSMUSG00000049013.
DR GeneID; 368202; -.
DR KEGG; mmu:368202; -.
DR UCSC; uc008pqz.1; mouse.
DR CTD; 345062; -.
DR MGI; MGI:2685865; Prss48.
DR VEuPathDB; HostDB:ENSMUSG00000049013; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000160791; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q14B25; -.
DR OMA; GQTHICG; -.
DR OrthoDB; 288421at2759; -.
DR PhylomeDB; Q14B25; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 368202; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q14B25; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q14B25; protein.
DR Bgee; ENSMUSG00000049013; Expressed in morula and 24 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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 Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..312
FT /note="Serine protease 48"
FT /id="PRO_0000331637"
FT DOMAIN 40..276
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 80
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 160..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 190..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 225..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 43
FT /note="G -> D (in Ref. 2; AAI16379/AAI16380)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="M -> I (in Ref. 2; AAI16379/AAI16380)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 34637 MW; 8CF0683C9CD3A038 CRC64;
MGPAGLKVLL LLFLGAFQGS FTKKKNLQSV CGRPVHTGRI VGGQDAALGR WPWQVSLRFD
YTHSCGGSLI SDHWVLTAAH CIKKTWYSFL YSVWLGSIDR EYSSTGKEYY VSRIAIPDKH
RHTEADIALL KLSSRVTFSS VILPICLPNI SKQLTVPASC WVTGWGQNQE GHYPSTLQEL
EVPVISSEAC EQLYNPIGVF LPDLERVIKE DMFCAGERQS RKDSCKGDSG GPLSCHIDGV
WRLMGVVSWG LECGKDLPGV YTNVTYYQKW ISAIISRAPP GWGGDSTHMT SCSLLCYFLW
LSWDPPEPLA LA