ID   PRS54_MOUSE             Reviewed;         383 AA.
AC   Q7M756;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Inactive serine protease 54;
DE   AltName: Full=Plasma kallikrein-like protein 4;
DE   Flags: Precursor;
GN   Name=Prss54; Synonyms=Klkbl4;
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   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. Plasma kallikrein
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- CAUTION: Although related to peptidase S1 family, lacks the essential
CC       His, Asp, and Ser residues of the catalytic triad at positions 73, 119
CC       and 210 and is therefore predicted to have lost protease activity.
CC       {ECO:0000305}.
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DR   EMBL; AC102555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01187779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000132; CAD67595.1; -; mRNA.
DR   CCDS; CCDS80916.1; -.
DR   RefSeq; NP_081916.1; NM_027640.1.
DR   AlphaFoldDB; Q7M756; -.
DR   SMR; Q7M756; -.
DR   STRING; 10090.ENSMUSP00000058859; -.
DR   MEROPS; S01.992; -.
DR   GlyGen; Q7M756; 1 site.
DR   PaxDb; Q7M756; -.
DR   PRIDE; Q7M756; -.
DR   ProteomicsDB; 291804; -.
DR   Antibodypedia; 29072; 84 antibodies from 15 providers.
DR   Ensembl; ENSMUST00000180075; ENSMUSP00000137577; ENSMUSG00000048400.
DR   Ensembl; ENSMUST00000213096; ENSMUSP00000148608; ENSMUSG00000048400.
DR   UCSC; uc009myo.1; mouse.
DR   MGI; MGI:1918243; Prss54.
DR   VEuPathDB; HostDB:ENSMUSG00000048400; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01020000230389; -.
DR   InParanoid; Q7M756; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q7M756; -.
DR   BioGRID-ORCS; 70993; 0 hits in 73 CRISPR screens.
DR   PRO; PR:Q7M756; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q7M756; protein.
DR   Bgee; ENSMUSG00000048400; Expressed in spermatid and 9 other tissues.
DR   ExpressionAtlas; Q7M756; baseline and differential.
DR   Genevisible; Q7M756; MM.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Serine protease homolog; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..383
FT                   /note="Inactive serine protease 54"
FT                   /id="PRO_5000095973"
FT   DOMAIN          21..258
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          305..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        154..216
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        185..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        206..237
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   383 AA;  42758 MW;  982B61714A56FC95 CRC64;
     MAEMRGMLLM LLYISHSSSA ICGIQKATIA DKLKENLVSS TEFPWVVSIQ DKQYTHLAFG
     CILSEFWILS TASALQHRPE VIAVVGISNM DPRKTDHREY SVNTIIPHEN FDNVSMGNNI
     ALLKTESAMH FNDLVQAICF LGKKLHKPPA LKNCWVAGWN PTSATGNHMT MSILRRISVK
     DIEVCPLRRH QKTECASHTK EPNNVCLGEP GSPMMCQAKK LDLWILRGLL AYGGDSCPGL
     FLYTSVADYS DWITAKTRKA GPSLSSLHLW EKLVFELPFH ESNIALTTNS FSIHTYAEWP
     HSYSQGQRMS TKSNKQKDAG QNFRVNRQPE TSGPSKVAIQ PMYYDYYGGE AGEGGAVAGQ
     NRLHWSQERI LMSFVLVFLG SGV