BSSP4_MOUSE
ID BSSP4_MOUSE Reviewed; 307 AA.
AC Q9ER10; Q7TML0;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Brain-specific serine protease 4;
DE Short=BSSP-4;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease 22;
DE AltName: Full=Serine protease 26;
DE AltName: Full=Tryptase epsilon;
DE Flags: Precursor;
GN Name=Prss22; Synonyms=Bssp4, Prss26;
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 [MRNA].
RC TISSUE=Brain;
RA Mitsui S., Okui A., Kominami K., Yamaguchi N.;
RT "Cloning and characterization of a novel serine protease, mBSSP-4.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [3] {ECO:0000312|EMBL:EDL22288.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH55854.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH55854.1};
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 -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB010778; BAB20262.1; -; mRNA.
DR EMBL; AC110262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466606; EDL22288.1; -; Genomic_DNA.
DR EMBL; BC055854; AAH55854.1; -; mRNA.
DR CCDS; CCDS37482.1; -.
DR RefSeq; NP_598492.2; NM_133731.2.
DR AlphaFoldDB; Q9ER10; -.
DR SMR; Q9ER10; -.
DR STRING; 10090.ENSMUSP00000039808; -.
DR MEROPS; S01.252; -.
DR GlyGen; Q9ER10; 1 site.
DR PaxDb; Q9ER10; -.
DR PRIDE; Q9ER10; -.
DR ProteomicsDB; 265249; -.
DR ProteomicsDB; 336893; -.
DR Antibodypedia; 42617; 80 antibodies from 20 providers.
DR DNASU; 70835; -.
DR Ensembl; ENSMUST00000041649; ENSMUSP00000039808; ENSMUSG00000045027.
DR GeneID; 70835; -.
DR KEGG; mmu:70835; -.
DR UCSC; uc012amb.1; mouse.
DR CTD; 64063; -.
DR MGI; MGI:1918085; Prss22.
DR VEuPathDB; HostDB:ENSMUSG00000045027; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000160305; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q9ER10; -.
DR OMA; NTSCWIA; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9ER10; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 70835; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Prss22; mouse.
DR PRO; PR:Q9ER10; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9ER10; protein.
DR Bgee; ENSMUSG00000045027; Expressed in conjunctival fornix and 93 other tissues.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016504; F:peptidase activator activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0010952; P:positive regulation of peptidase activity; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
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 Serine protease; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..307
FT /note="Brain-specific serine protease 4"
FT /id="PRO_0000027505"
FT DOMAIN 50..290
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 90
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 242
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 175..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 208..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 238..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 268..270
FT /note="ERN -> DD (in Ref. 1; BAB20262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 33432 MW; 58692F29355B704E CRC64;
MMISRPPPAL GGDQFSILIL LVLLTSTAPI SAATIRVSPD CGKPQQLNRI VGGEDSMDAQ
WPWIVSILKN GSHHCAGSLL TNRWVVTAAH CFKSNMDKPS LFSVLLGAWK LGSPGPRSQK
VGIAWVLPHP RYSWKEGTHA DIALVRLEHS IQFSERILPI CLPDSSVRLP PKTDCWIAGW
GSIQDGVPLP HPQTLQKLKV PIIDSELCKS LYWRGAGQEA ITEGMLCAGY LEGERDACLG
DSGGPLMCQV DDHWLLTGII SWGEGCAERN RPGVYTSLLA HRSWVQRIVQ GVQLRGYLAD
SGDTGSS
