POLS2_MOUSE
ID POLS2_MOUSE Reviewed; 849 AA.
AC Q5K2P8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Polyserase-2;
DE EC=3.4.21.-;
DE AltName: Full=Polyserine protease 2;
DE AltName: Full=Serine protease 36;
DE Flags: Precursor;
GN Name=Prss36;
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 STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=15536082; DOI=10.1074/jbc.m409139200;
RA Cal S., Quesada V., Llamazares M., Diaz-Perales A., Garabaya C.,
RA Lopez-Otin C.;
RT "Human polyserase-2, a novel enzyme with three tandem serine protease
RT domains in a single polypeptide chain.";
RL J. Biol. Chem. 280:1953-1961(2005).
CC -!- FUNCTION: Serine protease. Hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg-
CC AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-
CC Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for
CC substrates with an Arg instead of a Lys residue in position P1 (By
CC similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Inhibited by serine proteinase inhibitor 4-(2-
CC aminoethyl)-benzenesulfonyl fluoride, but not with EDTA or E-64.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Note=Not attached to membranes. {ECO:0000250}.
CC -!- DOMAIN: The first serine protease domain is catalytically active,
CC whereas the second domain lacks the essential His residue of the
CC catalytic triad at position 363, and the third domain lacks the
CC essential Asp residue of the catalytic triad at position 673. The
CC second and third domains are therefore predicted to be inactive.
CC -!- PTM: The 3 protease domains are not proteolytically cleaved.
CC {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AJ784939; CAH05010.1; -; mRNA.
DR AlphaFoldDB; Q5K2P8; -.
DR SMR; Q5K2P8; -.
DR STRING; 10090.ENSMUSP00000091565; -.
DR MEROPS; S01.414; -.
DR GlyGen; Q5K2P8; 6 sites.
DR PRIDE; Q5K2P8; -.
DR MGI; MGI:1924863; Prss36.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q5K2P8; -.
DR ChiTaRS; Prss36; mouse.
DR PRO; PR:Q5K2P8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5K2P8; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IC:MGI.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 3.
DR InterPro; IPR017326; Pept_S1A_polyserase-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 InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 3.
DR PIRSF; PIRSF037933; Polyserase-2; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 3.
DR SUPFAM; SSF50494; SSF50494; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 3.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..46
FT /evidence="ECO:0000255"
FT /id="PRO_0000027881"
FT CHAIN 47..849
FT /note="Polyserase-2"
FT /id="PRO_0000027882"
FT DOMAIN 47..291
FT /note="Peptidase S1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 323..567
FT /note="Peptidase S1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 584..802
FT /note="Peptidase S1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 87
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 173..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 206..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 239..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 348..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 438..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 466..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 500..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 609..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 705..766
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 733..745
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 849 AA; 91852 MW; 06128D0909B6D1B6 CRC64;
MSPHLFLPVV VLVVSPTPGA FQDSAVSPTQ GEFEDLDCGR PEPSSRIVGG SDAHPGTWPW
QVSLHHGGGH ICGGSLIAPS WVLSAAHCFV TNGTLEPADE WSVLLGVHSQ DGPLEGAHMR
SVATILVPDN YSRVELGADL ALLRLASPAK LGPSVKPVCL PRASHLFAHG TACWATGWGD
VQESDPLPVP WVLQEVELKL LGETACQCLY SRPGPFNLTL QLLPGMLCAG YPEGRRDTCQ
GDSGGPLVCE DGGRWFLAGI TSFGFGCGRR NRPGVFTAVA HYESWIREHV MGSEPGPAFP
SQLQKPPSEP WEPREENCTF AQPECGKATR PGTWPWEAQV MVPGSTPCYG ALVSDSWVLA
PASCFLDSLH DFETWRVLLP SRPEEKRVVR LVAHENASRN FASDLALLQL RTRVNLTAAP
SAVCLPHREH YFLPGSRCRL ARWGHGEPAP RSSAQLEAQL LNSWWCHCLY GRQGESVPPP
GDPPHLLCPA YQEEEEAGAC WVDSGWSLLC REEGTWFLAG YRTLSNGCLR PRAFSPMQTH
GLWISHVTQG AYLEDQLTWD WGPEGEETEK QTCPPHTEHG ACGLRPQSTP AGVLWPWLTE
VHVTGDRVCT GILVAPGWVL AATHCILRLG SSTVPYIDVY LGLAGVSSLP QGHQVSRSVV
SIRLPRHSGL RPPLALLELN SRVEPSPSAL PICLHPEGVP PGASCWVLGW KDPQNRVPVA
AAVSILTPRL CHCLYQGALT PGTFCVFYTE EQEDRCEMTS APPLLCQTEG GPWVLVGMAV
RGSRELFAAI GPEATWISQT VGEAHFLHLG GSSYWSPEGS DPCPQDLAGS ASSPKVAALP
LLLALLIPR
