ID   POLS2_RAT               Reviewed;         875 AA.
AC   Q5K2P9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   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 387, and the third domain lacks the
CC       essential Asp residue of the catalytic triad at position 697. 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   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AJ784938; CAH05009.1; -; mRNA.
DR   AlphaFoldDB; Q5K2P9; -.
DR   SMR; Q5K2P9; -.
DR   MEROPS; S01.414; -.
DR   GlyGen; Q5K2P9; 6 sites.
DR   UCSC; RGD:1593186; rat.
DR   RGD; 1593186; Prss36.
DR   InParanoid; Q5K2P9; -.
DR   PhylomeDB; Q5K2P9; -.
DR   PRO; PR:Q5K2P9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 4.
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; 1.
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..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..50
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027883"
FT   CHAIN           51..875
FT                   /note="Polyserase-2"
FT                   /id="PRO_0000027884"
FT   DOMAIN          51..315
FT                   /note="Peptidase S1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DOMAIN          347..573
FT                   /note="Peptidase S1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DOMAIN          608..826
FT                   /note="Peptidase S1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          320..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        91
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        163
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        267
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        197..273
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        230..252
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        263..291
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        372..388
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        462..534
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        490..512
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        524..552
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        633..649
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        729..790
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        757..769
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   875 AA;  94483 MW;  251C8DE6909FDE17 CRC64;
     MSHHLFLPVV IMVVSPIPPG AFQDSVVSPT QGEFEDLDCG DCGRPEPSSR IVGGSDAHPG
     TWPWQVSLHQ GGGHICGGSL IAPSWVLSAA HCFVTNGTLE PADELSVLLG VHSQDGPLEG
     AHMRSVATIL IPDNYSTVEL GADLALLRLA SPAKLGPSVR GADLALLRLA SPAKLGPSVR
     PVCLPRASHL FAHGTACWAT GWGDVQEAVP LPLPWVLQEV ELRLLGEAAC QCLYSRPGPF
     NLTFQLLPGM LCAGYPAGRR DTCQGDSGGP LVCEDGGRWF LAGITSFGFG CGRRNRPGVF
     TAVAPYESWI REHVMGSEPG PVFPSQLQKP QSGPWEPREE NCTFAQPECG KAPRPGTWPW
     EAQVTVPGST PCYGALVSDR WVLAPASCFL DSPHDFETWR VLLPSRPEEE RVARLVAHEN
     ASRDFASDLA LLQLRTRVNL TAAPSAVCLP HHEHYFLPGS HCRLARWGRG ELAPGSSAQL
     EAQLLNGWWC HCLYGRQGET VPRPGDPPHL LCPAYQEEEE AGLCWVDSSW SLLCREEGTW
     FLAGYRTLSD GCLRPRAFSP MQTHGPWIRH VTQGAYLEDQ LTWDWGPEGE ETEKQTCPTH
     TEHGACGLRP KSTPAGVLWP WLTEVHVTGD RVCTGILVAP GWVLAATHCI LRLGSTTVPY
     IEVYLGRAGV SSLPQGHQVS RSVVSIRLPR HLGLRPPLAL LELNSRVEPS PSALPICLHP
     GGIPSGASCW VLGWKNPQDR VPVVAAVSIL TPRLCHCLYP GILTPGTFCV LYSEGQEDRC
     EVTSAPPLLC QTEEGPWVLV GMAVRGNREL FAAIGPEATW ISQTVGEAHF LHLGGSSYWS
     PEGSDLCPQD LAGSASSPKV TALLLLLLLA PLIPR