ID   POLS2_HUMAN             Reviewed;         855 AA.
AC   Q5K4E3; A8K2P5; B4DW80; B7ZMK8; E7EX56; Q8NBY4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   13-FEB-2019, entry version 123.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   GLYCOSYLATION.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Placenta, Synovium, and Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Serine protease. Hydrolyzes the peptides N-t-Boc-Gln-
CC       Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent,
CC       N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a
CC       preference for substrates with an Arg instead of a Lys residue in
CC       position P1.
CC   -!- ACTIVITY REGULATION: Inhibited by serine proteinase inhibitor 4-
CC       (2-aminoethyl)-benzenesulfonyl fluoride, but not with EDTA or E-
CC       64. {ECO:0000269|PubMed:15536082}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:15536082}. Note=Not attached to
CC       membranes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5K4E3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5K4E3-2; Sequence=VSP_044718;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q5K4E3-3; Sequence=VSP_046639;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in fetal kidney, skeletal muscle,
CC       liver, placenta and heart. Also expressed in tumor cell lines
CC       derived from lung and colon adenocarcinomas.
CC       {ECO:0000269|PubMed:15536082}.
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 679. The
CC       second and third domains are therefore predicted to be inactive
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: The 3 protease domains are not proteolytically cleaved.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15536082}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AJ627034; CAF25303.1; -; mRNA.
DR   EMBL; AK075142; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK290310; BAF82999.1; -; mRNA.
DR   EMBL; AK301409; BAG62942.1; -; mRNA.
DR   EMBL; AC009088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC137396; AAI37397.1; -; mRNA.
DR   EMBL; BC144615; AAI44616.1; -; mRNA.
DR   CCDS; CCDS32436.1; -. [Q5K4E3-1]
DR   CCDS; CCDS58452.1; -. [Q5K4E3-2]
DR   CCDS; CCDS58453.1; -. [Q5K4E3-3]
DR   RefSeq; NP_001245219.1; NM_001258290.1. [Q5K4E3-3]
DR   RefSeq; NP_001245220.1; NM_001258291.1. [Q5K4E3-2]
DR   RefSeq; NP_775773.2; NM_173502.4. [Q5K4E3-1]
DR   UniGene; Hs.256632; -.
DR   ProteinModelPortal; Q5K4E3; -.
DR   SMR; Q5K4E3; -.
DR   STRING; 9606.ENSP00000268281; -.
DR   MEROPS; S01.414; -.
DR   BioMuta; PRSS36; -.
DR   DMDM; 209572670; -.
DR   PaxDb; Q5K4E3; -.
DR   PeptideAtlas; Q5K4E3; -.
DR   PRIDE; Q5K4E3; -.
DR   ProteomicsDB; 63543; -.
DR   Ensembl; ENST00000268281; ENSP00000268281; ENSG00000178226. [Q5K4E3-1]
DR   Ensembl; ENST00000418068; ENSP00000407160; ENSG00000178226. [Q5K4E3-2]
DR   Ensembl; ENST00000569305; ENSP00000454768; ENSG00000178226. [Q5K4E3-3]
DR   GeneID; 146547; -.
DR   KEGG; hsa:146547; -.
DR   UCSC; uc002ebd.5; human. [Q5K4E3-1]
DR   CTD; 146547; -.
DR   EuPathDB; HostDB:ENSG00000178226.10; -.
DR   GeneCards; PRSS36; -.
DR   H-InvDB; HIX0038569; -.
DR   HGNC; HGNC:26906; PRSS36.
DR   HPA; HPA036079; -.
DR   MIM; 610560; gene.
DR   neXtProt; NX_Q5K4E3; -.
DR   OpenTargets; ENSG00000178226; -.
DR   PharmGKB; PA142671123; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000161761; -.
DR   HOGENOM; HOG000115606; -.
DR   HOVERGEN; HBG053635; -.
DR   InParanoid; Q5K4E3; -.
DR   KO; K09630; -.
DR   OMA; QENRCEM; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q5K4E3; -.
DR   TreeFam; TF351678; -.
DR   GenomeRNAi; 146547; -.
DR   PRO; PR:Q5K4E3; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   Bgee; ENSG00000178226; Expressed in 91 organ(s), highest expression level in blood.
DR   ExpressionAtlas; Q5K4E3; baseline and differential.
DR   Genevisible; Q5K4E3; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR017326; Pept_S1A_polyserase-2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   PROPEP       23     46       {ECO:0000255}.
FT                                /FTId=PRO_0000027879.
FT   CHAIN        47    855       Polyserase-2.
FT                                /FTId=PRO_0000027880.
FT   DOMAIN       47    291       Peptidase S1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   DOMAIN      323    555       Peptidase S1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   DOMAIN      590    808       Peptidase S1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     87     87       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    139    139       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    243    243       Charge relay system. {ECO:0000250}.
FT   CARBOHYD     92     92       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    217    217       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    317    317       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    369    369       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    402    402       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    407    407       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    421    421       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    508    508       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     72     88       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    173    249       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    206    228       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    239    267       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    348    364       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    444    516       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    506    534       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    615    631       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    711    772       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   DISULFID    739    751       {ECO:0000255|PROSITE-ProRule:PRU00274}.
FT   VAR_SEQ     503    507       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_046639.
FT   VAR_SEQ     661    763       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_044718.
FT   CONFLICT    135    135       E -> K (in Ref. 2; BAG62942).
FT                                {ECO:0000305}.
FT   CONFLICT    812    812       F -> L (in Ref. 1; CAF25303).
FT                                {ECO:0000305}.
SQ   SEQUENCE   855 AA;  91955 MW;  D1AF7888311FB871 CRC64;
     MARHLLLPLV MLVISPIPGA FQDSALSPTQ EEPEDLDCGR PEPSARIVGG SNAQPGTWPW
     QVSLHHGGGH ICGGSLIAPS WVLSAAHCFM TNGTLEPAAE WSVLLGVHSQ DGPLDGAHTR
     AVAAIVVPAN YSQVELGADL ALLRLASPAS LGPAVWPVCL PRASHRFVHG TACWATGWGD
     VQEADPLPLP WVLQEVELRL LGEATCQCLY SQPGPFNLTL QILPGMLCAG YPEGRRDTCQ
     GDSGGPLVCE EGGRWFQAGI TSFGFGCGRR NRPGVFTAVA TYEAWIREQV MGSEPGPAFP
     TQPQKTQSDP QEPREENCTI ALPECGKAPR PGAWPWEAQV MVPGSRPCHG ALVSESWVLA
     PASCFLDPNS SDSPPRDLDA WRVLLPSRPR AERVARLVQH ENASWDNASD LALLQLRTPV
     NLSAASRPVC LPHPEHYFLP GSRCRLARWG RGEPALGPGA LLEAELLGGW WCHCLYGRQG
     AAVPLPGDPP HALCPAYQEK EEVGSCWNDS RWSLLCQEEG TWFLAGIRDF PSGCLRPRAF
     FPLQTHGPWI SHVTRGAYLE DQLAWDWGPD GEETETQTCP PHTEHGACGL RLEAAPVGVL
     WPWLAEVHVA GDRVCTGILL APGWVLAATH CVLRPGSTTV PYIEVYLGRA GASSLPQGHQ
     VSRLVISIRL PQHLGLRPPL ALLELSSRVE PSPSALPICL HPAGIPPGAS CWVLGWKEPQ
     DRVPVAAAVS ILTQRICDCL YQGILPPGTL CVLYAEGQEN RCEMTSAPPL LCQMTEGSWI
     LVGMAVQGSR ELFAAIGPEE AWISQTVGEA NFLPPSGSPH WPTGGSNLCP PELAKASGSP
     HAVYFLLLLT LLIQS
//
