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PRS27_HUMAN
ID   PRS27_HUMAN             Reviewed;         290 AA.
AC   Q9BQR3;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Serine protease 27;
DE            EC=3.4.21.-;
DE   AltName: Full=Marapsin;
DE   AltName: Full=Pancreasin;
DE   Flags: Precursor;
GN   Name=PRSS27; Synonyms=MPN; ORFNames=UNQ1884/PRO4327;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Fortunato M., Dando P.M., Rawlings N.D., Barrett A.J.;
RT   "Cloning, sequencing and expression of marapsin, a human serine
RT   proteinase.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Okaze H., Hayashi A., Kozuma S., Saito T.;
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX   PubMed=12441343; DOI=10.1074/jbc.m209353200;
RA   Bhagwandin V.J., Hau L.W.-T., Mallen-St Clair J., Wolters P.J.,
RA   Caughey G.H.;
RT   "Structure and activity of human pancreasin, a novel tryptic serine
RT   peptidase expressed primarily by the pancreas.";
RL   J. Biol. Chem. 278:3363-3371(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the pancreas.
CC       {ECO:0000269|PubMed:12441343}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12441343}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AJ306593; CAC35467.1; -; mRNA.
DR   EMBL; AB056161; BAB85497.1; -; mRNA.
DR   EMBL; AY030095; AAK38168.1; -; mRNA.
DR   EMBL; AY359106; AAQ89464.1; -; mRNA.
DR   EMBL; BC034294; AAH34294.1; -; mRNA.
DR   CCDS; CCDS10476.1; -.
DR   RefSeq; NP_001305324.1; NM_001318395.1.
DR   RefSeq; NP_114154.1; NM_031948.4.
DR   AlphaFoldDB; Q9BQR3; -.
DR   SMR; Q9BQR3; -.
DR   BioGRID; 123797; 1.
DR   STRING; 9606.ENSP00000306390; -.
DR   MEROPS; S01.074; -.
DR   GlyGen; Q9BQR3; 2 sites.
DR   iPTMnet; Q9BQR3; -.
DR   PhosphoSitePlus; Q9BQR3; -.
DR   BioMuta; PRSS27; -.
DR   DMDM; 18202734; -.
DR   MassIVE; Q9BQR3; -.
DR   PaxDb; Q9BQR3; -.
DR   PeptideAtlas; Q9BQR3; -.
DR   PRIDE; Q9BQR3; -.
DR   ProteomicsDB; 78710; -.
DR   Antibodypedia; 23859; 223 antibodies from 23 providers.
DR   DNASU; 83886; -.
DR   Ensembl; ENST00000302641.8; ENSP00000306390.3; ENSG00000172382.10.
DR   GeneID; 83886; -.
DR   KEGG; hsa:83886; -.
DR   MANE-Select; ENST00000302641.8; ENSP00000306390.3; NM_031948.5; NP_114154.1.
DR   UCSC; uc002crf.4; human.
DR   CTD; 83886; -.
DR   DisGeNET; 83886; -.
DR   GeneCards; PRSS27; -.
DR   HGNC; HGNC:15475; PRSS27.
DR   HPA; ENSG00000172382; Group enriched (esophagus, vagina).
DR   MIM; 608018; gene.
DR   neXtProt; NX_Q9BQR3; -.
DR   OpenTargets; ENSG00000172382; -.
DR   PharmGKB; PA33837; -.
DR   VEuPathDB; HostDB:ENSG00000172382; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000162015; -.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; Q9BQR3; -.
DR   OMA; YILPVCM; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q9BQR3; -.
DR   TreeFam; TF351676; -.
DR   PathwayCommons; Q9BQR3; -.
DR   SignaLink; Q9BQR3; -.
DR   BioGRID-ORCS; 83886; 12 hits in 1066 CRISPR screens.
DR   GenomeRNAi; 83886; -.
DR   Pharos; Q9BQR3; Tbio.
DR   PRO; PR:Q9BQR3; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9BQR3; protein.
DR   Bgee; ENSG00000172382; Expressed in lower esophagus mucosa and 103 other tissues.
DR   ExpressionAtlas; Q9BQR3; baseline and differential.
DR   Genevisible; Q9BQR3; HS.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 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; 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   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..34
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027506"
FT   CHAIN           35..290
FT                   /note="Serine protease 27"
FT                   /id="PRO_0000027507"
FT   DOMAIN          35..277
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        124
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        229
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        158..235
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        191..214
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        225..253
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   290 AA;  31940 MW;  67BDC93EC70BFF7B CRC64;
     MRRPAAVPLL LLLCFGSQRA KAATACGRPR MLNRMVGGQD TQEGEWPWQV SIQRNGSHFC
     GGSLIAEQWV LTAAHCFRNT SETSLYQVLL GARQLVQPGP HAMYARVRQV ESNPLYQGTA
     SSADVALVEL EAPVPFTNYI LPVCLPDPSV IFETGMNCWV TGWGSPSEED LLPEPRILQK
     LAVPIIDTPK CNLLYSKDTE FGYQPKTIKN DMLCAGFEEG KKDACKGDSG GPLVCLVGQS
     WLQAGVISWG EGCARQNRPG VYIRVTAHHN WIHRIIPKLQ FQPARLGGQK
 
 
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