ID   PRS27_RAT               Reviewed;         328 AA.
AC   Q6BEA2;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
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;
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   STRAIN=Wistar; TISSUE=Limbal epithelium;
RA   Adachi W., Norman B., Davis J., Piatigorsky J.;
RT   "Comprehensive analysis of gene expression of rat corneal epithelium and
RT   limbal epithelium.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AB101677; BAC81507.1; -; mRNA.
DR   RefSeq; NP_891994.3; NM_182949.3.
DR   AlphaFoldDB; Q6BEA2; -.
DR   SMR; Q6BEA2; -.
DR   STRING; 10116.ENSRNOP00000007392; -.
DR   MEROPS; S01.074; -.
DR   GlyGen; Q6BEA2; 1 site.
DR   PaxDb; Q6BEA2; -.
DR   PRIDE; Q6BEA2; -.
DR   Ensembl; ENSRNOT00000007392; ENSRNOP00000007392; ENSRNOG00000005336.
DR   GeneID; 287108; -.
DR   KEGG; rno:287108; -.
DR   UCSC; RGD:1303256; rat.
DR   CTD; 83886; -.
DR   RGD; 1303256; Prss27.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000162015; -.
DR   InParanoid; Q6BEA2; -.
DR   OMA; YILPVCM; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q6BEA2; -.
DR   TreeFam; TF351676; -.
DR   PRO; PR:Q6BEA2; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000005336; Expressed in esophagus and 3 other tissues.
DR   ExpressionAtlas; Q6BEA2; baseline and differential.
DR   Genevisible; Q6BEA2; RN.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
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   2: Evidence at transcript 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..37
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027510"
FT   CHAIN           38..328
FT                   /note="Serine protease 27"
FT                   /id="PRO_0000027511"
FT   DOMAIN          38..280
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        78
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        127
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        232
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        161..238
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        194..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        228..256
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   328 AA;  35803 MW;  9235EECAF62C1358 CRC64;
     MRQPHITALL LLPLLLRSGT EGAEAMRACG HPRMFNRMVG GEDALEGEWP WQVSIQRNGA
     HFCGGSLIAP TWVLTAAHCF SNTSDISIYQ VLLGALKLQQ PGPHALYVPV KRVKSHPEYQ
     GMASSADVAL VELQVPVTFT KYILPVCLPD PSVVFKSGMN CWVTGWGSPS EQDRLPNPRI
     LQKLAVPLID TPKCNLLYSK DAEADIQLKT IKDDMLCAGF AEGKKDACKG DSGGPLVCLV
     DQSWVQAGVI SWGEGCARRN RPGVYIRVAS HYQWIHQIIP ELQFQGRAGS QQQQRDPRGW
     QPLAENSAPC LAAHAVLLAL GALMLGIL