PRS27_MOUSE
ID PRS27_MOUSE Reviewed; 328 AA.
AC Q8BJR6; Q14A25;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 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=Urinary bladder;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF542056; AAO27572.1; -; mRNA.
DR EMBL; AK080281; BAC37864.1; -; mRNA.
DR EMBL; AY162410; AAO17162.1; -; Genomic_DNA.
DR EMBL; BC117009; AAI17010.1; -; mRNA.
DR EMBL; BC117011; AAI17012.1; -; mRNA.
DR CCDS; CCDS28472.1; -.
DR RefSeq; NP_780649.1; NM_175440.4.
DR AlphaFoldDB; Q8BJR6; -.
DR SMR; Q8BJR6; -.
DR STRING; 10090.ENSMUSP00000056483; -.
DR MEROPS; S01.074; -.
DR GlyGen; Q8BJR6; 1 site.
DR PhosphoSitePlus; Q8BJR6; -.
DR PaxDb; Q8BJR6; -.
DR PRIDE; Q8BJR6; -.
DR ProteomicsDB; 291898; -.
DR Antibodypedia; 23859; 223 antibodies from 23 providers.
DR DNASU; 213171; -.
DR Ensembl; ENSMUST00000059482; ENSMUSP00000056483; ENSMUSG00000050762.
DR GeneID; 213171; -.
DR KEGG; mmu:213171; -.
DR UCSC; uc008aug.1; mouse.
DR CTD; 83886; -.
DR MGI; MGI:2450123; Prss27.
DR VEuPathDB; HostDB:ENSMUSG00000050762; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162015; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q8BJR6; -.
DR OMA; YILPVCM; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8BJR6; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 213171; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8BJR6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BJR6; protein.
DR Bgee; ENSMUSG00000050762; Expressed in esophagus and 31 other tissues.
DR Genevisible; Q8BJR6; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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_0000027508"
FT CHAIN 38..328
FT /note="Serine protease 27"
FT /id="PRO_0000027509"
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; 35789 MW; DC0B20F1AB3EB840 CRC64;
MRQPHIAALL LLPLLLRSGT EGARTLRACG HPKMFNRMVG GENALEGEWP WQVSIQRNGI
HFCGGSLIAP TWVLTAAHCF SNTSDISIYQ VLLGALKLQQ PGPHALYVPV KQVKSNPQYQ
GMASSADVAL VELQGPVTFT NYILPVCLPD PSVIFESGMN CWVTGWGSPS EQDRLPNPRV
LQKLAVPIID TPKCNLLYNK DVESDFQLKT IKDDMLCAGF AEGKKDACKG DSGGPLVCLV
DQSWVQAGVI SWGEGCARRN RPGVYIRVTS HHKWIHQIIP ELQFQGRAGT QQQQKDSQGQ
QRLAGNSAPC LAAHAMVLAL GALLLRIV
