PRS28_MOUSE
ID PRS28_MOUSE Reviewed; 274 AA.
AC Q924N9; Q3UN30;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Serine protease 28;
DE EC=3.4.21.-;
DE AltName: Full=Implantation serine proteinase 1;
DE Short=ISP-1;
DE AltName: Full=Strypsin;
DE AltName: Full=Tryptase-like proteinase;
DE Flags: Precursor;
GN Name=Prss28; Synonyms=Isp1;
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP FUNCTION.
RC STRAIN=129/SvJ, and CD-1;
RX PubMed=11425330; DOI=10.1530/rep.0.1220061;
RA O'Sullivan C.M., Rancourt S.L., Liu S.Y., Rancourt D.E.;
RT "A novel murine tryptase involved in blastocyst hatching and outgrowth.";
RL Reproduction 122:61-71(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL TISSUE
RP SPECIFICITY, FUNCTION, REGULATION BY PROGESTERONE, AND SUBUNIT.
RX PubMed=15293213; DOI=10.1002/mrd.20115;
RA O'Sullivan C.M., Tang L., Xu H., Liu S., Rancourt D.E.;
RT "Origin of the murine implantation serine proteinase subfamily.";
RL Mol. Reprod. Dev. 69:126-136(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, REGULATION BY PROGESTERONE, AND
RP SUBUNITS.
RX PubMed=12112596; DOI=10.1002/mrd.10142;
RA O'Sullivan C.M., Liu S.Y., Karpinka J.B., Rancourt D.E.;
RT "Embryonic hatching enzyme strypsin/ISP1 is expressed with ISP2 in
RT endometrial glands during implantation.";
RL Mol. Reprod. Dev. 62:328-334(2002).
RN [6]
RP SUBCELLULAR LOCATION, REGULATION BY PROGESTERONE, SUBUNITS, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15349836; DOI=10.1002/mrd.20169;
RA O'Sullivan C.M., Ungarian J.L., Singh K., Liu S., Hance J., Rancourt D.E.;
RT "Uterine secretion of ISP1 & 2 tryptases is regulated by progesterone and
RT estrogen during pregnancy and the endometrial cycle.";
RL Mol. Reprod. Dev. 69:252-259(2004).
RN [7]
RP SUBUNITS, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=17156484; DOI=10.1186/1471-213x-6-61;
RA Sharma N., Liu S., Tang L., Irwin J., Meng G., Rancourt D.E.;
RT "Implantation serine proteinases heterodimerize and are critical in
RT hatching and implantation.";
RL BMC Dev. Biol. 6:61-61(2006).
CC -!- FUNCTION: Involved in embryo hatching and implantation.
CC {ECO:0000269|PubMed:11425330, ECO:0000269|PubMed:15293213,
CC ECO:0000269|PubMed:17156484}.
CC -!- ACTIVITY REGULATION: Inhibited by benzamidine, (4-amidino-phenyl)-
CC methane-sulfonyl (APMSF), N-p-tosyl-L-lysine chloromethylketone (TLCK),
CC gabexate, mesylate, BABIM and trypsin soybean inhibitor (TSI).
CC {ECO:0000269|PubMed:17156484}.
CC -!- SUBUNIT: Homooligomer, heterodimer and heterotetramer. Able to form
CC homo- and hetero- tetrameric structures. Heterotetramer is far more
CC stable than the homotetramer. {ECO:0000269|PubMed:12112596,
CC ECO:0000269|PubMed:15293213, ECO:0000269|PubMed:15349836,
CC ECO:0000269|PubMed:17156484}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Secretion into the
CC glandular and uterine lumen may occur as a consequence of progesterone-
CC induced epithelial differentiation. {ECO:0000269|PubMed:12112596,
CC ECO:0000269|PubMed:15349836}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos throughout the preimplantation
CC period, during blastocyst hatching and embryo outgrowth. Found in
CC uterus especially in glandular epithelium.
CC {ECO:0000269|PubMed:11425330, ECO:0000269|PubMed:12112596,
CC ECO:0000269|PubMed:15293213}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed from 6.5 dpc in embryo plus
CC deciduum. Faintly detectable at 11.5 dpc and 13.5 dpc in placenta. Not
CC detected at 8.5 dpc, 11.5 dpc and 13.5 dpc in embryo proper. Expressed
CC at 4.0 dpc in uterus. {ECO:0000269|PubMed:11425330,
CC ECO:0000269|PubMed:15349836}.
CC -!- INDUCTION: By progesterone.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF184895; AAK84171.1; -; mRNA.
DR EMBL; AY520825; AAT66743.1; -; Genomic_DNA.
DR EMBL; AK144498; BAE25918.1; -; mRNA.
DR EMBL; BC119386; AAI19387.1; -; mRNA.
DR EMBL; BC119388; AAI19389.1; -; mRNA.
DR CCDS; CCDS28515.1; -.
DR RefSeq; NP_444489.2; NM_053259.2.
DR AlphaFoldDB; Q924N9; -.
DR SMR; Q924N9; -.
DR STRING; 10090.ENSMUSP00000015267; -.
DR MEROPS; S01.314; -.
DR GlyGen; Q924N9; 1 site.
DR PaxDb; Q924N9; -.
DR PRIDE; Q924N9; -.
DR ProteomicsDB; 291899; -.
DR DNASU; 114661; -.
DR GeneID; 114661; -.
DR KEGG; mmu:114661; -.
DR UCSC; uc008ban.1; mouse.
DR CTD; 114661; -.
DR MGI; MGI:2149951; Prss28.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q924N9; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q924N9; -.
DR TreeFam; TF351676; -.
DR BioGRID-ORCS; 114661; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q924N9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q924N9; protein.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:MGI.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IMP:MGI.
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.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..274
FT /note="Serine protease 28"
FT /id="PRO_0000349225"
FT DOMAIN 31..274
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 77
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 227
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 158..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 191..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 223..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 36
FT /note="R -> C (in Ref. 3; BAE25918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 30628 MW; 47CCD1E2C4AEBBE5 CRC64;
MFRLLLLALS CLESTVFMAS VSISRSKPVG IVGGQRTPPG KWPWQVSLRM YSYEVNSWVH
ICGGSIIHPQ WILTAAHCIQ SQDADPAVYR VQVGEVYLYK EQELLNISRI IIHPDYNDVS
KRFDLALMQL TALLVTSTNV SPVSLPKDSS TFDSTDQCWL VGWGNLLQRV PLQPPYQLHE
VKIPIQDNKS CKRAYRKKSS DEHKAVAIFD DMLCAGTSGR GPCFGDSGGP LVCWKSNKWI
QVGVVSKGID CSNNLPSIFS RVQSSLAWIH QHIQ
