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Serine protease 28 (EC 3.4.21.-) (Implantation serine proteinase 1) (ISP-1) (Strypsin) (Tryptase-like proteinase)

 PRS28_MOUSE             Reviewed;         274 AA.
Q924N9; Q3UN30;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
30-AUG-2017, entry version 109.
RecName: Full=Serine protease 28;
EC=3.4.21.-;
AltName: Full=Implantation serine proteinase 1;
Short=ISP-1;
AltName: Full=Strypsin;
AltName: Full=Tryptase-like proteinase;
Flags: Precursor;
Name=Prss28; Synonyms=Isp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
AND FUNCTION.
STRAIN=129/SvJ, and CD-1;
PubMed=11425330; DOI=10.1530/rep.0.1220061;
O'Sullivan C.M., Rancourt S.L., Liu S.Y., Rancourt D.E.;
"A novel murine tryptase involved in blastocyst hatching and
outgrowth.";
Reproduction 122:61-71(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL
TISSUE SPECIFICITY, FUNCTION, REGULATION BY PROGESTERONE, AND SUBUNIT.
PubMed=15293213; DOI=10.1002/mrd.20115;
O'Sullivan C.M., Tang L., Xu H., Liu S., Rancourt D.E.;
"Origin of the murine implantation serine proteinase subfamily.";
Mol. Reprod. Dev. 69:126-136(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, REGULATION BY PROGESTERONE,
AND SUBUNITS.
PubMed=12112596; DOI=10.1002/mrd.10142;
O'Sullivan C.M., Liu S.Y., Karpinka J.B., Rancourt D.E.;
"Embryonic hatching enzyme strypsin/ISP1 is expressed with ISP2 in
endometrial glands during implantation.";
Mol. Reprod. Dev. 62:328-334(2002).
[6]
SUBCELLULAR LOCATION, REGULATION BY PROGESTERONE, SUBUNITS, AND
DEVELOPMENTAL STAGE.
PubMed=15349836; DOI=10.1002/mrd.20169;
O'Sullivan C.M., Ungarian J.L., Singh K., Liu S., Hance J.,
Rancourt D.E.;
"Uterine secretion of ISP1 & 2 tryptases is regulated by progesterone
and estrogen during pregnancy and the endometrial cycle.";
Mol. Reprod. Dev. 69:252-259(2004).
[7]
SUBUNITS, ENZYME REGULATION, AND FUNCTION.
PubMed=17156484; DOI=10.1186/1471-213X-6-61;
Sharma N., Liu S., Tang L., Irwin J., Meng G., Rancourt D.E.;
"Implantation serine proteinases heterodimerize and are critical in
hatching and implantation.";
BMC Dev. Biol. 6:61-61(2006).
-!- FUNCTION: Involved in embryo hatching and implantation.
{ECO:0000269|PubMed:11425330, ECO:0000269|PubMed:15293213,
ECO:0000269|PubMed:17156484}.
-!- ENZYME REGULATION: Inhibited by benzamidine, (4-amidino-phenyl)-
methane-sulfonyl (APMSF), N-p-tosyl-L-lysine chloromethylketone
(TLCK), gabexate, mesylate, BABIM and trypsin soybean inhibitor
(TSI). {ECO:0000269|PubMed:17156484}.
-!- SUBUNIT: Homooligomer, heterodimer and heterotetramer. Able to
form homo- and hetero- tetrameric structures. Heterotetramer is
far more stable than the homotetramer.
{ECO:0000269|PubMed:12112596, ECO:0000269|PubMed:15293213,
ECO:0000269|PubMed:15349836, ECO:0000269|PubMed:17156484}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Secretion into
the glandular and uterine lumen may occur as a consequence of
progesterone-induced epithelial differentiation.
{ECO:0000269|PubMed:12112596, ECO:0000269|PubMed:15349836}.
-!- TISSUE SPECIFICITY: Expressed in embryos throughout the
preimplantation period, during blastocyst hatching and embryo
outgrowth. Found in uterus especially in glandular epithelium.
{ECO:0000269|PubMed:11425330, ECO:0000269|PubMed:12112596,
ECO:0000269|PubMed:15293213}.
-!- DEVELOPMENTAL STAGE: Highly expressed from E6.5 in embryo plus
deciduum. Faintly detectable at E11.5 and E13.5 in placenta. Not
detected at E8.5, E11.5 and E13.5 in embryo proper. Expressed at
E4.0 in uterus. {ECO:0000269|PubMed:11425330,
ECO:0000269|PubMed:15349836}.
-!- INDUCTION: By progesterone.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; AF184895; AAK84171.1; -; mRNA.
EMBL; AY520825; AAT66743.1; -; Genomic_DNA.
EMBL; AK144498; BAE25918.1; -; mRNA.
EMBL; BC119386; AAI19387.1; -; mRNA.
EMBL; BC119388; AAI19389.1; -; mRNA.
CCDS; CCDS28515.1; -.
RefSeq; NP_444489.2; NM_053259.2.
UniGene; Mm.207081; -.
ProteinModelPortal; Q924N9; -.
SMR; Q924N9; -.
STRING; 10090.ENSMUSP00000015267; -.
MEROPS; S01.314; -.
PaxDb; Q924N9; -.
PRIDE; Q924N9; -.
GeneID; 114661; -.
KEGG; mmu:114661; -.
UCSC; uc008ban.1; mouse.
CTD; 114661; -.
MGI; MGI:2149951; Prss28.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q924N9; -.
PhylomeDB; Q924N9; -.
TreeFam; TF351676; -.
PRO; PR:Q924N9; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005576; C:extracellular region; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; IDA:MGI.
GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
GO; GO:0007566; P:embryo implantation; IMP:MGI.
GO; GO:0006508; P:proteolysis; IMP:MGI.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Protease;
Reference proteome; Secreted; Serine protease; Signal.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 274 Serine protease 28.
/FTId=PRO_0000349225.
DOMAIN 31 274 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 77 77 Charge relay system. {ECO:0000250}.
ACT_SITE 124 124 Charge relay system. {ECO:0000250}.
ACT_SITE 227 227 Charge relay system. {ECO:0000250}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 62 78 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 158 233 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 191 214 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 223 251 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 36 36 R -> C (in Ref. 3; BAE25918).
{ECO:0000305}.
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


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