PRS29_MOUSE
ID PRS29_MOUSE Reviewed; 279 AA.
AC Q99MS4; Q3MI54; Q3UN95;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Serine protease 29;
DE EC=3.4.21.-;
DE AltName: Full=Implantation serine proteinase 2;
DE Short=ISP-2;
DE AltName: Full=Strypsin-2;
DE AltName: Full=Strypsin-related protein;
DE AltName: Full=Tryptase-like proteinase;
DE Flags: Precursor;
GN Name=Prss29; Synonyms=Isp2;
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,
RP INDUCTION, AND FUNCTION.
RC STRAIN=129/SvJ; TISSUE=Embryo;
RX PubMed=11467974; DOI=10.1530/rep.0.1220235;
RA O'Sullivan C.M., Liu S.Y., Rancourt S.L., Rancourt D.E.;
RT "Regulation of the strypsin-related proteinase ISP2 by progesterone in
RT endometrial gland epithelium during implantation in mice.";
RL Reproduction 122:235-244(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Uterus;
RX PubMed=12883636;
RA Huang Z.P., Wang J., Yu H., Shen W.X., Huang P., Tso J.K., Yang Z.M.,
RA Shen Q.X.;
RT "Cloning, expression, and antibody production of mouse ISP2.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:649-654(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
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 [7]
RP SUBCELLULAR LOCATION, INDUCTION, SUBUNIT, AND 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 [8]
RP INDUCTION, AND FUNCTION.
RX PubMed=15304212; DOI=10.10371/rd03102;
RA Huang Z.P., Yu H., Yang Z.M., Shen W.X., Wang J., Shen Q.X.;
RT "Uterine expression of implantation serine proteinase 2 during the
RT implantation period and in vivo inhibitory effect of its antibody on embryo
RT implantation in mice.";
RL Reprod. Fertil. Dev. 16:379-384(2004).
RN [9]
RP SUBUNIT, 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:11467974, ECO:0000269|PubMed:15304212,
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:15349836, ECO:0000269|PubMed:17156484}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12112596,
CC ECO:0000269|PubMed:15349836}. Note=Secretion into the glandular and
CC uterine lumen may occur as a consequence of progesterone-induced
CC epithelial differentiation.
CC -!- TISSUE SPECIFICITY: Expressed in embryos and placenta. Found in uterus
CC especially in glandular epithelium during zona lysis and implantation.
CC {ECO:0000269|PubMed:11467974, ECO:0000269|PubMed:12112596}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed from 6.5 dpc plus deciduum. Also
CC expressed, but to a lower extent, in placenta from 11.5 dpc and 13.5
CC dpc. Not expressed at 8.5 dpc and 11.5 dpc in embryo proper. Expressed
CC at 4.0 dpc in uterus. {ECO:0000269|PubMed:11467974,
CC ECO:0000269|PubMed:12883636, ECO:0000269|PubMed:15349836}.
CC -!- INDUCTION: Up-regulated in uterine endometrial glands following the
CC initiation of embryo implantation. By progesterone.
CC {ECO:0000269|PubMed:11467974, ECO:0000269|PubMed:15304212,
CC ECO:0000269|PubMed:15349836}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF305425; AAK15264.2; -; mRNA.
DR EMBL; AF442819; AAL38005.1; -; mRNA.
DR EMBL; AY520825; AAT66744.1; -; Genomic_DNA.
DR EMBL; AK144368; BAE25852.1; -; mRNA.
DR EMBL; BC104122; AAI04123.1; -; mRNA.
DR EMBL; BC104123; AAI04124.1; -; mRNA.
DR CCDS; CCDS28516.1; -.
DR RefSeq; NP_444490.2; NM_053260.3.
DR AlphaFoldDB; Q99MS4; -.
DR SMR; Q99MS4; -.
DR STRING; 10090.ENSMUSP00000024993; -.
DR MEROPS; S01.315; -.
DR GlyGen; Q99MS4; 2 sites.
DR jPOST; Q99MS4; -.
DR PaxDb; Q99MS4; -.
DR PRIDE; Q99MS4; -.
DR ProteomicsDB; 291749; -.
DR DNASU; 114662; -.
DR GeneID; 114662; -.
DR KEGG; mmu:114662; -.
DR CTD; 114662; -.
DR MGI; MGI:2149952; Prss29.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q99MS4; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q99MS4; -.
DR BioGRID-ORCS; 114662; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q99MS4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99MS4; protein.
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; IGI:MGI.
DR GO; GO:0006508; P:proteolysis; IDA: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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..279
FT /note="Serine protease 29"
FT /id="PRO_0000349226"
FT DOMAIN 31..276
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 228
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 158..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 191..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 224..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 1
FT /note="M -> L (in Ref. 5; AAI04124)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="D -> G (in Ref. 4; BAE25852)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="P -> S (in Ref. 4; BAE25852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 30986 MW; 81C43A59935244D7 CRC64;
MLIQLCLTLF FLGCSIAGTP APGPEDVLMG IVGGHSAPQG KWPWQVSLRI YRYYWAFWVH
NCGGSIIHPQ WVLTAAHCIR ERDADPSVFR IRVGEAYLYG GKELLSVSRV IIHPDFVHAG
LGSDVALLQL AVSVQSFPNV KPVKLPSESL EVTKKDVCWV TGWGAVSTHR SLPPPYRLQQ
VQVKIIDNSL CEEMYHNATR HRNRGQKLIL KDMLCAGNQG QDSCYGDSGG PLVCNVTGSW
TLVGVVSWGY GCALRDFPGV YARVQSFLPW ITQQMQRFS
