PRS23_MOUSE
ID PRS23_MOUSE Reviewed; 382 AA.
AC Q9D6X6; Q544M8; Q8VEG1;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine protease 23;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=Prss23;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Diencephalon, Spleen, and Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
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DR EMBL; AK009847; BAB26541.1; -; mRNA.
DR EMBL; AK034439; BAC28708.1; -; mRNA.
DR EMBL; AK078518; BAC37319.1; -; mRNA.
DR EMBL; AK156348; BAE33683.1; -; mRNA.
DR EMBL; BC018517; AAH18517.1; -; mRNA.
DR CCDS; CCDS21442.1; -.
DR RefSeq; NP_083890.2; NM_029614.3.
DR RefSeq; XP_006508367.1; XM_006508304.3.
DR RefSeq; XP_006508368.1; XM_006508305.1.
DR AlphaFoldDB; Q9D6X6; -.
DR BioGRID; 218133; 3.
DR IntAct; Q9D6X6; 1.
DR STRING; 10090.ENSMUSP00000045191; -.
DR GlyGen; Q9D6X6; 2 sites.
DR iPTMnet; Q9D6X6; -.
DR PhosphoSitePlus; Q9D6X6; -.
DR MaxQB; Q9D6X6; -.
DR PaxDb; Q9D6X6; -.
DR PeptideAtlas; Q9D6X6; -.
DR PRIDE; Q9D6X6; -.
DR ProteomicsDB; 291823; -.
DR Antibodypedia; 31454; 79 antibodies from 20 providers.
DR DNASU; 76453; -.
DR Ensembl; ENSMUST00000041761; ENSMUSP00000045191; ENSMUSG00000039405.
DR Ensembl; ENSMUST00000207932; ENSMUSP00000147183; ENSMUSG00000039405.
DR GeneID; 76453; -.
DR KEGG; mmu:76453; -.
DR UCSC; uc009ifz.1; mouse.
DR CTD; 11098; -.
DR MGI; MGI:1923703; Prss23.
DR VEuPathDB; HostDB:ENSMUSG00000039405; -.
DR eggNOG; ENOG502QTW6; Eukaryota.
DR GeneTree; ENSGT00390000000155; -.
DR HOGENOM; CLU_055829_0_0_1; -.
DR InParanoid; Q9D6X6; -.
DR OMA; RQQQKWE; -.
DR OrthoDB; 1245017at2759; -.
DR PhylomeDB; Q9D6X6; -.
DR TreeFam; TF329011; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 76453; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q9D6X6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D6X6; protein.
DR Bgee; ENSMUSG00000039405; Expressed in endothelial cell of lymphatic vessel and 256 other tissues.
DR ExpressionAtlas; Q9D6X6; baseline and differential.
DR Genevisible; Q9D6X6; MM.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR Pfam; PF00089; Trypsin; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..382
FT /note="Serine protease 23"
FT /id="PRO_0000027848"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10078"
FT ACT_SITE 239
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10078"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10078"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 159..175
FT /evidence="ECO:0000250"
FT CONFLICT 260
FT /note="M -> I (in Ref. 1; BAB26541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 43071 MW; 6F09A5C80A5B2306 CRC64;
MAGIPGLFIL LVLLCVFMQV SPYTVPWKPT WPAYRLPVVL PQSTLNLAKA DFDAKAKLEV
SSSCGPQCHK GTPLPTYEEA KQYLSYETLY ANGSRTETRV GIYILSNGEG RARGRDSEAT
GRSRRKRQIY GYDGRFSIFG KDFLLNYPFS TSVKLSTGCT GTLVAEKHVL TAAHCIHDGK
TYVKGTQKLR VGFLKPKYKD GAGGDNSSSS AMPDKMKFQW IRVKRTHVPK GWIKGNANDI
GMDYDYALLE LKKPHKRQFM KIGVSPPAKQ LPGGRIHFSG YDNDRPGNLV YRFCDVKDET
YDLLYQQCDA QPGASGSGVY VRMWKRPQQK WERKIIGIFS GHQWVDMNGS PQDFNVAVRI
TPLKYAQICY WIKGNYLDCR EG
