PRS58_MOUSE
ID PRS58_MOUSE Reviewed; 241 AA.
AC Q8BW11;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Putative inactive serine protease 58;
DE EC=3.4.21.4;
DE AltName: Full=Trypsin-X3;
DE Flags: Precursor;
GN Name=Prss58; Synonyms=Tryx3;
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 [GENOMIC DNA].
RX PubMed=11160223; DOI=10.4049/jimmunol.166.3.1771;
RA Chen F., Rowen L., Hood L., Rothenberg E.V.;
RT "Differential transcriptional regulation of individual TCR V beta segments
RT before gene rearrangement.";
RL J. Immunol. 166:1771-1780(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 MRNA].
RC TISSUE=Testis;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Thr-195 is present instead of the conserved Ser which is
CC expected to be an active site residue. It is therefore unsure if this
CC protein has kept its catalytic activity. {ECO:0000305}.
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DR EMBL; AE000663; AAB69042.1; -; Genomic_DNA.
DR EMBL; AK075754; BAC35932.1; -; mRNA.
DR EMBL; BC048599; AAH48599.1; -; mRNA.
DR CCDS; CCDS20040.1; -.
DR RefSeq; NP_778185.1; NM_175020.3.
DR AlphaFoldDB; Q8BW11; -.
DR SMR; Q8BW11; -.
DR STRING; 10090.ENSMUSP00000069833; -.
DR MEROPS; S01.984; -.
DR GlyGen; Q8BW11; 1 site.
DR iPTMnet; Q8BW11; -.
DR PhosphoSitePlus; Q8BW11; -.
DR PaxDb; Q8BW11; -.
DR PRIDE; Q8BW11; -.
DR ProteomicsDB; 291681; -.
DR Antibodypedia; 50270; 32 antibodies from 9 providers.
DR DNASU; 232717; -.
DR Ensembl; ENSMUST00000063523; ENSMUSP00000069833; ENSMUSG00000051936.
DR GeneID; 232717; -.
DR KEGG; mmu:232717; -.
DR UCSC; uc009bnk.1; mouse.
DR CTD; 136541; -.
DR MGI; MGI:3608323; Prss58.
DR VEuPathDB; HostDB:ENSMUSG00000051936; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_6_1; -.
DR InParanoid; Q8BW11; -.
DR OMA; KESMLCV; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8BW11; -.
DR TreeFam; TF331065; -.
DR BioGRID-ORCS; 232717; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8BW11; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BW11; protein.
DR Bgee; ENSMUSG00000051936; Expressed in spermatid and 4 other tissues.
DR Genevisible; Q8BW11; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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 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.
PE 2: Evidence at transcript 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..241
FT /note="Putative inactive serine protease 58"
FT /id="PRO_0000317764"
FT DOMAIN 18..239
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 56
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 101
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 133..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 165..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 191..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 241 AA; 26865 MW; 8FC9D0D994A4AE7F CRC64;
MKLAFLCILS TLLRTFAYNP DHIAGTTPPY LVYLKSDYLP CTGVLIHPLW VITAAHCNLP
NLQVILGITN PADPMERDVE VSDYEKIFHH PNFLVSSISH DLLLIKLKRR IKHSNYAKAV
KLPQHIVSVN AMCSVSTWAY NLCDVTKDPD SLQTVNVTVI SKAECRNAYK AFDITENMIC
VGIVPGRRLP CKEVTAAPAV CNGVLYGILS YADGCVLRAD VGIYASIFHY LPWIEDTMKN
N
