ID Q8BNF3_MOUSE Unreviewed; 320 AA. AC Q8BNF3; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=Peptidase S53 domain-containing protein {ECO:0000259|PROSITE:PS51695}; 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 {ECO:0000313|EMBL:BAC39034.1}; RN [1] {ECO:0000313|EMBL:BAC39034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39034.1}; RC TISSUE=Spinal ganglion {ECO:0000313|EMBL:BAC39034.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAC39034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39034.1}; RC TISSUE=Spinal ganglion {ECO:0000313|EMBL:BAC39034.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAC39034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39034.1}; RC TISSUE=Spinal ganglion {ECO:0000313|EMBL:BAC39034.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAC39034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39034.1}; RC TISSUE=Spinal ganglion {ECO:0000313|EMBL:BAC39034.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAC39034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39034.1}; RC TISSUE=Spinal ganglion {ECO:0000313|EMBL:BAC39034.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAC39034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39034.1}; RC TISSUE=Spinal ganglion {ECO:0000313|EMBL:BAC39034.1}; RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P., RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K., RA Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K., RA Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y., RA Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., RA Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R., RA Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K., RA Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T., RA Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S., RA Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M., RA Hayashizaki Y.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAC39034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39034.1}; RC TISSUE=Spinal ganglion {ECO:0000313|EMBL:BAC39034.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAC39034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39034.1}; RC TISSUE=Spinal ganglion {ECO:0000313|EMBL:BAC39034.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01032}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE- CC ProRule:PRU01032}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK083832; BAC39034.1; -; mRNA. DR AlphaFoldDB; Q8BNF3; -. DR MEROPS; S53.003; -. DR PeptideAtlas; Q8BNF3; -. DR ChiTaRS; Tpp1; mouse. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd04056; Peptidases_S53; 1. DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1. DR InterPro; IPR000209; Peptidase_S8/S53_dom. DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf. DR InterPro; IPR030400; Sedolisin_dom. DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1. DR PANTHER; PTHR14218:SF15; TRIPEPTIDYL-PEPTIDASE 1; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR SUPFAM; SSF52743; Subtilisin-like; 1. DR PROSITE; PS51695; SEDOLISIN; 1. PE 2: Evidence at transcript level; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813}; KW Calcium {ECO:0000256|PROSITE-ProRule:PRU01032}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032}; KW Protease {ECO:0000256|PROSITE-ProRule:PRU01032}; KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}. FT DOMAIN 1..320 FT /note="Peptidase S53" FT /evidence="ECO:0000259|PROSITE:PS51695" FT ACT_SITE 29 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT ACT_SITE 33 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT ACT_SITE 232 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 274 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 275 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 298 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 300 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" SQ SEQUENCE 320 AA; 34523 MW; 91DC3FBF778631C8 CRC64; MRLFGGSFTH QASVAKVVGK QGRGRAGIEA SLDVEYLMSA GANISTWVYS SPGRHEAQEP FLQWLLLLSN ESSLPHVHTV SYGDDEDSLS SIYIQRVNTE FMKAAARGLT LLFASGDTGA GCWSVSGRHK FRPSFPASSP YVTTVGGTSF KNPFLITDEV VDYISGGGFS NVFPRPPYQE EAVAQFLKSS SHLPPSSYFN ASGRAYPDVA ALSDGYWVVS NMVPIPWVSG TSASTPVFGG ILSLINEHRI LNGRPPLGFL NPRLYQQHGT GLFDVTHGCH ESCLNEEVEG QGFCSGPGWD PVTGWGTPNF PALLKTLLNP //