GenomeNet

Database: UniProt
Entry: Q9D1A6_MOUSE
LinkDB: Q9D1A6_MOUSE
Original site: Q9D1A6_MOUSE 
ID   Q9D1A6_MOUSE            Unreviewed;       160 AA.
AC   Q9D1A6;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-NOV-2023, entry version 103.
DE   RecName: Full=Lon proteolytic domain-containing protein {ECO:0000259|PROSITE:PS51786};
GN   Name=Lonp2 {ECO:0000313|MGI:MGI:1914137};
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:BAB22984.1};
RN   [1] {ECO:0000313|EMBL:BAB22984.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22984.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAB22984.1};
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:BAB22984.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22984.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAB22984.1};
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:BAB22984.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22984.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAB22984.1};
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:BAB22984.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22984.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAB22984.1};
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H., Arakawa T.,
RA   Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M., Hanagaki T.,
RA   Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H., Kawai J., Kojima Y.,
RA   Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., Miyazaki A.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Okazaki Y., Okido T., Owa C.,
RA   Saito H., Saito R., Sakai C., Sakai K., Sano H., Sasaki D., Shibata K.,
RA   Shibata Y., Shinagawa A., Shiraki T., Sogabe Y., Suzuki H., Tagami M.,
RA   Tagawa A., Takahashi F., Tanaka T., Tejima Y., Toya T., Yamamura T.,
RA   Yasunishi A., Yoshida K., Yoshino M., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:BAB22984.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22984.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAB22984.1};
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   [6] {ECO:0000313|EMBL:BAB22984.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22984.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAB22984.1};
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   [7] {ECO:0000313|EMBL:BAB22984.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22984.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAB22984.1};
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:BAB22984.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAB22984.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAB22984.1};
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   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01122}.
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; AK003766; BAB22984.1; -; mRNA.
DR   AlphaFoldDB; Q9D1A6; -.
DR   PeptideAtlas; Q9D1A6; -.
DR   AGR; MGI:1914137; -.
DR   MGI; MGI:1914137; Lonp2.
DR   ChiTaRS; Lonp2; mouse.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR   PROSITE; PS01046; LON_SER; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   DOMAIN          1..145
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ   SEQUENCE   160 AA;  17220 MW;  BFAF1085BF8C3657 CRC64;
     MKESAHLAIS WLRSNAKKYH LTNAFGSFDL LDNTDIHLHF PAGAVTKDGP SAGVTIVTCL
     ASLFSGRLVR SDVAMTGEIT LRGLVLPVGG IKDKVLAAHR AGLKQIIIPQ RNEKDLEEIP
     SNVRQDLSFV TASCLDEVLN AAFDGGFPVK TRPGLIDSKL
//
DBGET integrated database retrieval system