ID   CATO_MOUSE              Reviewed;         312 AA.
AC   Q8BM88; Q3TM69; Q80V35; Q8BKX0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Cathepsin O;
DE            EC=3.4.22.42;
DE   Flags: Precursor;
GN   Name=Ctso;
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; TISSUE=Diencephalon, Embryo, and Lung;
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] OF 21-312.
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   -!- FUNCTION: Proteolytic enzyme possibly involved in normal cellular
CC       protein degradation and turnover. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The recombinant human enzyme hydrolyzes synthetic
CC         endopeptidase substrates including Z-Phe-Arg-NHMec and Z-Arg-Arg-
CC         NHMec.; EC=3.4.22.42;
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089}.
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; AK034490; BAC28728.1; -; mRNA.
DR   EMBL; AK049470; BAC33765.1; -; mRNA.
DR   EMBL; AK165930; BAE38466.1; -; mRNA.
DR   EMBL; AK166103; BAE38573.1; -; mRNA.
DR   EMBL; BC044664; AAH44664.1; -; mRNA.
DR   CCDS; CCDS17426.1; -.
DR   RefSeq; NP_808330.1; NM_177662.3.
DR   AlphaFoldDB; Q8BM88; -.
DR   SMR; Q8BM88; -.
DR   STRING; 10090.ENSMUSP00000029649; -.
DR   MEROPS; C01.035; -.
DR   GlyCosmos; Q8BM88; 2 sites, No reported glycans.
DR   GlyGen; Q8BM88; 2 sites.
DR   iPTMnet; Q8BM88; -.
DR   PhosphoSitePlus; Q8BM88; -.
DR   MaxQB; Q8BM88; -.
DR   PaxDb; 10090-ENSMUSP00000029649; -.
DR   ProteomicsDB; 265447; -.
DR   Antibodypedia; 48148; 144 antibodies from 26 providers.
DR   DNASU; 229445; -.
DR   Ensembl; ENSMUST00000029649.3; ENSMUSP00000029649.3; ENSMUSG00000028015.4.
DR   GeneID; 229445; -.
DR   KEGG; mmu:229445; -.
DR   UCSC; uc008pon.1; mouse.
DR   AGR; MGI:2139628; -.
DR   CTD; 1519; -.
DR   MGI; MGI:2139628; Ctso.
DR   VEuPathDB; HostDB:ENSMUSG00000028015; -.
DR   eggNOG; KOG1542; Eukaryota.
DR   GeneTree; ENSGT00940000159253; -.
DR   HOGENOM; CLU_012184_1_3_1; -.
DR   InParanoid; Q8BM88; -.
DR   OMA; FPHENST; -.
DR   OrthoDB; 5472948at2759; -.
DR   PhylomeDB; Q8BM88; -.
DR   TreeFam; TF331594; -.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   BioGRID-ORCS; 229445; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Ctso; mouse.
DR   PRO; PR:Q8BM88; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8BM88; Protein.
DR   Bgee; ENSMUSG00000028015; Expressed in gastrula and 218 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   PANTHER; PTHR12411:SF947; CATHEPSIN O; 1.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
DR   Genevisible; Q8BM88; MM.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW   Reference proteome; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..98
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026323"
FT   CHAIN           99..312
FT                   /note="Cathepsin O"
FT                   /id="PRO_0000026324"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        120..161
FT                   /evidence="ECO:0000250"
FT   DISULFID        154..195
FT                   /evidence="ECO:0000250"
FT   DISULFID        253..301
FT                   /evidence="ECO:0000250"
FT   CONFLICT        63
FT                   /note="F -> L (in Ref. 1; BAC33765)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   312 AA;  34723 MW;  4C7C056D0771807C CRC64;
     MKPQLVNLLL LCCCCLGRHG VAGTWSWSHQ REAAALRESL HRHRYLNSFP HENSTAFYGV
     NQFSYLFPEE FKALYLGSKY AWAPRYPAEG QRPIPNVSLP LRFDWRDKHV VNPVRNQEMC
     GGCWAFSVVS AIESARAIQG KSLDYLSVQQ VIDCSFNNSG CLGGSPLCAL RWLNETQLKL
     VADSQYPFKA VNGQCRHFPQ SQAGVSVKDF SAYNFRGQED EMARALLSFG PLVVIVDAMS
     WQDYLGGIIQ HHCSSGEANH AVLITGFDRT GNTPYWMVRN SWGSSWGVEG YAHVKMGGNV
     CGIADSVAAV FV
//