CATO_MOUSE
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 03-AUG-2022, entry version 128.
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}.
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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 GlyGen; Q8BM88; 2 sites.
DR iPTMnet; Q8BM88; -.
DR PhosphoSitePlus; Q8BM88; -.
DR MaxQB; Q8BM88; -.
DR PaxDb; Q8BM88; -.
DR PRIDE; Q8BM88; -.
DR ProteomicsDB; 265447; -.
DR Antibodypedia; 48148; 135 antibodies from 26 providers.
DR DNASU; 229445; -.
DR Ensembl; ENSMUST00000029649; ENSMUSP00000029649; ENSMUSG00000028015.
DR GeneID; 229445; -.
DR KEGG; mmu:229445; -.
DR UCSC; uc008pon.1; mouse.
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; QNGLCRY; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q8BM88; -.
DR TreeFam; TF331594; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR BioGRID-ORCS; 229445; 2 hits in 71 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 215 other tissues.
DR Genevisible; Q8BM88; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
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 InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
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
