CATM_MOUSE
ID CATM_MOUSE Reviewed; 333 AA.
AC Q9JL96; Q91Z75; Q91ZF3; Q9CQB9;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cathepsin M;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=Ctsm; Synonyms=Catm;
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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND VARIANT
RP SER-272.
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=10760593; DOI=10.1016/s0167-4781(00)00030-0;
RA Sol-Church K., Frenck J., Mason R.W.;
RT "Mouse cathepsin M, a placenta-specific lysosomal cysteine protease related
RT to cathepsins L and P.";
RL Biochim. Biophys. Acta 1491:289-294(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/Sv, and C57BL/6J; TISSUE=Placenta, and Spleen;
RX PubMed=11829493; DOI=10.1006/geno.2002.6696;
RA Deussing J., Kouadio M., Rehman S., Werber I., Schwinde A., Peters C.;
RT "Identification and characterization of a dense cluster of placenta-
RT specific cysteine peptidase genes and related genes on mouse chromosome
RT 13.";
RL Genomics 79:225-240(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
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).
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Placenta. {ECO:0000269|PubMed:10760593}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult but not in embryo.
CC {ECO:0000269|PubMed:10760593}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10089}.
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DR EMBL; AF202528; AAF68224.1; -; mRNA.
DR EMBL; AY014777; AAK00506.1; -; mRNA.
DR EMBL; AY057446; AAL15416.1; -; Genomic_DNA.
DR EMBL; AK005550; BAB24116.1; -; mRNA.
DR EMBL; AK005428; BAB24022.1; -; mRNA.
DR CCDS; CCDS36694.1; -.
DR RefSeq; NP_071721.2; NM_022326.3.
DR RefSeq; XP_006517372.1; XM_006517309.3.
DR RefSeq; XP_011242849.1; XM_011244547.2.
DR AlphaFoldDB; Q9JL96; -.
DR SMR; Q9JL96; -.
DR STRING; 10090.ENSMUSP00000097050; -.
DR MEROPS; C01.023; -.
DR GlyGen; Q9JL96; 3 sites.
DR PaxDb; Q9JL96; -.
DR PRIDE; Q9JL96; -.
DR DNASU; 64139; -.
DR GeneID; 64139; -.
DR KEGG; mmu:64139; -.
DR UCSC; uc007qwj.1; mouse.
DR CTD; 64139; -.
DR MGI; MGI:1927229; Ctsm.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; Q9JL96; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9JL96; -.
DR TreeFam; TF313739; -.
DR BioGRID-ORCS; 64139; 1 hit in 70 CRISPR screens.
DR PRO; PR:Q9JL96; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JL96; protein.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISS:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0097655; F:serpin family protein binding; ISO:MGI.
DR GO; GO:0030574; P:collagen catabolic process; ISO:MGI.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; ISO:MGI.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; ISO:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0016540; P:protein autoprocessing; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISO:MGI.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR GO; GO:0031638; P:zymogen activation; ISO:MGI.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 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..15
FT /evidence="ECO:0000255"
FT PROPEP 16..113
FT /note="Activation peptide"
FT /id="PRO_0000026281"
FT CHAIN 114..333
FT /note="Cathepsin M"
FT /id="PRO_0000026282"
FT ACT_SITE 138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 135..178
FT /evidence="ECO:0000250"
FT DISULFID 169..211
FT /evidence="ECO:0000250"
FT DISULFID 269..322
FT /evidence="ECO:0000250"
FT VARIANT 272
FT /note="C -> S"
FT /evidence="ECO:0000269|PubMed:10760593"
FT CONFLICT 54
FT /note="D -> E (in Ref. 2; AAL15416)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="Q -> R (in Ref. 2; AAL15416)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="Q -> P (in Ref. 2; AAL15416)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="D -> E (in Ref. 2; AAL15416)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="T -> A (in Ref. 2; AAL15416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 37409 MW; BB97F8CF8C2AF03A CRC64;
MTSAIFLAML CLGMALPSPA PDPILDVEWQ KWKIKYGKAY SLEEEGQKRA VWEDNMKKIK
LHNGENGLGK HGFTMEMNAF GDMTLEEFRK VMIEIPVPTV KKGKSVQKRL SVNLPKFINW
KKRGYVTPVQ TQGRCNSCWA FSVTGAIEGQ MFRKTGQLIP LSVQNLVDCS RPQGNWGCYL
GNTYLALHYV MENGGLESEA TYPYEEKDGS CRYSPENSTA NITGFEFVPK NEDALMNAVA
SIGPISVAID ARHASFLFYK RGIYYEPNCS SCVVTHSMLL VGYGFTGRES DGRKYWLVKN
SMGTQWGNKG YMKISRDKGN HCGIATYALY PRV
