ID Q922Q7_MOUSE Unreviewed; 333 AA. AC Q922Q7; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 24-JUL-2024, entry version 107. DE RecName: Full=Pro-cathepsin H {ECO:0000256|ARBA:ARBA00039372}; GN Name=Ctsh {ECO:0000313|EMBL:AAH06878.1, ECO:0000313|MGI:MGI:107285}; 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:AAH06878.1}; RN [1] {ECO:0000313|EMBL:AAH06878.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N {ECO:0000313|EMBL:AAH06878.1}; RC TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old RC virgin mouse. Taken by biopsy. {ECO:0000313|EMBL:AAH06878.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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: Important for the overall degradation of proteins in CC lysosomes. {ECO:0000256|ARBA:ARBA00037522}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably, CC cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16; CC Evidence={ECO:0000256|ARBA:ARBA00036517}; CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}. CC -!- SIMILARITY: Belongs to the peptidase C1 family. CC {ECO:0000256|ARBA:ARBA00008455, ECO:0000256|PROSITE-ProRule:PRU10090}. 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; BC006878; AAH06878.1; -; mRNA. DR AlphaFoldDB; Q922Q7; -. DR MEROPS; C01.040; -. DR PeptideAtlas; Q922Q7; -. DR AGR; MGI:107285; -. DR MGI; MGI:107285; Ctsh. DR ChiTaRS; Ctsh; mouse. DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:TreeGrafter. DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:TreeGrafter. 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; IPR025661; Pept_asp_AS. 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 InterPro; IPR013201; Prot_inhib_I29. DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1. DR PANTHER; PTHR12411:SF642; PRO-CATHEPSIN H; 1. 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; Cysteine proteinases; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1. PE 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU10090}; Lysosome {ECO:0000256|ARBA:ARBA00023228}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE- KW ProRule:PRU10090}; Signal {ECO:0000256|SAM:SignalP}; KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE- KW ProRule:PRU10090}; Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..333 FT /note="Pro-cathepsin H" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5018655415" FT DOMAIN 33..88 FT /note="Cathepsin propeptide inhibitor" FT /evidence="ECO:0000259|SMART:SM00848" FT DOMAIN 114..330 FT /note="Peptidase C1A papain C-terminal" FT /evidence="ECO:0000259|SMART:SM00645" FT ACT_SITE 299 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10090" SQ SEQUENCE 333 AA; 37155 MW; C28B344AC3439DE8 CRC64; MWAALPLLCA GAWLLSTGAT AELTVNAIEK FHFKSWMKQH QKTYSSVEYN HRLQMFANNW RKIQAHNQRN HTFKMALNQF SDMSFAEIKH KFLWSEPQNC SATKSNYLRG TGPYPSSMDW RKKGNVVSPV INQGACGSCW TFSTTGALES AVAIASGKML SLAEQQLVDC AQAFNNHGCK GGLPSQAFEY ILYNKGIMEE DSYPYIGKDS SCRFNPQKAV AFVKNVVNIT LNDEAAMVEA VALYNPVSFA FEVTEDFLMY KSGVYSSKSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS WGSQWGENGY FLIERGKNMC GLAACASYPI PQV //