ID Q922Q7_MOUSE Unreviewed; 333 AA. AC Q922Q7; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 03-AUG-2022, entry version 102. DE SubName: Full=Cathepsin H {ECO:0000313|EMBL:AAH06878.1}; 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 -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}. CC -!- SIMILARITY: Belongs to the peptidase C1 family. CC {ECO:0000256|ARBA:ARBA00008455}. 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 MEROPS; C01.040; -. DR PeptideAtlas; Q922Q7; -. DR MGI; MGI:107285; Ctsh. DR ChiTaRS; Ctsh; mouse. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd02248; Peptidase_C1A; 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; 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; 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}; KW Lysosome {ECO:0000256|ARBA:ARBA00023228}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP}; KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..333 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5018655415" FT DOMAIN 33..88 FT /note="Inhibitor_I29" FT /evidence="ECO:0000259|SMART:SM00848" FT DOMAIN 114..330 FT /note="Pept_C1" FT /evidence="ECO:0000259|SMART:SM00645" 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 //