CATH_MOUSE
ID CATH_MOUSE Reviewed; 333 AA.
AC P49935; Q3UCD6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Pro-cathepsin H;
DE AltName: Full=Cathepsin B3;
DE AltName: Full=Cathepsin BA;
DE Contains:
DE RecName: Full=Cathepsin H mini chain;
DE Contains:
DE RecName: Full=Cathepsin H;
DE EC=3.4.22.16;
DE Contains:
DE RecName: Full=Cathepsin H heavy chain;
DE Contains:
DE RecName: Full=Cathepsin H light chain;
DE Flags: Precursor;
GN Name=Ctsh;
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 [MRNA].
RX PubMed=7722423; DOI=10.1002/jlb.57.4.663;
RA Lafuse W.P., Brown D., Castle L., Zwilling B.S.;
RT "IFN-gamma increases cathepsin H mRNA levels in mouse macrophages.";
RL J. Leukoc. Biol. 57:663-669(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 136-301, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Cartilage;
RX PubMed=10395917; DOI=10.1016/s0167-4781(99)00068-8;
RA Soederstroem M., Salminen H., Glumoff V., Kirschke H., Aro H., Vuorio E.;
RT "Cathepsin expression during skeletal development.";
RL Biochim. Biophys. Acta 1446:35-46(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=23830514; DOI=10.1016/j.ajhg.2013.06.002;
RA Aldahmesh M.A., Khan A.O., Alkuraya H., Adly N., Anazi S., Al-Saleh A.A.,
RA Mohamed J.Y., Hijazi H., Prabakaran S., Tacke M., Al-Khrashi A., Hashem M.,
RA Reinheckel T., Assiri A., Alkuraya F.S.;
RT "Mutations in LRPAP1 are associated with severe myopia in humans.";
RL Am. J. Hum. Genet. 93:313-320(2013).
CC -!- FUNCTION: Important for the overall degradation of proteins in
CC lysosomes.
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 -!- SUBUNIT: Composed of a mini chain and a large chain. The large chain
CC may be split into heavy and light chain. All chains are held together
CC by disulfide bonds.
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression found in
CC non-skeletal tissues. Low levels found in skeletal tissue.
CC {ECO:0000269|PubMed:10395917}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit markedly abnormal posterior chamber
CC of eyeball with a configuration suggestive of increased axial
CC lengthening, compared to the rounded appearance in wild-type
CC littermates. {ECO:0000269|PubMed:23830514}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; U06119; AAA82966.1; -; mRNA.
DR EMBL; AK149949; BAE29188.1; -; mRNA.
DR EMBL; AK150583; BAE29677.1; -; mRNA.
DR EMBL; AK157376; BAE34071.1; -; mRNA.
DR EMBL; AK160026; BAE35569.1; -; mRNA.
DR EMBL; CH466560; EDL20901.1; -; Genomic_DNA.
DR EMBL; Y18464; CAA77182.1; -; mRNA.
DR CCDS; CCDS23399.1; -.
DR RefSeq; NP_001299578.1; NM_001312649.1.
DR RefSeq; NP_031827.2; NM_007801.3.
DR AlphaFoldDB; P49935; -.
DR SMR; P49935; -.
DR BioGRID; 198973; 15.
DR STRING; 10090.ENSMUSP00000034915; -.
DR ChEMBL; CHEMBL1949491; -.
DR MEROPS; C01.040; -.
DR MEROPS; I29.003; -.
DR GlyGen; P49935; 3 sites.
DR iPTMnet; P49935; -.
DR PhosphoSitePlus; P49935; -.
DR jPOST; P49935; -.
DR MaxQB; P49935; -.
DR PaxDb; P49935; -.
DR PeptideAtlas; P49935; -.
DR PRIDE; P49935; -.
DR ProteomicsDB; 265541; -.
DR Antibodypedia; 1041; 405 antibodies from 35 providers.
DR DNASU; 13036; -.
DR Ensembl; ENSMUST00000034915; ENSMUSP00000034915; ENSMUSG00000032359.
DR GeneID; 13036; -.
DR KEGG; mmu:13036; -.
DR UCSC; uc009qzv.2; mouse.
DR CTD; 1512; -.
DR MGI; MGI:107285; Ctsh.
DR VEuPathDB; HostDB:ENSMUSG00000032359; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000160227; -.
DR HOGENOM; CLU_012184_1_1_1; -.
DR InParanoid; P49935; -.
DR OMA; AYNNFGC; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; P49935; -.
DR TreeFam; TF328985; -.
DR BRENDA; 3.4.22.16; 3474.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 13036; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ctsh; mouse.
DR PRO; PR:P49935; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P49935; protein.
DR Bgee; ENSMUSG00000032359; Expressed in left lung lobe and 239 other tissues.
DR ExpressionAtlas; P49935; baseline and differential.
DR Genevisible; P49935; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0097208; C:alveolar lamellar body; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0001520; C:outer dense fiber; ISO:MGI.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IGI:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0030108; F:HLA-A specific activating MHC class I receptor activity; ISS:UniProtKB.
DR GO; GO:0030984; F:kininogen binding; ISO:MGI.
DR GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; IGI:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
DR GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0060448; P:dichotomous subdivision of terminal units involved in lung branching; IMP:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0002764; P:immune response-regulating signaling pathway; ISS:UniProtKB.
DR GO; GO:0033619; P:membrane protein proteolysis; IMP:UniProtKB.
DR GO; GO:0001656; P:metanephros development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010813; P:neuropeptide catabolic process; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0010952; P:positive regulation of peptidase activity; IGI:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; IDA:UniProtKB.
DR GO; GO:0043129; P:surfactant homeostasis; ISS:UniProtKB.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IGI:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..95
FT /note="Activation peptide"
FT /id="PRO_0000026212"
FT CHAIN 96..103
FT /note="Cathepsin H mini chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026213"
FT PROPEP 104..113
FT /evidence="ECO:0000255"
FT /id="PRO_0000026214"
FT CHAIN 114..333
FT /note="Cathepsin H"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026215"
FT CHAIN 114..290
FT /note="Cathepsin H heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026216"
FT CHAIN 291..333
FT /note="Cathepsin H light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026217"
FT ACT_SITE 139
FT /evidence="ECO:0000250"
FT ACT_SITE 279
FT /evidence="ECO:0000250"
FT ACT_SITE 299
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..325
FT /evidence="ECO:0000250"
FT DISULFID 136..179
FT /evidence="ECO:0000250"
FT DISULFID 170..212
FT /evidence="ECO:0000250"
FT DISULFID 270..320
FT /evidence="ECO:0000250"
FT CONFLICT 137
FT /note="G -> A (in Ref. 1; AAA82966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 37170 MW; 96688394A87CCA36 CRC64;
MWAALPLLCA GAWLLSTGAT AELTVNAIEK FHFKSWMKQH QKTYSSVEYN HRLQMFANNW
RKIQAHNQRN HTFKMALNQF SDMSFAEIKH KFLWSEPQNC SATKSNYLRG TGPYPSSMDW
RKKGNVVSPV KNQGACGSCW TFSTTGALES AVAIASGKML SLAEQQLVDC AQAFNNHGCK
GGLPSQAFEY ILYNKGIMEE DSYPYIGKDS SCRFNPQKAV AFVKNVVNIT LNDEAAMVEA
VALYNPVSFA FEVTEDFLMY KSGVYSSKSC HKTPDKVNHA VLAVGYGEQN GLLYWIVKNS
WGSQWGENGY FLIERGKNMC GLAACASYPI PQV
