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Pro-cathepsin H (Cathepsin B3) (Cathepsin BA) [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain]

 CATH_MOUSE              Reviewed;         333 AA.
P49935; Q3UCD6;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 136.
RecName: Full=Pro-cathepsin H;
AltName: Full=Cathepsin B3;
AltName: Full=Cathepsin BA;
Contains:
RecName: Full=Cathepsin H mini chain;
Contains:
RecName: Full=Cathepsin H;
EC=3.4.22.16;
Contains:
RecName: Full=Cathepsin H heavy chain;
Contains:
RecName: Full=Cathepsin H light chain;
Flags: Precursor;
Name=Ctsh;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7722423;
Lafuse W.P., Brown D., Castle L., Zwilling B.S.;
"IFN-gamma increases cathepsin H mRNA levels in mouse macrophages.";
J. Leukoc. Biol. 57:663-669(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 136-301, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Cartilage;
PubMed=10395917;
Soederstroem M., Salminen H., Glumoff V., Kirschke H., Aro H.,
Vuorio E.;
"Cathepsin expression during skeletal development.";
Biochim. Biophys. Acta 1446:35-46(1999).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
DISRUPTION PHENOTYPE.
PubMed=23830514; DOI=10.1016/j.ajhg.2013.06.002;
Aldahmesh M.A., Khan A.O., Alkuraya H., Adly N., Anazi S.,
Al-Saleh A.A., Mohamed J.Y., Hijazi H., Prabakaran S., Tacke M.,
Al-Khrashi A., Hashem M., Reinheckel T., Assiri A., Alkuraya F.S.;
"Mutations in LRPAP1 are associated with severe myopia in humans.";
Am. J. Hum. Genet. 93:313-320(2013).
-!- FUNCTION: Important for the overall degradation of proteins in
lysosomes.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins, acting as an
aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an
endopeptidase.
-!- SUBUNIT: Composed of a mini chain and a large chain. The large
chain may be split into heavy and light chain. All chains are held
together by disulfide bonds.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- TISSUE SPECIFICITY: Widely expressed with highest expression found
in non-skeletal tissues. Low levels found in skeletal tissue.
{ECO:0000269|PubMed:10395917}.
-!- DISRUPTION PHENOTYPE: Mice exhibit markedly abnormal posterior
chamber of eyeball with a configuration suggestive of increased
axial lengthening, compared to the rounded appearance in wild-type
littermates. {ECO:0000269|PubMed:23830514}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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EMBL; U06119; AAA82966.1; -; mRNA.
EMBL; AK149949; BAE29188.1; -; mRNA.
EMBL; AK150583; BAE29677.1; -; mRNA.
EMBL; AK157376; BAE34071.1; -; mRNA.
EMBL; AK160026; BAE35569.1; -; mRNA.
EMBL; CH466560; EDL20901.1; -; Genomic_DNA.
EMBL; Y18464; CAA77182.1; -; mRNA.
CCDS; CCDS23399.1; -.
RefSeq; NP_001299578.1; NM_001312649.1.
RefSeq; NP_031827.2; NM_007801.3.
UniGene; Mm.2277; -.
ProteinModelPortal; P49935; -.
SMR; P49935; -.
IntAct; P49935; 2.
MINT; MINT-4089943; -.
STRING; 10090.ENSMUSP00000034915; -.
ChEMBL; CHEMBL1949491; -.
MEROPS; I29.003; -.
iPTMnet; P49935; -.
PhosphoSitePlus; P49935; -.
MaxQB; P49935; -.
PaxDb; P49935; -.
PeptideAtlas; P49935; -.
PRIDE; P49935; -.
Ensembl; ENSMUST00000034915; ENSMUSP00000034915; ENSMUSG00000032359.
GeneID; 13036; -.
KEGG; mmu:13036; -.
UCSC; uc009qzv.2; mouse.
CTD; 1512; -.
MGI; MGI:107285; Ctsh.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140823; -.
HOGENOM; HOG000230774; -.
HOVERGEN; HBG011513; -.
InParanoid; P49935; -.
KO; K01366; -.
OMA; IMGEDTY; -.
OrthoDB; EOG091G0AKT; -.
TreeFam; TF328985; -.
Reactome; R-MMU-5683826; Surfactant metabolism.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:P49935; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032359; -.
CleanEx; MM_CTSH; -.
ExpressionAtlas; P49935; baseline and differential.
Genevisible; P49935; MM.
GO; GO:0097208; C:alveolar lamellar body; ISS:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IGI:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IMP:UniProtKB.
GO; GO:0030108; F:HLA-A specific activating MHC class I receptor activity; ISS:UniProtKB.
GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; IGI:MGI.
GO; GO:0008233; F:peptidase activity; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0070324; F:thyroid hormone binding; ISS:UniProtKB.
GO; GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
GO; GO:0060448; P:dichotomous subdivision of terminal units involved in lung branching; IMP:UniProtKB.
GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0002764; P:immune response-regulating signaling pathway; ISS:UniProtKB.
GO; GO:0033619; P:membrane protein proteolysis; IMP:UniProtKB.
GO; GO:0001656; P:metanephros development; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0010813; P:neuropeptide catabolic process; ISS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:0010952; P:positive regulation of peptidase activity; IGI:UniProtKB.
GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
GO; GO:0032526; P:response to retinoic acid; IDA:UniProtKB.
GO; GO:0043129; P:surfactant homeostasis; ISS:UniProtKB.
GO; GO:0001913; P:T cell mediated cytotoxicity; IGI:UniProtKB.
GO; GO:0031638; P:zymogen activation; IMP:UniProtKB.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
Protease; Reference proteome; Signal; Thiol protease; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 95 Activation peptide.
/FTId=PRO_0000026212.
CHAIN 96 103 Cathepsin H mini chain. {ECO:0000250}.
/FTId=PRO_0000026213.
PROPEP 104 113 {ECO:0000255}.
/FTId=PRO_0000026214.
CHAIN 114 333 Cathepsin H. {ECO:0000250}.
/FTId=PRO_0000026215.
CHAIN 114 290 Cathepsin H heavy chain. {ECO:0000250}.
/FTId=PRO_0000026216.
CHAIN 291 333 Cathepsin H light chain. {ECO:0000250}.
/FTId=PRO_0000026217.
ACT_SITE 139 139 {ECO:0000250}.
ACT_SITE 279 279 {ECO:0000250}.
ACT_SITE 299 299 {ECO:0000250}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 228 228 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 100 325 {ECO:0000250}.
DISULFID 136 179 {ECO:0000250}.
DISULFID 170 212 {ECO:0000250}.
DISULFID 270 320 {ECO:0000250}.
CONFLICT 137 137 G -> A (in Ref. 1; AAA82966).
{ECO:0000305}.
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


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