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

 CATH_HUMAN              Reviewed;         335 AA.
P09668; B2RBK0; Q96NY6; Q9BUM7;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 4.
25-OCT-2017, entry version 188.
RecName: Full=Pro-cathepsin H;
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; Synonyms=CPSB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-26 AND TYR-179.
TISSUE=Liver;
PubMed=2587265; DOI=10.1093/nar/17.22.9471;
Fuchs R., Gassen H.G.;
"Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine
proteinase.";
Nucleic Acids Res. 17:9471-9471(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TYR-179.
PubMed=11796715; DOI=10.1074/jbc.M109557200;
Waghray A., Keppler D., Sloane B.F., Schuger L., Chen Y.Q.;
"Analysis of a truncated form of cathepsin H in human prostate tumor
cells.";
J. Biol. Chem. 277:11533-11538(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-26.
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-26.
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 88-335, AND VARIANT TYR-179.
TISSUE=Kidney;
PubMed=2849458;
Fuchs R., Machleidt W., Gassen H.G.;
"Molecular cloning and sequencing of a cDNA coding for mature human
kidney cathepsin H.";
Biol. Chem. Hoppe-Seyler 369:469-475(1988).
[7]
PROTEIN SEQUENCE OF 98-105 AND 114-335, AND GLYCOSYLATION AT ASN-101
AND ASN-230.
TISSUE=Kidney;
PubMed=3342889; DOI=10.1016/0014-5793(88)80028-0;
Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V.;
"Amino acid sequences of the human kidney cathepsins H and L.";
FEBS Lett. 228:341-345(1988).
[8]
PROTEIN SEQUENCE OF 99-105; 116-159 AND 294-335.
Machleidt W., Ritonja A., Popovic T., Kotnik M., Brzin J., Turk V.,
Machleidt I., Mueller-Esterl W.;
"Human cathepsins B, H and L: characterization by amino acid sequences
and some kinetics of inhibition by the kininogens.";
(In) Turk V. (eds.);
Cysteine proteinases and their inhibitors, pp.3-18, Walter de Gruyter,
Berlin and New York (1986).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-230.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
VARIANT [LARGE SCALE ANALYSIS] ARG-126.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CTSHID40206ch15q25.html";
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EMBL; X16832; CAA34734.1; -; mRNA.
EMBL; AF426247; AAL23961.1; -; mRNA.
EMBL; AK314698; BAG37247.1; -; mRNA.
EMBL; AC011944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002479; AAH02479.1; -; mRNA.
EMBL; X07549; CAA30428.1; -; mRNA.
EMBL; X07549; CAA30429.1; -; mRNA.
CCDS; CCDS10308.1; -.
PIR; S12486; KHHUH.
RefSeq; NP_004381.2; NM_004390.4.
UniGene; Hs.148641; -.
PDB; 1BZN; Model; -; B=116-335.
PDBsum; 1BZN; -.
ProteinModelPortal; P09668; -.
SMR; P09668; -.
BioGrid; 107892; 21.
IntAct; P09668; 1.
STRING; 9606.ENSP00000220166; -.
BindingDB; P09668; -.
ChEMBL; CHEMBL2225; -.
DrugBank; DB08526; CARBOBENZYLOXY-(L)-LEUCINYL-(L)LEUCINYL METHOXYMETHYLKETONE.
DrugBank; DB04126; N-[1-Hydroxycarboxyethyl-Carbonyl]Leucylamino-2-Methyl-Butane.
DrugBank; DB02140; N1-(1-Dimethylcarbamoyl-2-Phenyl-Ethyl)-2-Oxo-N4-(2-Pyridin-2-Yl-Ethyl)-Succinamide.
DrugBank; DB03120; Para-Toluene Sulfonate.
GuidetoPHARMACOLOGY; 2349; -.
MEROPS; C01.040; -.
iPTMnet; P09668; -.
PhosphoSitePlus; P09668; -.
BioMuta; CTSH; -.
DMDM; 288558851; -.
EPD; P09668; -.
MaxQB; P09668; -.
PaxDb; P09668; -.
PeptideAtlas; P09668; -.
PRIDE; P09668; -.
DNASU; 1512; -.
Ensembl; ENST00000220166; ENSP00000220166; ENSG00000103811.
GeneID; 1512; -.
KEGG; hsa:1512; -.
UCSC; uc021srk.2; human.
CTD; 1512; -.
DisGeNET; 1512; -.
EuPathDB; HostDB:ENSG00000103811.15; -.
GeneCards; CTSH; -.
H-InvDB; HIX0012481; -.
HGNC; HGNC:2535; CTSH.
HPA; CAB000458; -.
HPA; HPA003524; -.
MalaCards; CTSH; -.
MIM; 116820; gene.
neXtProt; NX_P09668; -.
OpenTargets; ENSG00000103811; -.
Orphanet; 2073; Narcolepsy-cataplexy.
PharmGKB; PA27033; -.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140823; -.
HOGENOM; HOG000230774; -.
HOVERGEN; HBG011513; -.
InParanoid; P09668; -.
KO; K01366; -.
OMA; IMGEDTY; -.
OrthoDB; EOG091G0AKT; -.
PhylomeDB; P09668; -.
TreeFam; TF328985; -.
BRENDA; 3.4.22.16; 2681.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-5683826; Surfactant metabolism.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P09668; -.
ChiTaRS; CTSH; human.
GeneWiki; Cathepsin_H; -.
GenomeRNAi; 1512; -.
PRO; PR:P09668; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000103811; -.
CleanEx; HS_CTSH; -.
ExpressionAtlas; P09668; baseline and differential.
Genevisible; P09668; HS.
GO; GO:0097208; C:alveolar lamellar body; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0097486; C:multivesicular body lumen; TAS:Reactome.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0030108; F:HLA-A specific activating MHC class I receptor activity; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0070324; F:thyroid hormone binding; IDA:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEP:UniProtKB.
GO; GO:0019882; P:antigen processing and presentation; TAS:UniProtKB.
GO; GO:0010815; P:bradykinin catabolic process; IDA:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:UniProtKB.
GO; GO:0060448; P:dichotomous subdivision of terminal units involved in lung branching; ISS:UniProtKB.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0002764; P:immune response-regulating signaling pathway; IDA:UniProtKB.
GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
GO; GO:0001656; P:metanephros development; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0010813; P:neuropeptide catabolic process; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0010952; P:positive regulation of peptidase activity; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
GO; GO:0032526; P:response to retinoic acid; ISS:UniProtKB.
GO; GO:0043129; P:surfactant homeostasis; IDA:UniProtKB.
GO; GO:0001913; P:T cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0031638; P:zymogen activation; IDA: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;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Polymorphism;
Protease; Reference proteome; Signal; Thiol protease; Zymogen.
SIGNAL 1 22
PROPEP 23 97 Activation peptide.
{ECO:0000269|PubMed:3342889}.
/FTId=PRO_0000026206.
PEPTIDE 98 105 Cathepsin H mini chain.
/FTId=PRO_0000026207.
PROPEP 106 115 {ECO:0000269|Ref.8}.
/FTId=PRO_0000026208.
CHAIN 116 335 Cathepsin H.
/FTId=PRO_0000026209.
CHAIN 116 292 Cathepsin H heavy chain.
/FTId=PRO_0000026210.
CHAIN 293 335 Cathepsin H light chain.
/FTId=PRO_0000026211.
ACT_SITE 141 141 {ECO:0000250}.
ACT_SITE 281 281 {ECO:0000250}.
ACT_SITE 301 301 {ECO:0000250}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3342889}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:3342889}.
DISULFID 102 327 {ECO:0000250}.
DISULFID 138 181 {ECO:0000250}.
DISULFID 172 214 {ECO:0000250}.
DISULFID 272 322 {ECO:0000250}.
VARIANT 11 11 G -> R (in dbSNP:rs2289702).
/FTId=VAR_057038.
VARIANT 23 23 A -> T (in dbSNP:rs35001431).
/FTId=VAR_057039.
VARIANT 26 26 C -> S (in dbSNP:rs1036938).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2587265}.
/FTId=VAR_060368.
VARIANT 126 126 G -> R (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036478.
VARIANT 179 179 H -> Y (in dbSNP:rs1130856).
{ECO:0000269|PubMed:11796715,
ECO:0000269|PubMed:2587265,
ECO:0000269|PubMed:2849458}.
/FTId=VAR_067717.
CONFLICT 306 306 Q -> E (in Ref. 7; AA sequence and 8; AA
sequence). {ECO:0000305}.
SEQUENCE 335 AA; 37394 MW; E2CF3A5EEA59C1D1 CRC64;
MWATLPLLCA GAWLLGVPVC GAAELCVNSL EKFHFKSWMS KHRKTYSTEE YHHRLQTFAS
NWRKINAHNN GNHTFKMALN QFSDMSFAEI KHKYLWSEPQ NCSATKSNYL RGTGPYPPSV
DWRKKGNFVS PVKNQGACGS CWTFSTTGAL ESAIAIATGK MLSLAEQQLV DCAQDFNNHG
CQGGLPSQAF EYILYNKGIM GEDTYPYQGK DGYCKFQPGK AIGFVKDVAN ITIYDEEAMV
EAVALYNPVS FAFEVTQDFM MYRTGIYSST SCHKTPDKVN HAVLAVGYGE KNGIPYWIVK
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV


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Genprice Inc, Invoices and accounting
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