RAT:CATH

Species (Taxon ID)	Rattus norvegicus (Rat). (10116)
Gene Name(s)	Ctsh
Protein Name(s)	Pro-cathepsin H Cathepsin H mini chain Cathepsin H Cathepsin H heavy chain Cathepsin H light chain
External Links
UniProt	P00786
EMBL	Y00708 BC085352 M38135
PIR	S00211
RefSeq	NP_037071.1 XP_008764662.1
UniGene	Rn.1997
ProteinModelPortal	P00786
SMR	P00786
STRING	10116.ENSRNOP00000019285
BindingDB	P00786
MEROPS	C01.040
PaxDb	P00786
PRIDE	P00786
Ensembl	ENSRNOT00000019285
GeneID	25425
KEGG	rno:25425
UCSC	RGD:2447
CTD	1512
RGD	2447
eggNOG	COG4870
GeneTree	ENSGT00760000118871
HOGENOM	HOG000230774
HOVERGEN	HBG011513
InParanoid	P00786
KO	K01366
OMA	HKYLWSE
OrthoDB	EOG70KGPX
PhylomeDB	P00786
TreeFam	TF328985
NextBio	606599
PRO	PR:P00786
Proteomes	UP000002494
Genevestigator	P00786
GO	GO:0001669 GO:0097208 GO:0005930 GO:0005829 GO:0005615 GO:0070062 GO:0005764 GO:0001520 GO:0004177 GO:0008656 GO:0004197 GO:0030108 GO:0030984 GO:0032403 GO:0043621 GO:0004252 GO:0070324 GO:0006919 GO:0010815 GO:0097067 GO:0060448 GO:0070371 GO:0002764 GO:0033619 GO:0001656 GO:0043066 GO:0010813 GO:0045766 GO:2001235 GO:0030335 GO:0008284 GO:0010634 GO:0010628 GO:0010952 GO:0031648 GO:0006508 GO:0032526 GO:0007283 GO:0043129 GO:0001913 GO:0031638
InterPro	IPR025661 IPR000169 IPR025660 IPR013128 IPR000668 IPR013201
PANTHER	PTHR12411
Pfam	PF08246 PF00112
PRINTS	PR00705
SMART	SM00848 SM00645
PROSITE	PS00640 PS00139 PS00639

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0097208	alveolar lamellar body	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	C		Seeded From UniProt	complete
involved_in	GO:0097067	cellular response to thyroid hormone stimulus	PMID:21217776^[1]	ECO:0000270	expression pattern evidence used in manual assertion		P	occurs_in:(CL:0000002)	Seeded From UniProt	complete
involved_in	GO:0070371	ERK1 and ERK2 cascade	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
enables	GO:0070324	thyroid hormone binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	F		Seeded From UniProt	complete
involved_in	GO:0060448	dichotomous subdivision of terminal units involved in lung branching	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	P		Seeded From UniProt	complete
involved_in	GO:0045766	positive regulation of angiogenesis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	P		Seeded From UniProt	complete
involved_in	GO:0043129	surfactant homeostasis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	P		Seeded From UniProt	complete
involved_in	GO:0033619	membrane protein proteolysis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
involved_in	GO:0032526	response to retinoic acid	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	P		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	P		Seeded From UniProt	complete
involved_in	GO:0031638	zymogen activation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
involved_in	GO:0030335	positive regulation of cell migration	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
enables	GO:0030108	HLA-A specific activating MHC class I receptor activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	F		Seeded From UniProt	complete
involved_in	GO:0010952	positive regulation of peptidase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
involved_in	GO:0010952	positive regulation of peptidase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	P		Seeded From UniProt	complete
involved_in	GO:0010815	bradykinin catabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
involved_in	GO:0010813	neuropeptide catabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
involved_in	GO:0010634	positive regulation of epithelial cell migration	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
enables	GO:0008656	cysteine-type endopeptidase activator activity involved in apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	F		Seeded From UniProt	complete
enables	GO:0008656	cysteine-type endopeptidase activator activity involved in apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	F		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	C		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	F		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	F		Seeded From UniProt	complete
involved_in	GO:0002764	immune response-regulating signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09668	P		Seeded From UniProt	complete
involved_in	GO:0001913	T cell mediated cytotoxicity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P49935	P		Seeded From UniProt	complete
involved_in	GO:0001656	metanephros development	PMID:16153003^[2]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990834	response to odorant	PMID:23103411^[3]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0097208	alveolar lamellar body	PMID:2005374^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097208	alveolar lamellar body	PMID:12034564^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:2470410^[6]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2447 RGD:621509 RGD:628643	F		Seeded From UniProt	complete
enables	GO:0043621	protein self-association	PMID:7550115^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030984	kininogen binding	PMID:3356189^[8]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2980	F		Seeded From UniProt	complete
involved_in	GO:0007283	spermatogenesis	PMID:9238520^[9]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:11788364^[10]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005930	axoneme	PMID:12838426^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:2005374^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:2005374^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004177	aminopeptidase activity	PMID:1483460^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0001669	acrosomal vesicle	PMID:12838426^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0001520	outer dense fiber	PMID:12838426^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051603	proteolysis involved in cellular protein catabolic process	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:107341 PANTHER:PTN000274640 UniProtKB:P07711 UniProtKB:P07858 UniProtKB:P25774 UniProtKB:P43235	P		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0013770 MGI:MGI:107341 MGI:MGI:1860262 MGI:MGI:88561 MGI:MGI:88564 PANTHER:PTN000274640 RGD:2445 RGD:2447 RGD:2448 RGD:61810 RGD:621509 UniProtKB:P07711 UniProtKB:P07858 UniProtKB:P09668 UniProtKB:P25774 UniProtKB:Q9UBR2 WB:WBGene00000786 dictyBase:DDB_G0279187	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0034229 FB:FBgn0034709 MGI:MGI:88564 PANTHER:PTN000274640 RGD:2447 RGD:61810 RGD:621509 RGD:708479 UniProtKB:P07711 UniProtKB:P07858 UniProtKB:P09668 UniProtKB:P25774 UniProtKB:P43235 UniProtKB:Q9UBR2	C		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:21873635^[13]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0013770 FB:FBgn0030521 MGI:MGI:107285 MGI:MGI:107341 PANTHER:PTN000274640 RGD:2448 RGD:621509 TAIR:locus:2133402 TAIR:locus:2157712 TAIR:locus:2204873 TAIR:locus:505006093 UniProtKB:P07711 UniProtKB:P07858 UniProtKB:P09668 UniProtKB:P25774 UniProtKB:P43235 UniProtKB:Q8IIL0	F		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008656	P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008656	P		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000668	P		Seeded From UniProt	complete
enables	GO:0008234	cysteine-type peptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000668 InterPro:IPR013128	F		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0458 UniProtKB-SubCell:SL-0158	C		Seeded From UniProt	complete
enables	GO:0008234	cysteine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0788	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Wu, SM et al. (2011) Cathepsin H regulated by the thyroid hormone receptors associate with tumor invasion in human hepatoma cells. Oncogene 30 2057-69 PubMed GONUTS page
↑ Vattimo, Mde F & Santos, OF (2005) Functional interface between cathepsins and growth factors in the kidney development. Ren Fail 27 615-22 PubMed GONUTS page
↑ Irwin, LN & Byers, DM (2012) Novel odors affect gene expression for cytokines and proteinases in the rat amygdala and hippocampus. Brain Res. 1489 1-7 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Ishii, Y et al. (1991) Cysteine proteinases in bronchoalveolar epithelial cells and lavage fluid of rat lung. J. Histochem. Cytochem. 39 461-8 PubMed GONUTS page
↑ Brasch, F et al. (2002) Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes. Am. J. Respir. Cell Mol. Biol. 26 659-70 PubMed GONUTS page
↑ Dahlmann, B et al. (1989) ATP-activated, high-molecular-mass proteinase-I from rat skeletal muscle is a cysteine proteinase-alpha 1-macroglobulin complex. Biochim. Biophys. Acta 991 253-62 PubMed GONUTS page
↑ Nishimura, Y et al. (1995) Biochemical properties and intracellular processing of lysosomal cathepsins B and H. Biol. Pharm. Bull. 18 829-36 PubMed GONUTS page
↑ Moreau, T et al. (1988) Cysteine-proteinase-inhibiting function of T kininogen and of its proteolytic fragments. Eur. J. Biochem. 173 185-90 PubMed GONUTS page
↑ Mathur, PP et al. (1997) Differential expression of multiple cathepsin mRNAs in the rat testis during maturation and following lonidamine induced tissue restructuring. Biochem. Mol. Biol. Int. 42 217-33 PubMed GONUTS page
↑ Farges, MC et al. (2002) Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis. Am. J. Physiol. Endocrinol. Metab. 282 E326-35 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Haraguchi, CM et al. (2003) Expression of cathepsin H in differentiating rat spermatids: immunoelectron microscopic study. Histochem. Cell Biol. 120 63-71 PubMed GONUTS page
↑ Rothe, M & Dodt, J (1992) Studies on the aminopeptidase activity of rat cathepsin H. Eur. J. Biochem. 210 759-64 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:21217776-1] Wu, SM et al. (2011) Cathepsin H regulated by the thyroid hormone receptors associate with tumor invasion in human hepatoma cells. Oncogene 30 2057-69 PubMed GONUTS page

[PMID:16153003-2] Vattimo, Mde F & Santos, OF (2005) Functional interface between cathepsins and growth factors in the kidney development. Ren Fail 27 615-22 PubMed GONUTS page

[PMID:23103411-3] Irwin, LN & Byers, DM (2012) Novel odors affect gene expression for cytokines and proteinases in the rat amygdala and hippocampus. Brain Res. 1489 1-7 PubMed GONUTS page

[PMID:2005374-4] 4.0 ^4.1 ^4.2 Ishii, Y et al. (1991) Cysteine proteinases in bronchoalveolar epithelial cells and lavage fluid of rat lung. J. Histochem. Cytochem. 39 461-8 PubMed GONUTS page

[PMID:12034564-5] Brasch, F et al. (2002) Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes. Am. J. Respir. Cell Mol. Biol. 26 659-70 PubMed GONUTS page

[PMID:2470410-6] Dahlmann, B et al. (1989) ATP-activated, high-molecular-mass proteinase-I from rat skeletal muscle is a cysteine proteinase-alpha 1-macroglobulin complex. Biochim. Biophys. Acta 991 253-62 PubMed GONUTS page

[PMID:7550115-7] Nishimura, Y et al. (1995) Biochemical properties and intracellular processing of lysosomal cathepsins B and H. Biol. Pharm. Bull. 18 829-36 PubMed GONUTS page

[PMID:3356189-8] Moreau, T et al. (1988) Cysteine-proteinase-inhibiting function of T kininogen and of its proteolytic fragments. Eur. J. Biochem. 173 185-90 PubMed GONUTS page

[PMID:9238520-9] Mathur, PP et al. (1997) Differential expression of multiple cathepsin mRNAs in the rat testis during maturation and following lonidamine induced tissue restructuring. Biochem. Mol. Biol. Int. 42 217-33 PubMed GONUTS page

[PMID:11788364-10] Farges, MC et al. (2002) Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis. Am. J. Physiol. Endocrinol. Metab. 282 E326-35 PubMed GONUTS page

[PMID:12838426-11] 11.0 ^11.1 ^11.2 Haraguchi, CM et al. (2003) Expression of cathepsin H in differentiating rat spermatids: immunoelectron microscopic study. Histochem. Cell Biol. 120 63-71 PubMed GONUTS page

[PMID:1483460-12] Rothe, M & Dodt, J (1992) Studies on the aminopeptidase activity of rat cathepsin H. Eur. J. Biochem. 210 759-64 PubMed GONUTS page

[PMID:21873635-13] 13.0 ^13.1 ^13.2 ^13.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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RAT:CATH

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