Katepsin D

CTSD
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1LYA, 1LYB, 1LYW, 4OBZ, 4OC6, 4OD9
Identifikatori
Aliasi	CTSD, CLN10, CPSD, HEL-S-130P, katepsin D
Vanjski ID-jevi	OMIM: 116840 MGI: 88562 HomoloGene: 55616 GeneCards: CTSD
Lokacija gena (čovjek)
Hrom.	Hromosom 11 (čovjek)
Kraj	1,764,573 bp
Lokacija gena (miš)
Hrom.	Hromosom 7 (miš)
Kraj	141,941,775 bp
Obrazac RNK ekspresije
	; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• GO:0070122 peptidase activity; • hydrolase activity; • GO:0001948, GO:0016582 vezivanje za proteine; • serine-type endopeptidase activity; • cysteine-type endopeptidase activity; • aspartic-type endopeptidase activity; • aspartic-type peptidase activity;
Ćelijska komponenta	• lysosomal lumen; • Egzosom; • Lipidni splav; • GO:0005578 Vanćelijski matriks; • Lizozom; • Melanosom; • Vanćelijsko; • specific granule lumen; • tertiary granule lumen; • ficolin-1-rich granule lumen; • extracellular region; • collagen-containing extracellular matrix; • lysosomal membrane; • endosome membrane;
Biološki proces	• GO:0044257 protein catabolic process; • Autofagija; • collagen catabolic process; • antigen processing and presentation of exogenous peptide antigen via MHC class II; • Proteoliza; • neutrophil degranulation; • lipoprotein catabolic process; • positive regulation of apoptotic process; • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; • regulation of establishment of protein localization;
	Izvori:Amigo / QuickGO
Ortolozi
	1509
	13033
	ENSG00000117984
	ENSMUSG00000007891
	P07339
	P18242
	NM_001909
	NM_009983
	NP_001900
	NP_034113
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Katepsin D je protein koji je kod čovjeka kodiran sa gena CTSD.^[5]^[6]^[7]^[8]^[9]^[10]

Ovaj gen kodira lizosomne aspartil proteaze koje se sastoji se od proteinskog dimera disulfidnih veza teškog i lahkog lanca, oba proizvedena iz jednog prekursorskog proteina. Ova proteinaza je član familije peptidaza A1, a ima specifičnost sličanu, ali užu nego pepsin A. Transkripcija ovog gena se pokrće sa nekoliko lokusa, uključujući i onaj koji je početak lokusa za regulaciju transporta estrogena. Mutacije u ovom genu su uključene u patogenezi nekoliko bolesti, uključujući rak dojke, a možda i Alzheimerovu bolest

Katepsin D se uzima kao marker tumora raka dojke.^[11]

Katepsin-D je aspartatna proteaza koja kritično ovisi o protonizaciji njenog aktivnog mjesta asparaginskog ostatka, aktiviranog na at pH 5 u endosomima hepatocita, gdje degradira insulin. Tokom Asp-protonizacije, niža pH vrijednost void ka uključivanju konformacije kathepsina-D : ako pH opada, segment N-kraja proteaze se skida sa aktivnog mjesta.^[12] ^[13] ^[14] Katepsin D aktiviraju keramidne veze.^[15]

Također pogledajte

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000117984 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000007891 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Faust PL, Kornfeld S, Chirgwin JM (Sep 1985). "Cloning and sequence analysis of cDNA for human cathepsin D". Proc Natl Acad Sci U S A. 82 (15): 4910–4. doi:10.1073/pnas.82.15.4910. PMC 390467. PMID 3927292.CS1 održavanje: više imena: authors list (link)
^ Cornish-Bowden A. (2004): Fundamentals of enzyme kinetics, 3rd Ed. Portland Press. ISBN 9781855781580; ISBN 1855781581.
^ Međedović S., Maslić E., Hadžiselimović R. (2000): Biologija 2. Svjetlost, Sarajevo, ISBN 9958-10-222-6.
^ Bajrović K, Jevrić-Čaušević A., Hadžiselimović R., Ed. (2005): Uvod u genetičko inženjerstvo i biotehnologiju. Institut za genetičko inženjerstvo i biotehnologiju (INGEB), Sarajevo, ISBN 9958-9344-1-8.
^ Graeme K. Hunter G. K. (2000): Vital Forces. The discovery of the molecular basis of life. Academic Press, London, ISBN 0-12-361811-8.
^ Nelson D. L., Michael M. Cox M. M. (2013): Lehninger Principles of Biochemistry. W. H. Freeman, 2013.ISBN 978-1-4641-0962-1.
^ Wolf M, Clark-Lewis I, Buri C, Langen H, Lis M, Mazzucchelli L (april 2003). "Cathepsin D specifically cleaves the chemokines macrophage inflammatory protein-1 alpha, macrophage inflammatory protein-1 beta, and SLC that are expressed in human breast cancer". Am. J. Pathol. 162 (4): 1183–90. doi:10.1016/S0002-9440(10)63914-4. PMC 1851240. PMID 12651610.CS1 održavanje: više imena: authors list (link)^{[mrtav link]}
^ Authier F, Métioui M, Fabrega S, Kouach M, Briand G (2002). "Endosomal proteolysis of internalized insulin at the C-terminal region of the B chain by cathepsin D". J. Biol. Chem. 277 (11): 9437–9446. doi:10.1074/jbc.M110188200. PMID 11779865.CS1 održavanje: više imena: authors list (link)
^ Lee Angela, Gulnik Sergei, Erickson John (1998). "Conformational switching in an aspartic proteinase". Nature Structural & Molecular Biology. 5 (10): 866–871. doi:10.1038/2306.CS1 održavanje: više imena: authors list (link)
^ Petsko Gregory, Ringe Dagmar (2004). Protein Structure and Function. ISBN 978-1-4051-1922-1.
^ Heinrich M1, Wickel M, Schneider-Brachert W, Sandberg C, Gahr J, Schwandner R, Weber T, Saftig P, Peters C, Brunner J, Krönke M, Schütze S (1999). "Cathepsin D targeted by acid sphingomyelinase-derived ceramide". The EMBO Journal. 18 (19): 5252–5263. doi:10.1093/emboj/18.19.5252. PMC 1171596. PMID 10508159.CS1 održavanje: više imena: authors list (link)

Vanjski linkovi

http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1509
MEROPS online database for peptidases and their inhibitors: A01.009 Arhivirano 2. 4. 2008. na Wayback Machine
GeneReviews/NIH/NCBI/UW entry on Neuronal Ceroid-Lipofuscinoses

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000117984 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000007891 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid3927292-5] Faust PL, Kornfeld S, Chirgwin JM (Sep 1985). "Cloning and sequence analysis of cDNA for human cathepsin D". Proc Natl Acad Sci U S A. 82 (15): 4910–4. doi:10.1073/pnas.82.15.4910. PMC 390467. PMID 3927292.CS1 održavanje: više imena: authors list (link)

[6] Cornish-Bowden A. (2004): Fundamentals of enzyme kinetics, 3rd Ed. Portland Press. ISBN 9781855781580; ISBN 1855781581.

[7] Međedović S., Maslić E., Hadžiselimović R. (2000): Biologija 2. Svjetlost, Sarajevo, ISBN 9958-10-222-6.

[8] Bajrović K, Jevrić-Čaušević A., Hadžiselimović R., Ed. (2005): Uvod u genetičko inženjerstvo i biotehnologiju. Institut za genetičko inženjerstvo i biotehnologiju (INGEB), Sarajevo, ISBN 9958-9344-1-8.

[9] Graeme K. Hunter G. K. (2000): Vital Forces. The discovery of the molecular basis of life. Academic Press, London, ISBN 0-12-361811-8.

[10] Nelson D. L., Michael M. Cox M. M. (2013): Lehninger Principles of Biochemistry. W. H. Freeman, 2013.ISBN 978-1-4641-0962-1.

[pmid12651610-11] Wolf M, Clark-Lewis I, Buri C, Langen H, Lis M, Mazzucchelli L (april 2003). "Cathepsin D specifically cleaves the chemokines macrophage inflammatory protein-1 alpha, macrophage inflammatory protein-1 beta, and SLC that are expressed in human breast cancer". Am. J. Pathol. 162 (4): 1183–90. doi:10.1016/S0002-9440(10)63914-4. PMC 1851240. PMID 12651610.CS1 održavanje: više imena: authors list (link)^{[mrtav link]}

[authierJBC-12] Authier F, Métioui M, Fabrega S, Kouach M, Briand G (2002). "Endosomal proteolysis of internalized insulin at the C-terminal region of the B chain by cathepsin D". J. Biol. Chem. 277 (11): 9437–9446. doi:10.1074/jbc.M110188200. PMID 11779865.CS1 održavanje: više imena: authors list (link)

[leeNSMB-13] Lee Angela, Gulnik Sergei, Erickson John (1998). "Conformational switching in an aspartic proteinase". Nature Structural & Molecular Biology. 5 (10): 866–871. doi:10.1038/2306.CS1 održavanje: više imena: authors list (link)

[petskoBook-14] Petsko Gregory, Ringe Dagmar (2004). Protein Structure and Function. ISBN 978-1-4051-1922-1.

[pmid10508159-15] Heinrich M1, Wickel M, Schneider-Brachert W, Sandberg C, Gahr J, Schwandner R, Weber T, Saftig P, Peters C, Brunner J, Krönke M, Schütze S (1999). "Cathepsin D targeted by acid sphingomyelinase-derived ceramide". The EMBO Journal. 18 (19): 5252–5263. doi:10.1093/emboj/18.19.5252. PMC 1171596. PMID 10508159.CS1 održavanje: više imena: authors list (link)

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