POP5

POP5
Identifikatori
Aliasi	POP5
Vanjski ID-jevi	OMIM: 609992 MGI: 2151221 HomoloGene: 41076 GeneCards: POP5
Lokacija gena (čovjek)
Hrom.	Hromosom 12 (čovjek)
Kraj	120,581,402 bp
Lokacija gena (miš)
Hrom.	Hromosom 5 (miš)
Kraj	115,383,410 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• ribonuclease activity; • GO:0001948, GO:0016582 vezivanje za proteine; • hydrolase activity; • ribonuclease P activity;
Ćelijska komponenta	• Jedarce; • nucleolar ribonuclease P complex; • jedro; • nukleoplazma; • ribonuclease MRP complex; • multimeric ribonuclease P complex;
Biološki proces	• RNA metabolic process; • RNA phosphodiester bond hydrolysis; • RNA phosphodiester bond hydrolysis, endonucleolytic; • tRNA processing; • protein lipoylation; • tRNA 5'-leader removal; • rRNA processing;
	Izvori:Amigo / QuickGO
Ortolozi
	51367
	117109
	ENSG00000167272
	ENSMUSG00000060152
	Q969H6
	Q9DB28
	NM_015918; NM_198201; NM_198202
	NM_026398
	NP_057002; NP_937845
	NP_080674; NP_001390591
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Podjedinica POP5 ribonukleaze P/proteina MRP je enzim koji je kod ljudi kodiran genom POP5.^[5]^[6]

U nedavnom radu navodi se da hipoplazija hrskavice i dlake (CHH) uzrokovana je mutacijama u genu koji kodira komponentu RNK RNaza MRP. Još nije poznato kako ove mutacije utiču na funkciju ove endoribonukleaze. Istraživan je učinak mutacija u P3 domenu na vezivanje proteina i nabiranje RNK. Dobijeni podaci pokazuju da su brojne supstitucije nukleotida P3 smanjile efikasnost njegove interakcije sa Rpp25 i Rpp20, dvije proteinske podjedinice koje se vezuju kao heterodimer za ovaj domen. Supstitucija 40G > A povezana sa CHH, kao i zamjena ostatka 47, gotovo je potpuno poništila vezivanje Rpp25 i Rpp20 u različitim testovima. Također, druge mutacije P3 povezane sa CHH smanjile su efikasnost kojom je RNaza MRP RNK vezana za Rpp25-Rpp20. Ovi podaci pokazuju da se najvažniji ostaci za vezivanje dimera Rpp25-Rpp20 nalaze u apikalnoj matičnoj petlji domena P3. Strukturne analize pomoću NMR-a nisu samo pokazale da ova petlja može usvojiti strukturu trostruke pseudopetlje, već su pokazale i da supstitucija 40G > A mijenja nabiranje ovog dijela domena P3. Tipodaci su prvi koji pružaju uvid u molekulski mehanizam kojim mutacije povezane s CHH utiču na funkciju RNaze MRP.^[7]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 163 aminokiseline, a molekulska težina 18.820 Da.^[8]

10	20	30	40	50
MVRFKHRYLL	CELVSDDPRC	RLSLDDRVLS	SLVRDTIARV	HGTFGAAACS
IGFAVRYLNA	YTGIVLLRCR	KEFYQLVWSA	LPFITYLENK	GHRYPCFFNT
LHVGGTIRTC	QKFLIQYNRR	QLLILLQNCT	DEGEREAIQK	SVTRSCLLEE
EEESGEEAAE	AME

Simboli

C: Cistein
D: Asparaginska kiselina
E: Glutaminska kiselina
F: Fenilalanin
G: Glicin
H: Histidin
I: Izoleucin
K: Lizin
L: Leucin
M: Metionin
N: Asparagin
P: Prolin
Q: Glutamin
R: Arginin
S: Serin
T: Treonin
V: Valin
W: Triptofan
Y: Tirozin

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000167272 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000060152 - 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.
^ van Eenennaam H, Lugtenberg D, Vogelzangs JH, van Venrooij WJ, Pruijn GJ (Aug 2001). "hPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases". J Biol Chem. 276 (34): 31635–41. doi:10.1074/jbc.M103399200. PMID 11413139.
^ "Entrez Gene: POP5 processing of precursor 5, ribonuclease P/MRP subunit (S. cerevisiae)".
^ Tim J M Welting , Sandy Mattijssen, Florence M A Peters, Nienke L van Doorn, Lianne Dekkers, Walther J van Venrooij, Hans A Heus, Luisa Bonafé, Ger J M Pruijn (2007): Cartilage-hair hypoplasia-associated mutations in the RNase MRP P3 domain affect RNA folding and ribonucleoprotein assembly. Biochim Biophys Acta, 1783(3):455-66.pmid: 18164267, doi: 10.1016/j.bbamcr.
^ "UniProt, Q969H6". Pristupljeno 12. 8. 2021.

Dopunska literatura

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
van Eenennaam H, Pruijn GJ, van Venrooij WJ (1999). "hPop4: a new protein subunit of the human RNase MRP and RNase P ribonucleoprotein complexes". Nucleic Acids Res. 27 (12): 2465–72. doi:10.1093/nar/27.12.2465. PMC 148449. PMID 10352175.
Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Welting TJ, van Venrooij WJ, Pruijn GJ (2004). "Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex". Nucleic Acids Res. 32 (7): 2138–46. doi:10.1093/nar/gkh539. PMC 407822. PMID 15096576.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.

Vanjski linkovi

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000167272 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000060152 - 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.

[pmid11413139-5] van Eenennaam H, Lugtenberg D, Vogelzangs JH, van Venrooij WJ, Pruijn GJ (Aug 2001). "hPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases". J Biol Chem. 276 (34): 31635–41. doi:10.1074/jbc.M103399200. PMID 11413139.

[entrez-6] "Entrez Gene: POP5 processing of precursor 5, ribonuclease P/MRP subunit (S. cerevisiae)".

[7] Tim J M Welting , Sandy Mattijssen, Florence M A Peters, Nienke L van Doorn, Lianne Dekkers, Walther J van Venrooij, Hans A Heus, Luisa Bonafé, Ger J M Pruijn (2007): Cartilage-hair hypoplasia-associated mutations in the RNase MRP P3 domain affect RNA folding and ribonucleoprotein assembly. Biochim Biophys Acta, 1783(3):455-66.pmid: 18164267, doi: 10.1016/j.bbamcr.

[UniProt-8] "UniProt, Q969H6". Pristupljeno 12. 8. 2021.

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