Primary Information |
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BoMiProt ID | Bomi8116 |
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Protein Name | Poly [ADP-ribose] polymerase 1/ADP-ribosyltransferase diphtheria toxin-like 1/DNA ADP-ribosyltransferase PARP1/NAD(+) ADP-ribosyltransferase 1/Poly[ADP-ribose] synthase 1/Protein poly-ADP-ribosyltransferase PARP1 |
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Organism | Bos taurus |
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Uniprot ID | P18493 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_777176.1 |
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Aminoacid Length | 1016 |
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Molecular Weight | 113486 |
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FASTA Sequence |
Download |
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Gene Name | PARP1/ADPRT |
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Gene ID | 286764 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | Poly(ADP-ribose) polymerase-1 (PARP-1) is a nuclear enzyme with a crucial role in the maintenance of genomic stability. In addition to the role of PARP-1 in DNA repair, multiple studies have also demonstrated its involvement in several inflammatory diseases, such as septic shock, asthma, atherosclerosis, and stroke, as well as in cancer. |
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Biochemical Properties | Poly(ADP-ribose)polymerase-1 (PARP-1) catalyzes the polymerization of ADP-ribose units from NAD+ modules on target proteins, resulting in the attachment of linear or branched polymers. There are six functional domains (A-F) of PARP-1 molecule is present in context of three classic domains, i.e., DNA binding (DBD), automodification (AD) and catalytic (CD) released by proteolytic enzymes. |
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Significance in milk | PARP1 is activated during mastitis, which may prove to be a useful biomarker of mastitis.PARP1 is involved in several cellular processes including transcription, epigenetics, chromatin re-modelling as well as in the maintenance of genomic stability. |
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PTMs | Acetylation,Phosphorylation and ADP-ribosylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P18493|PARP1_BOVIN Poly [ADP-ribose] polymerase 1 OS=Bos taurus OX=9913 GN=PARP1 PE=2 SV=2
MAESSDKLYRVEYAKSGRASCKKCKESIPKDSIRMAFMVES*41PMFDGKIPHWYHLSCFWKV
GFSIWHPDVEVEGFSELRWDDQQTIKKMAETGGRTDVSGKGQDGVGSKTEKTLIDFGAGY
AKSNRSTCKSCMEKIDKGQVRLSKKVVYPDKPQLGMVDCWYHPKCFVQKREELGFRPEFS*180
ATHLMGFS*188VLTAEDQETLKKQLPAIKGERKRKGDEVDGIDEVTKKKSKKEKDKEIKLEKA
LKAQNDLIWNVKDELKKACSTNDLKELLIFNKQEVPS*277GES*280AILDRVADGMVFGALLPCEE
CSGQLVFKGDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYFKKLKIKKQDRIF
PPESSTPVGAAAPPSAASAPAAVHSGPPDKPLSNMKILTLGKLSQNKDEVKATIEKLGGK
LTGTANKASLCISTKKEVDKLNKKMEEVKEANIRVVSEDFLQDISASTKSLQELLSTHLL
SPWGAEVKVEPVEAVGPKGKSGAAPSKKSKGPVKEEGTNKSEKRMKLTLKGGAAVDPDSG
LEHNAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGTVIGS
NKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKHPKKFYPLEIDYGQDEEAVKKLTVN
PGTKSKLPKPVQNLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQ
ALSQGSSDSHILDLSNRFYTLIPHDFGMKKPPLLNNANSVQAKVEMLDNLLDIEVAYSLL
RGGS*784DDSS*788KDPIDVNYEKLKTDIKVVDKDSEEAEIIRKYVKNTHATTHNAYDLEVVDIFK
IEREGESQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFA
DMVSKSANYCHTSQGDPIGLILLGEAALGNMYELKHARHISKLPKGKHSVKGLGKTTPDP
SASITVDGVEVPLGTGISSGVNDTCLLYNEYIVYDIAQVHLKYLLKLKFNFKTSLW
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | PARP-1 is the most important member, exhibiting poly (ADP-rybosil)ation activity, is a protein postransductional modification essential to cellular processes, such as the regulation of DNA reparation, the maintenance of chromatin function and genomic stability, the regulation of transcription, cell cycle progression, and cell death. |
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Bibliography | 1.García S, Conde C. The Role of Poly(ADP-ribose) Polymerase-1 in Rheumatoid Arthritis. Mediators Inflamm. 2015;2015:837250. doi: 10.1155/2015/837250. Epub 2015 Mar 3. PMID: 26339143; PMCID: PMC4539103. 2.Kiliańska ZM, Zołnierczyk J, Wesierska-Gadek J. Biologiczna aktywność polimerazy poli(ADP-rybozy)-1 [Biological activity of poly(ADP-ribose)polymerase-1]. Postepy Hig Med Dosw (Online). 2010 Jul 30;64:344-63. Polish. PMID: 20679690. 3. J. C. Ame, C. Spenlehauer, and G. de Murcia, “The PARP ´
superfamily,” BioEssays, vol. 26, no. 8, pp. 882–893, 2004. 4.V. Schreiber, F. Dantzer, J. C. Ame, and G. de Murcia, “Poly
(ADP-ribose): novel functions for an old molecule,” Nature
Reviews Molecular Cell Biology, vol. 7, no. 7, pp. 517–528, 2006. 5.B. C. Woodhouse and G. L. Dianov, “Poly ADP-ribose polymerase-1: an international molecule of mystery,” DNA Repair,
vol. 7, no. 7, pp. 1077–1086, 2008. 6.De Matteis G, Reale A, Grandoni F, Meyer-Ficca ML, Scatà MC, Meyer RG, Buttazzoni L, Moioli B. Assessment of Poly(ADP-ribose) Polymerase1 (PARP1) expression and activity in cells purified from blood and milk of dairy cattle. Vet Immunol Immunopathol. 2018 Aug;202:102-108. doi: 10.1016/j.vetimm.2018.06.013. Epub 2018 Jun 30. PMID: 30078582. |