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Database: UniProt
Entry: F7CBC7_MONDO
LinkDB: F7CBC7_MONDO
Original site: F7CBC7_MONDO 
ID   F7CBC7_MONDO            Unreviewed;       530 AA.
AC   F7CBC7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|RuleBase:RU362114};
DE            Short=PARP {ECO:0000256|RuleBase:RU362114};
DE            EC=2.4.2.- {ECO:0000256|RuleBase:RU362114};
GN   Name=PARP3 {ECO:0000313|Ensembl:ENSMODP00000014791.4};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000014791.4, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000014791.4, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000014791.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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DR   RefSeq; XP_007500582.1; XM_007500520.2.
DR   AlphaFoldDB; F7CBC7; -.
DR   STRING; 13616.ENSMODP00000014791; -.
DR   Ensembl; ENSMODT00000015063.4; ENSMODP00000014791.4; ENSMODG00000011807.4.
DR   GeneID; 100031207; -.
DR   KEGG; mdo:100031207; -.
DR   CTD; 10039; -.
DR   eggNOG; KOG1037; Eukaryota.
DR   GeneTree; ENSGT00940000158855; -.
DR   HOGENOM; CLU_004841_2_3_1; -.
DR   InParanoid; F7CBC7; -.
DR   OMA; HHITTDN; -.
DR   OrthoDB; 5481368at2759; -.
DR   TreeFam; TF315407; -.
DR   Proteomes; UP000002280; Chromosome 6.
DR   Bgee; ENSMODG00000011807; Expressed in lung and 17 other cell types or tissues.
DR   GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR   GO; GO:0140294; F:NAD DNA ADP-ribosyltransferase activity; IEA:Ensembl.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0140806; F:NAD+- protein-aspartate ADP-ribosyltransferase activity; IEA:Ensembl.
DR   GO; GO:0140804; F:NAD+- protein-lysine ADP-ribosyltransferase activity; IEA:Ensembl.
DR   GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0140807; F:NAD+-protein-glutamate ADP-ribosyltransferase activity; IEA:Ensembl.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030592; P:DNA ADP-ribosylation; IEA:Ensembl.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   GO; GO:0045829; P:negative regulation of isotype switching; IEA:Ensembl.
DR   GO; GO:0051106; P:positive regulation of DNA ligation; IEA:Ensembl.
DR   GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0070213; P:protein auto-ADP-ribosylation; IEA:Ensembl.
DR   GO; GO:1990166; P:protein localization to site of double-strand break; IEA:Ensembl.
DR   GO; GO:0060236; P:regulation of mitotic spindle organization; IEA:Ensembl.
DR   GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR   CDD; cd01437; parp_like; 1.
DR   CDD; cd08002; WGR_PARP3_like; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR   Gene3D; 2.20.140.10; WGR domain; 1.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR   InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR   InterPro; IPR036930; WGR_dom_sf.
DR   InterPro; IPR008893; WGR_domain.
DR   PANTHER; PTHR10459; DNA LIGASE; 1.
DR   PANTHER; PTHR10459:SF66; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP3; 1.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF02877; PARP_reg; 1.
DR   Pfam; PF05406; WGR; 1.
DR   SMART; SM00773; WGR; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR   SUPFAM; SSF142921; WGR domain-like; 1.
DR   PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS51977; WGR; 1.
PE   3: Inferred from homology;
KW   ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU362114};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU362114};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT   DOMAIN          58..148
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          183..300
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   DOMAIN          315..530
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  59592 MW;  E74C1094B650A8D6 CRC64;
     MASKRKAASA STKSPKTKKE KPATEDNFHL AKEALKAAPK EARKAQVDSL CPLSNNPDVQ
     VYEDYDCTLN QTNIGNNNNK FYLIQLLDEG GQYQCWNRWG RVGEVGQSKL KPFSSLDDAK
     KDFEKKFQEK TKNRWADRDN FVAHQGKYTL IEVQADDGQE GQEGTVKVES VDGVQAVEQI
     VKPCTLDPAT QKLVELIFSS DMFKDAMKCM NLDIRKMPLG KLSKKQIAKG FEALEALEDA
     LQKGAQEGQL EELSSRFYTI IPHNFGRAKP PCICSQEILQ TKKDMLLVLA DIELAKSLQA
     AGEDEKKAKV EEVPHPLDRD YQLLKCQLQP LATDTHEYKL IQTYVEKTGW SHLRILHVWK
     VNREGEGDRF QAHAQIGNRR LLWHGTNVAV VAAILKSGLR IMPHSGGRVG KGIYFASENS
     KSASYVGCTS QKIGLMFLSE VVLGQVHHIT GDDPSLREPP SGYHSVIARG RTEPDPSQDV
     ELELEGHKVV VPQGPPVILP SFQESSFWQS EYLIYQESQC RLRYLLQLHF
//
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