ID M3YK28_MUSPF Unreviewed; 531 AA.
AC M3YK28;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:ENSMPUP00000011685.1,
GN ECO:0000313|RefSeq:XP_004780143.1, ECO:0000313|RefSeq:XP_012905214.1,
GN ECO:0000313|RefSeq:XP_012905216.1, ECO:0000313|RefSeq:XP_012905217.1,
GN ECO:0000313|RefSeq:XP_012905218.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000011685.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000011685.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004780143.1, ECO:0000313|RefSeq:XP_012905214.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004780143.1,
RC ECO:0000313|RefSeq:XP_012905214.1};
RG RefSeq;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEYP01099218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004780143.1; XM_004780086.3.
DR RefSeq; XP_012905214.1; XM_013049760.2.
DR RefSeq; XP_012905215.1; XM_013049761.1.
DR RefSeq; XP_012905216.1; XM_013049762.2.
DR RefSeq; XP_012905217.1; XM_013049763.2.
DR RefSeq; XP_012905218.1; XM_013049764.2.
DR STRING; 9669.ENSMPUP00000011685; -.
DR Ensembl; ENSMPUT00000011877.1; ENSMPUP00000011685.1; ENSMPUG00000011779.1.
DR GeneID; 101680699; -.
DR KEGG; mpuf:101680699; -.
DR CTD; 10039; -.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000158855; -.
DR HOGENOM; CLU_004841_2_3_1; -.
DR OMA; HHITTDN; -.
DR OrthoDB; 5481368at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0140294; F:NAD DNA ADP-ribosyltransferase activity; IEA:Ensembl.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
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: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; IEA:Ensembl.
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:UP000000715};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 59..149
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 181..299
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 311..531
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 59592 MW; DC9945206FB11AE3 CRC64;
MAPKRKSQVP HEGPDKKQGR QGAEEEDNFR STAEALRAAP TEKHTVRVDP ACPLSHSPRT
QVHEDYACTL NQTNIGSNNN KFYIIQLLEE GDRFACWNRW GRVGEVGQSK LSYFKLLEDA
KKDFEKKFRD KTKNSWAERD HFVAHPGKYT LIEVQGDDEA QEAVVKVDGG PVRSVVQRVR
PCSLDAATQK LITNIFSKDM FKNAMTLMNL DVKKMPLGKL SKQQIARGFE ALEALEAALR
APADGGLSLE ELSSHFYTVI PHNFGRNRPP PINSPELLQA KKDMLLVLAD IELAQTLQAT
PEEEKVEEVP HPLDRDYHLL KCQLELLDPK APEYKVIRTY LEQTGNSYRC PALQHVWKVN
REGEGDRFQA HSKLGNRKLL WHGTNVAVVA AILTSGLRIM PHSGGRVGKG IYFASENSKS
ASYVTGMSCG AHQLGYMFLG EVALGREHHI TVDDPSLKQP PPGFDSVIAR GHTEPDPTQD
TELELDGQRV VVPQGRPVLC AEFSSSRFSQ SEYLIYQDSQ CHLRYLLEVH L
//
