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Poly [ADP-ribose] polymerase 2 (PARP-2) (mPARP-2) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 2) (ARTD2) (NAD( ) ADP-ribosyltransferase 2) (ADPRT-2) (Poly[ADP-ribose] synthase 2) (pADPRT-2)

 PARP2_MOUSE             Reviewed;         559 AA.
O88554; Q99N29;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 3.
12-SEP-2018, entry version 157.
RecName: Full=Poly [ADP-ribose] polymerase 2;
Short=PARP-2;
Short=mPARP-2;
EC=2.4.2.30;
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 2;
Short=ARTD2;
AltName: Full=NAD(+) ADP-ribosyltransferase 2;
Short=ADPRT-2;
AltName: Full=Poly[ADP-ribose] synthase 2;
Short=pADPRT-2;
Name=Parp2; Synonyms=Adprt2, Adprtl2, Aspartl2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Embryo;
PubMed=10364231; DOI=10.1074/jbc.274.25.17860;
Ame J.-C., Rolli V., Schreiber V., Niedergang C., Apiou F., Decker P.,
Muller S., Hoeger T., Menissier-de Murcia J., de Murcia G.M.;
"PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose)
polymerase.";
J. Biol. Chem. 274:17860-17868(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=11133988; DOI=10.1074/jbc.M007870200;
Ame J.-C., Schreiber V., Fraulob V., Dolle P., de Murcia G.M.,
Niedergang C.P.;
"A bidirectional promoter connects the poly(ADP-ribose) polymerase 2
(PARP-2) gene to the gene for RNase P RNA. Structure and expression of
the mouse PARP-2 gene.";
J. Biol. Chem. 276:11092-11099(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-559.
STRAIN=C57BL/6 X 129/Sv;
PubMed=10338144; DOI=10.1016/S0014-5793(99)00448-2;
Berghammer H., Ebner M., Marksteiner R., Auer B.;
"pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene
related to truncated pADPRT homologues in plants and Caenorhabditis
elegans.";
FEBS Lett. 449:259-263(1999).
[5]
INTERACTION WITH PARP1; XRCC1; POLB AND LRIG3, AND
POLY-ADP-RIBOSYLATION.
PubMed=11948190; DOI=10.1074/jbc.M202390200;
Schreiber V., Ame J.-C., Dolle P., Schultz I., Rinaldi B., Fraulob V.,
Menissier-de Murcia J., de Murcia G.M.;
"Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base
excision DNA repair in association with PARP-1 and XRCC1.";
J. Biol. Chem. 277:23028-23036(2002).
[6]
ACETYLATION AT LYS-36 AND LYS-37, ADP-RIBOSYLATION AT LYS-36 AND
LYS-37, AND MUTAGENESIS OF LYS-36 AND LYS-37.
PubMed=18436469; DOI=10.1016/j.biocel.2008.03.008;
Haenni S.S., Hassa P.O., Altmeyer M., Fey M., Imhof R., Hottiger M.O.;
"Identification of lysines 36 and 37 of PARP-2 as targets for
acetylation and auto-ADP-ribosylation.";
Int. J. Biochem. Cell Biol. 40:2274-2283(2008).
-!- FUNCTION: Involved in the base excision repair (BER) pathway, by
catalyzing the poly(ADP-ribosyl)ation of a limited number of
acceptor proteins involved in chromatin architecture and in DNA
metabolism (PubMed:10364231). This modification follows DNA
damages and appears as an obligatory step in a detection/signaling
pathway leading to the reparation of DNA strand breaks
(PubMed:10364231). Mediates serine ADP-ribosylation of target
proteins following interaction with HPF1; HPF1 conferring serine
specificity (By similarity). {ECO:0000250|UniProtKB:Q9UGN5,
ECO:0000269|PubMed:10364231}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000255|PROSITE-ProRule:PRU00397}.
-!- SUBUNIT: Component of a base excision repair (BER) complex,
containing at least XRCC1, PARP1, POLB and LRIG3. Homo- and
heterodimer with PARP1 (PubMed:11948190). Interacts weakly (via
the PARP catalytic domain) with HPF1 (By similarity).
{ECO:0000250|UniProtKB:Q9UGN5, ECO:0000269|PubMed:11948190}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10364231}.
-!- TISSUE SPECIFICITY: Widely expressed; the highest levels were in
testis followed by ovary. Expression is correlated with
proliferation, with higher levels occurring during early fetal
development and organogenesis and in the highly proliferative cell
compartments of adult.
-!- DEVELOPMENTAL STAGE: At stage E12.5, expressed at high level in
the developing liver and kidneys. At E18.5, preferentially
expressed in the thymus and in regions of the nervous system.
Within the developing trunk, preferential expression persisted in
the liver and became restricted to the cortical region of the
kidney, spleen, adrenal gland, and to stomach and intestinal
epithelia. From E14.5 to E18.5, as well as in the adult, expressed
at the highest level in thymus. Expression is particularly high in
the subcapsular zone of the thymus where immature lymphocytes
proliferate.
-!- INDUCTION: By high levels of DNA-damaging agents.
-!- PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000269|PubMed:11948190}.
-!- PTM: Acetylation reduces DNA binding and enzymatic activity.
{ECO:0000269|PubMed:18436469}.
-!- SEQUENCE CAUTION:
Sequence=AAC25415.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ007780; CAA07679.1; -; mRNA.
EMBL; AF191547; AAK13253.1; -; Genomic_DNA.
EMBL; BC062150; AAH62150.1; -; mRNA.
EMBL; AF072521; AAC25415.1; ALT_INIT; mRNA.
CCDS; CCDS27025.1; -.
RefSeq; NP_033762.1; NM_009632.2.
RefSeq; XP_006518505.1; XM_006518442.3.
UniGene; Mm.281482; -.
PDB; 1GS0; X-ray; 2.80 A; A/B=207-557.
PDBsum; 1GS0; -.
ProteinModelPortal; O88554; -.
SMR; O88554; -.
BioGrid; 197999; 3.
IntAct; O88554; 1.
MINT; O88554; -.
STRING; 10090.ENSMUSP00000048877; -.
BindingDB; O88554; -.
ChEMBL; CHEMBL2794; -.
iPTMnet; O88554; -.
PhosphoSitePlus; O88554; -.
EPD; O88554; -.
MaxQB; O88554; -.
PaxDb; O88554; -.
PeptideAtlas; O88554; -.
PRIDE; O88554; -.
Ensembl; ENSMUST00000036126; ENSMUSP00000048877; ENSMUSG00000036023.
GeneID; 11546; -.
KEGG; mmu:11546; -.
UCSC; uc007tlq.1; mouse.
CTD; 10038; -.
MGI; MGI:1341112; Parp2.
eggNOG; KOG1037; Eukaryota.
eggNOG; ENOG410XP18; LUCA.
GeneTree; ENSGT00390000017341; -.
HOGENOM; HOG000173055; -.
HOVERGEN; HBG053514; -.
InParanoid; O88554; -.
KO; K10798; -.
OMA; IPHVFGR; -.
OrthoDB; EOG091G13H1; -.
PhylomeDB; O88554; -.
TreeFam; TF315407; -.
Reactome; R-MMU-110362; POLB-Dependent Long Patch Base Excision Repair.
Reactome; R-MMU-5685939; HDR through MMEJ (alt-NHEJ).
Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-MMU-5696400; Dual Incision in GG-NER.
EvolutionaryTrace; O88554; -.
PMAP-CutDB; O88554; -.
PRO; PR:O88554; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000036023; Expressed in 279 organ(s), highest expression level in embryo.
CleanEx; MM_PARP2; -.
Genevisible; O88554; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:MGI.
GO; GO:1990404; F:protein ADP-ribosylase activity; ISS:UniProtKB.
GO; GO:0006284; P:base-excision repair; IMP:MGI.
GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
GO; GO:0006281; P:DNA repair; TAS:MGI.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
Gene3D; 1.20.142.10; -; 1.
Gene3D; 2.20.140.10; -; 1.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
InterPro; IPR036930; WGR_dom_sf.
InterPro; IPR008893; WGR_domain.
Pfam; PF00644; PARP; 1.
Pfam; PF02877; PARP_reg; 1.
Pfam; PF05406; WGR; 1.
SMART; SM00773; WGR; 1.
SUPFAM; SSF142921; SSF142921; 1.
SUPFAM; SSF47587; SSF47587; 1.
PROSITE; PS51060; PARP_ALPHA_HD; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Complete proteome;
DNA-binding; Glycosyltransferase; NAD; Nucleus; Phosphoprotein;
Reference proteome; Transferase.
CHAIN 1 559 Poly [ADP-ribose] polymerase 2.
/FTId=PRO_0000211328.
DOMAIN 207 324 PARP alpha-helical. {ECO:0000255|PROSITE-
ProRule:PRU00398}.
DOMAIN 332 559 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
DNA_BIND 1 65 {ECO:0000255}.
MOTIF 3 9 Nuclear localization signal.
{ECO:0000255}.
MOTIF 33 39 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 36 36 N6-(ADP-ribosyl)lysine; alternate.
{ECO:0000269|PubMed:18436469}.
MOD_RES 36 36 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:18436469}.
MOD_RES 37 37 N6-(ADP-ribosyl)lysine; alternate.
{ECO:0000269|PubMed:18436469}.
MOD_RES 37 37 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:18436469}.
MOD_RES 208 208 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UGN5}.
MUTAGEN 36 36 K->R: Decreases levels of mono-ADP-
ribosylation without loss of enzyme
activity. {ECO:0000269|PubMed:18436469}.
MUTAGEN 37 37 K->R: Decreases levels of mono-ADP-
ribosylation without loss of enzyme
activity. {ECO:0000269|PubMed:18436469}.
CONFLICT 82 82 L -> V (in Ref. 2; AAK13253).
{ECO:0000305}.
CONFLICT 177 177 V -> I (in Ref. 2; AAK13253).
{ECO:0000305}.
CONFLICT 486 486 R -> Q (in Ref. 2; AAK13253).
{ECO:0000305}.
HELIX 212 222 {ECO:0000244|PDB:1GS0}.
HELIX 224 232 {ECO:0000244|PDB:1GS0}.
TURN 233 235 {ECO:0000244|PDB:1GS0}.
STRAND 238 241 {ECO:0000244|PDB:1GS0}.
HELIX 243 245 {ECO:0000244|PDB:1GS0}.
HELIX 248 266 {ECO:0000244|PDB:1GS0}.
HELIX 272 284 {ECO:0000244|PDB:1GS0}.
HELIX 300 320 {ECO:0000244|PDB:1GS0}.
HELIX 333 340 {ECO:0000244|PDB:1GS0}.
STRAND 343 347 {ECO:0000244|PDB:1GS0}.
HELIX 353 364 {ECO:0000244|PDB:1GS0}.
STRAND 372 385 {ECO:0000244|PDB:1GS0}.
HELIX 388 391 {ECO:0000244|PDB:1GS0}.
STRAND 399 406 {ECO:0000244|PDB:1GS0}.
HELIX 408 410 {ECO:0000244|PDB:1GS0}.
HELIX 411 417 {ECO:0000244|PDB:1GS0}.
STRAND 424 426 {ECO:0000244|PDB:1GS0}.
HELIX 428 430 {ECO:0000244|PDB:1GS0}.
STRAND 434 441 {ECO:0000244|PDB:1GS0}.
HELIX 443 447 {ECO:0000244|PDB:1GS0}.
HELIX 448 450 {ECO:0000244|PDB:1GS0}.
STRAND 454 456 {ECO:0000244|PDB:1GS0}.
STRAND 458 467 {ECO:0000244|PDB:1GS0}.
STRAND 470 476 {ECO:0000244|PDB:1GS0}.
HELIX 481 484 {ECO:0000244|PDB:1GS0}.
STRAND 489 493 {ECO:0000244|PDB:1GS0}.
STRAND 496 498 {ECO:0000244|PDB:1GS0}.
HELIX 501 503 {ECO:0000244|PDB:1GS0}.
STRAND 505 507 {ECO:0000244|PDB:1GS0}.
STRAND 510 512 {ECO:0000244|PDB:1GS0}.
STRAND 525 527 {ECO:0000244|PDB:1GS0}.
STRAND 534 538 {ECO:0000244|PDB:1GS0}.
HELIX 540 542 {ECO:0000244|PDB:1GS0}.
STRAND 543 555 {ECO:0000244|PDB:1GS0}.
SEQUENCE 559 AA; 63397 MW; E0AEDAEE412C1445 CRC64;
MAPRRQRSGS GRRVLNEAKK VDNGNKATED DSPPGKKMRT CQRKGPMAGG KDADRTKDNR
DSVKTLLLKG KAPVDPECAA KLGKAHVYCE GDDVYDVMLN QTNLQFNNNK YYLIQLLEDD
AQRNFSVWMR WGRVGKTGQH SLVTCSGDLN KAKEIFQKKF LDKTKNNWED RENFEKVPGK
YDMLQMDYAA STQDESKTKE EETLKPESQL DLRVQELLKL ICNVQTMEEM MIEMKYDTKR
APLGKLTVAQ IKAGYQSLKK IEDCIRAGQH GRALVEACNE FYTRIPHDFG LSIPPVIRTE
KELSDKVKLL EALGDIEIAL KLVKSERQGL EHPLDQHYRN LHCALRPLDH ESNEFKVISQ
YLQSTHAPTH KDYTMTLLDV FEVEKEGEKE AFREDLPNRM LLWHGSRLSN WVGILSHGLR
VAPPEAPITG YMFGKGIYFA DMSSKSANYC FASRLKNTGL LLLSEVALGQ CNELLEANPK
AQGLLRGKHS TKGMGKMAPS PAHFITLNGS TVPLGPASDT GILNPEGYTL NYNEFIVYSP
NQVRMRYLLK IQFNFLQLW


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