PARP3_MOUSE
ID PARP3_MOUSE Reviewed; 533 AA.
AC Q3ULW8; A0A1L1SRP6; E9PX17; E9Q992; Q3UGL7; Q8BHN6; Q8BXU2; Q8CFB8; Q91YR6;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP3 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9Y6F1};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 3 {ECO:0000250|UniProtKB:Q9Y6F1};
DE Short=ARTD3 {ECO:0000250|UniProtKB:Q9Y6F1};
DE AltName: Full=DNA ADP-ribosyltransferase PARP3 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9Y6F1};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 3 {ECO:0000303|PubMed:12448766};
DE Short=ADPRT-3 {ECO:0000303|PubMed:12448766};
DE AltName: Full=Poly [ADP-ribose] polymerase 3 {ECO:0000303|PubMed:21270334};
DE Short=PARP-3 {ECO:0000303|PubMed:21270334};
DE AltName: Full=Poly[ADP-ribose] synthase 3 {ECO:0000303|PubMed:21270334};
DE Short=pADPRT-3 {ECO:0000250|UniProtKB:Q9Y6F1};
GN Name=Parp3 {ECO:0000303|PubMed:21270334, ECO:0000312|MGI:MGI:1891258};
GN Synonyms=Adprt3 {ECO:0000303|PubMed:12448766};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=12448766;
RA Urbanek P., Paces J., Kralova J., Dvorak M., Paces V.;
RT "Cloning and expression of PARP-3 (Adprt3) and U3-55k, two genes closely
RT linked on mouse chromosome 9.";
RL Folia Biol. (Praha) 48:182-191(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Mammary gland, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21270334; DOI=10.1073/pnas.1016574108;
RA Boehler C., Gauthier L.R., Mortusewicz O., Biard D.S., Saliou J.M.,
RA Bresson A., Sanglier-Cianferani S., Smith S., Schreiber V., Boussin F.,
RA Dantzer F.;
RT "Poly(ADP-ribose) polymerase 3 (PARP3), a newcomer in cellular response to
RT DNA damage and mitotic progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2783-2788(2011).
RN [6]
RP FUNCTION.
RX PubMed=24598253; DOI=10.1093/nar/gku174;
RA Beck C., Boehler C., Guirouilh Barbat J., Bonnet M.E., Illuzzi G.,
RA Ronde P., Gauthier L.R., Magroun N., Rajendran A., Lopez B.S., Scully R.,
RA Boussin F.D., Schreiber V., Dantzer F.;
RT "PARP3 affects the relative contribution of homologous recombination and
RT nonhomologous end-joining pathways.";
RL Nucleic Acids Res. 42:5616-5632(2014).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26000965; DOI=10.1371/journal.pgen.1005240;
RA Robert I., Gaudot L., Rogier M., Heyer V., Noll A., Dantzer F.,
RA Reina-San-Martin B.;
RT "Parp3 negatively regulates immunoglobulin class switch recombination.";
RL PLoS Genet. 11:E1005240-E1005240(2015).
RN [8]
RP FUNCTION.
RX PubMed=30213852; DOI=10.1073/pnas.1801591115;
RA Layer J.V., Cleary J.P., Brown A.J., Stevenson K.E., Morrow S.N.,
RA Van Scoyk A., Blasco R.B., Karaca E., Meng F.L., Frock R.L., Tivey T.,
RA Kim S., Fuchs H., Chiarle R., Alt F.W., Roberts S.A., Weinstock D.M.,
RA Day T.A.;
RT "Parp3 promotes long-range end joining in murine cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:10076-10081(2018).
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins and plays a key role in the response to
CC DNA damage (PubMed:21270334, PubMed:24598253). Mediates mono-ADP-
CC ribosylation of glutamate, aspartate or lysine residues on target
CC proteins (By similarity). In contrast to PARP1 and PARP2, it is not
CC able to mediate poly-ADP-ribosylation (By similarity). Associates with
CC a number of DNA repair factors and is involved in the response to
CC exogenous and endogenous DNA strand breaks (PubMed:21270334). Together
CC with APLF, promotes the retention of the LIG4-XRCC4 complex on
CC chromatin and accelerate DNA ligation during non-homologous end-joining
CC (NHEJ) (By similarity). Cooperates with the XRCC5-XRCC6 (Ku80-Ku70)
CC heterodimer to limit end-resection thereby promoting accurate NHEJ
CC (PubMed:24598253). Involved in DNA repair by mediating mono-ADP-
CC ribosylation of a limited number of acceptor proteins involved in
CC chromatin architecture and in DNA metabolism, such as XRCC5 and XRCC6
CC (By similarity). ADP-ribosylation follows DNA damage and appears as an
CC obligatory step in a detection/signaling pathway leading to the
CC reparation of DNA strand breaks (By similarity). May link the DNA
CC damage surveillance network to the mitotic fidelity checkpoint (By
CC similarity). In addition to proteins, also able to ADP-ribosylate DNA:
CC mediates DNA mono-ADP-ribosylation of DNA strand break termini via
CC covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal
CC phosphate residues in DNA containing multiple strand breaks (By
CC similarity). Acts as a negative regulator of immunoglobulin class
CC switch recombination, probably by controlling the level of AICDA /AID
CC on the chromatin (PubMed:26000965). {ECO:0000250|UniProtKB:Q9Y6F1,
CC ECO:0000269|PubMed:21270334, ECO:0000269|PubMed:24598253,
CC ECO:0000269|PubMed:26000965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6F1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6F1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + NAD(+) = H(+) + N(6)-(ADP-D-ribosyl)-L-
CC lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58220, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:15088, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142515; Evidence={ECO:0000250|UniProtKB:Q9Y6F1};
CC -!- SUBUNIT: Interacts with PARP1; leading to activate PARP1 in absence of
CC DNA. Interacts with PRKDC. Interacts with XRCC5/Ku80; the interaction
CC is dependent on nucleic acids. Interacts with XRCC6/Ku70; the
CC interaction is dependent on nucleic acids. Interacts with EZH2, HDAC1,
CC HDAC2, SUZ12, YY1, LRIG3 and LIG4. {ECO:0000250|UniProtKB:Q9Y6F1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus
CC {ECO:0000250|UniProtKB:Q8K3Y6}. Note=Localizes in the cytoplasm at
CC steady state, but shuttles between nucleus and cytoplasm in a XPO1-
CC dependent manner. {ECO:0000250|UniProtKB:Q8K3Y6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3ULW8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3ULW8-2; Sequence=VSP_060032;
CC -!- PTM: Auto-ADP-ribosylated. {ECO:0000250|UniProtKB:Q9Y6F1}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in normal conditions, but
CC mutant mice are sensitive to ionizing radiation (PubMed:21270334). In
CC B-cells, class switch recombination is increased, while somatic
CC hypermutation is unaffected, due to increased occupancy of Aicda/Aid at
CC the donor switch region (PubMed:26000965).
CC {ECO:0000269|PubMed:21270334, ECO:0000269|PubMed:26000965}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AF368233; AAN62793.1; -; mRNA.
DR EMBL; AY046316; AAL08055.1; -; mRNA.
DR EMBL; AY046317; AAL08056.1; -; mRNA.
DR EMBL; AK044223; BAC31826.1; -; mRNA.
DR EMBL; AK147868; BAE28191.1; -; mRNA.
DR EMBL; AK170541; BAE41867.1; -; mRNA.
DR EMBL; AK145259; BAE26330.1; -; mRNA.
DR EMBL; AC151729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014870; AAH14870.1; -; mRNA.
DR EMBL; BC058754; AAH58754.1; -; mRNA.
DR CCDS; CCDS23480.1; -. [Q3ULW8-2]
DR CCDS; CCDS81066.1; -. [Q3ULW8-1]
DR RefSeq; NP_001298079.1; NM_001311150.1. [Q3ULW8-1]
DR RefSeq; NP_663594.2; NM_145619.3. [Q3ULW8-2]
DR RefSeq; XP_006511781.1; XM_006511718.1. [Q3ULW8-1]
DR RefSeq; XP_006511782.1; XM_006511719.3. [Q3ULW8-1]
DR RefSeq; XP_006511783.1; XM_006511720.1. [Q3ULW8-2]
DR AlphaFoldDB; Q3ULW8; -.
DR SMR; Q3ULW8; -.
DR STRING; 10090.ENSMUSP00000064513; -.
DR BindingDB; Q3ULW8; -.
DR ChEMBL; CHEMBL3292; -.
DR iPTMnet; Q3ULW8; -.
DR PhosphoSitePlus; Q3ULW8; -.
DR EPD; Q3ULW8; -.
DR jPOST; Q3ULW8; -.
DR MaxQB; Q3ULW8; -.
DR PRIDE; Q3ULW8; -.
DR ProteomicsDB; 309835; -.
DR ProteomicsDB; 336548; -. [Q3ULW8-1]
DR ProteomicsDB; 342746; -.
DR ProteomicsDB; 363513; -.
DR ProteomicsDB; 365744; -.
DR Antibodypedia; 7395; 316 antibodies from 37 providers.
DR DNASU; 235587; -.
DR Ensembl; ENSMUST00000067218; ENSMUSP00000064513; ENSMUSG00000023249. [Q3ULW8-2]
DR Ensembl; ENSMUST00000112479; ENSMUSP00000108098; ENSMUSG00000023249. [Q3ULW8-1]
DR Ensembl; ENSMUST00000123555; ENSMUSP00000123054; ENSMUSG00000023249. [Q3ULW8-2]
DR GeneID; 235587; -.
DR KEGG; mmu:235587; -.
DR UCSC; uc009rjw.1; mouse.
DR UCSC; uc009rjz.1; mouse. [Q3ULW8-1]
DR CTD; 10039; -.
DR MGI; MGI:1891258; Parp3.
DR VEuPathDB; HostDB:ENSMUSG00000023249; -.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000158855; -.
DR HOGENOM; CLU_1566515_0_0_1; -.
DR InParanoid; Q3ULW8; -.
DR OMA; AKRVQPC; -.
DR OrthoDB; 909382at2759; -.
DR PhylomeDB; Q3ULW8; -.
DR TreeFam; TF315407; -.
DR BioGRID-ORCS; 235587; 3 hits in 107 CRISPR screens.
DR ChiTaRS; Parp3; mouse.
DR PRO; PR:Q3ULW8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3ULW8; protein.
DR Bgee; ENSMUSG00000023249; Expressed in extra-ocular muscle and 202 other tissues.
DR ExpressionAtlas; Q3ULW8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; IDA:MGI.
DR GO; GO:0140294; F:NAD DNA ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISO:MGI.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISO:MGI.
DR GO; GO:0030592; P:DNA ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IGI:MGI.
DR GO; GO:0045829; P:negative regulation of isotype switching; IMP:UniProtKB.
DR GO; GO:1905662; P:negative regulation of telomerase RNA reverse transcriptase activity; ISO:MGI.
DR GO; GO:0051106; P:positive regulation of DNA ligation; ISO:MGI.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISO:MGI.
DR GO; GO:1990166; P:protein localization to site of double-strand break; ISO:MGI.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; ISO:MGI.
DR Gene3D; 1.20.142.10; -; 1.
DR InterPro; IPR031275; PARP3.
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:SF66; PTHR10459:SF66; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Alternative splicing; Cytoplasm; DNA damage; DNA repair;
KW Glycosyltransferase; NAD; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..533
FT /note="Protein mono-ADP-ribosyltransferase PARP3"
FT /id="PRO_0000446170"
FT DOMAIN 57..147
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 181..299
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 313..533
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..18
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 9..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6F1"
FT MOD_RES 12
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6F1"
FT MOD_RES 24
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6F1"
FT MOD_RES 32
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6F1"
FT MOD_RES 138
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6F1"
FT MOD_RES 160
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6F1"
FT MOD_RES 230
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6F1"
FT MOD_RES 309
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6F1"
FT MOD_RES 310
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6F1"
FT VAR_SEQ 165..169
FT /note="Missing (in isoform 2)"
FT /id="VSP_060032"
FT CONFLICT 17
FT /note="R -> Q (in Ref. 2; BAC31826 and 4; AAH14870/
FT AAH58754)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="Y -> D (in Ref. 2; BAC31826 and 4; AAH14870/
FT AAH58754)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="A -> V (in Ref. 4; AAH14870/AAH58754)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="D -> N (in Ref. 2; BAC31826 and 4; AAH14870/
FT AAH58754)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="L -> I (in Ref. 2; BAE28191)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="S -> P (in Ref. 2; BAC31826 and 4; AAH14870/
FT AAH58754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 59949 MW; DC6EB55D4985766F CRC64;
MAPKRKASVQ TEGSKKRRQG TEEEDSFRST AEALRAAPAD NRVIRVDPSC PFSRNPGIQV
HEDYDCTLNQ TNIGNNNNKF YIIQLLEEGS RFFCWNRWGR VGEVGQSKMN HFTCLEDAKK
DFKKKFWEKT KNKWEERDRF VAQPNKYTLI EVQGEAESQE AVVKALSPQV YSGPVRTVVK
PCSLDPATQN LITNIFSKEM FKNAMTLMNL DVKKMPLGKL TKQQIARGFE ALEALEEAMK
NPTGDGQSLE ELSSCFYTVI PHNFGRSRPP PINSPDVLQA KKDMLLVLAD IELAQTLQAA
PGEEEEKVEE VPHPLDRDYQ LLRCQLQLLD SGESEYKAIQ TYLKQTGNSY RCPDLRHVWK
VNREGEGDRF QAHSKLGNRR LLWHGTNVAV VAAILTSGLR IMPHSGGRVG KGIYFASENS
KSAGYVTTMH CGGHQVGYMF LGEVALGKEH HITIDDPSLK SPPSGFDSVI ARGQTEPDPA
QDIELELDGQ PVVVPQGPPV QCPSFKSSSF SQSEYLIYKE SQCRLRYLLE IHL
