PARP1_MOUSE
ID PARP1_MOUSE Reviewed; 1013 AA.
AC P11103; Q9JLX4; Q9QVQ3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Poly [ADP-ribose] polymerase 1;
DE Short=PARP-1;
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 1;
DE Short=ARTD1;
DE AltName: Full=DNA ADP-ribosyltransferase PARP1 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 1;
DE Short=ADPRT 1;
DE AltName: Full=Poly[ADP-ribose] synthase 1;
DE Short=msPARP;
DE AltName: Full=Protein poly-ADP-ribosyltransferase PARP1 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
GN Name=Parp1; Synonyms=Adprp, Adprt, Adprt1;
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 1).
RC STRAIN=BXSB;
RX PubMed=2498841; DOI=10.1093/nar/17.9.3387;
RA Huppi K., Bhatia K., Siwarski D., Klinman D., Cherney B., Smulson M.;
RT "Sequence and organization of the mouse poly (ADP-ribose) polymerase
RT gene.";
RL Nucleic Acids Res. 17:3387-3401(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6 X 129/Sv; TISSUE=Fibroblast;
RX PubMed=10809783; DOI=10.1074/jbc.275.20.15504;
RA Sallmann F.R., Vodenicharov M.D., Wang Z.-Q., Poirier G.G.;
RT "Characterization of sPARP-1. An alternative product of PARP-1 gene with
RT poly(ADP-ribose) polymerase activity independent of DNA strand breaks.";
RL J. Biol. Chem. 275:15504-15511(2000).
RN [3]
RP PROTEIN SEQUENCE OF 109-119 AND 865-875, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=9642267; DOI=10.1074/jbc.273.27.17025;
RA Borggrefe T., Wabl M., Akhmedov A.T., Jessberger R.;
RT "A B-cell-specific DNA recombination complex.";
RL J. Biol. Chem. 273:17025-17035(1998).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=7578427; DOI=10.1016/0300-9084(96)88158-2;
RA Auer B., Flick K., Wang Z.Q., Haidacher D., Jaeger S., Berghammer H.,
RA Kofler B., Schweiger M., Wagner E.F.;
RT "On the biological role of the nuclear polymerizing NAD+: protein(ADP-
RT ribosyl) transferase (ADPRT): ADPRT from Dictyostelium discoideum and
RT inactivation of the ADPRT gene in the mouse.";
RL Biochimie 77:444-449(1995).
RN [5]
RP INTERACTION WITH PARP2; XRCC1; POLB AND LRIG3, AND DEVELOPMENTAL STAGE.
RX PubMed=11948190; DOI=10.1074/jbc.m202390200;
RA Schreiber V., Ame J.-C., Dolle P., Schultz I., Rinaldi B., Fraulob V.,
RA Menissier-de Murcia J., de Murcia G.M.;
RT "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base
RT excision DNA repair in association with PARP-1 and XRCC1.";
RL J. Biol. Chem. 277:23028-23036(2002).
RN [6]
RP INTERACTION WITH ZNF423.
RX PubMed=14623329; DOI=10.1016/j.bbrc.2003.10.053;
RA Ku M.-C., Stewart S., Hata A.;
RT "Poly(ADP-ribose) polymerase 1 interacts with OAZ and regulates BMP-target
RT genes.";
RL Biochem. Biophys. Res. Commun. 311:702-707(2003).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=12727891; DOI=10.1093/emboj/cdg206;
RA Menissier de Murcia J., Ricoul M., Tartier L., Niedergang C., Huber A.,
RA Dantzer F., Schreiber V., Ame J.C., Dierich A., LeMeur M., Sabatier L.,
RA Chambon P., de Murcia G.;
RT "Functional interaction between PARP-1 and PARP-2 in chromosome stability
RT and embryonic development in mouse.";
RL EMBO J. 22:2255-2263(2003).
RN [8]
RP S-NITROSYLATION.
RX PubMed=16464859; DOI=10.1074/jbc.m511049200;
RA Yu Z., Kuncewicz T., Dubinsky W.P., Kone B.C.;
RT "Nitric oxide-dependent negative feedback of PARP-1 trans-activation of the
RT inducible nitric-oxide synthase gene.";
RL J. Biol. Chem. 281:9101-9109(2006).
RN [9]
RP INTERACTION WITH TIAM2.
RX PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028;
RA Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T., Nakayama M.,
RA Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K., Amano M.;
RT "Rho-kinase modulates the function of STEF, a Rac GEF, through its
RT phosphorylation.";
RL Biochem. Biophys. Res. Commun. 355:788-794(2007).
RN [10]
RP INTERACTION WITH RNF4.
RX PubMed=19779455; DOI=10.1038/emboj.2009.279;
RA Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C., Zhang X.D.,
RA Bischof O., Seeler J.S., Dejean A.;
RT "PARP-1 transcriptional activity is regulated by sumoylation upon heat
RT shock.";
RL EMBO J. 28:3534-3548(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP INTERACTION WITH SNAI1.
RX PubMed=21577210; DOI=10.1038/onc.2011.153;
RA Rodriguez M.I., Gonzalez-Flores A., Dantzer F., Collard J.,
RA de Herreros A.G., Oliver F.J.;
RT "Poly(ADP-ribose)-dependent regulation of Snail1 protein stability.";
RL Oncogene 30:4365-4372(2011).
RN [13]
RP FUNCTION, ADP-RIBOSYLATION AT LYS-520, AND MUTAGENESIS OF ASP-387; GLU-488;
RP GLU-491; LYS-498; LYS-520 AND LYS-523.
RX PubMed=21680843; DOI=10.1126/science.1202723;
RA Mao Z., Hine C., Tian X., Van Meter M., Au M., Vaidya A., Seluanov A.,
RA Gorbunova V.;
RT "SIRT6 promotes DNA repair under stress by activating PARP1.";
RL Science 332:1443-1446(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP INTERACTION WITH KHDC3, AND SUBCELLULAR LOCATION.
RX PubMed=25936915; DOI=10.1016/j.stem.2015.03.017;
RA Zhao B., Zhang W.D., Duan Y.L., Lu Y.Q., Cun Y.X., Li C.H., Guo K.,
RA Nie W.H., Li L., Zhang R., Zheng P.;
RT "Filia Is an ESC-Specific Regulator of DNA Damage Response and Safeguards
RT Genomic Stability.";
RL Cell Stem Cell 16:684-698(2015).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-
CC ribosylation of proteins and plays a key role in DNA repair
CC (PubMed:21680843). Mediates glutamate, aspartate, serine or tyrosine
CC ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is
CC transferred to the acceptor carboxyl group of target residues and
CC further ADP-ribosyl groups are transferred to the 2'-position of the
CC terminal adenosine moiety, building up a polymer with an average chain
CC length of 20-30 units (By similarity). Serine ADP-ribosylation of
CC proteins constitutes the primary form of ADP-ribosylation of proteins
CC in response to DNA damage (By similarity). Mainly mediates glutamate
CC and aspartate ADP-ribosylation of target proteins in absence of HPF1
CC (By similarity). Following interaction with HPF1, catalyzes serine ADP-
CC ribosylation of target proteins; HPF1 conferring serine specificity by
CC completing the PARP1 active site (By similarity). Also catalyzes
CC tyrosine ADP-ribosylation of target proteins following interaction with
CC HPF1 (By similarity). PARP1 initiates the repair of DNA breaks:
CC recognizes and binds DNA breaks within chromatin and recruits HPF1,
CC licensing serine ADP-ribosylation of target proteins, such as histones,
CC thereby promoting decompaction of chromatin and the recruitment of
CC repair factors leading to the reparation of DNA strand breaks (By
CC similarity). In addition to base excision repair (BER) pathway, also
CC involved in double-strand breaks (DSBs) repair: together with TIMELESS,
CC accumulates at DNA damage sites and promotes homologous recombination
CC repair by mediating poly-ADP-ribosylation (By similarity). Mediates the
CC poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF
CC and CHFR (By similarity). In addition to proteins, also able to ADP-
CC ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini
CC containing terminal phosphates and a 2'-OH group in single- and double-
CC stranded DNA, respectively (By similarity). Required for PARP9 and
CC DTX3L recruitment to DNA damage sites (By similarity). PARP1-dependent
CC PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific
CC recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage
CC sites (By similarity). Acts as a regulator of transcription: positively
CC regulates the transcription of MTUS1 and negatively regulates the
CC transcription of MTUS2/TIP150 (By similarity). Plays a role in the
CC positive regulation of IFNG transcription in T-helper 1 cells as part
CC of an IFNG promoter-binding complex with TXK and EEF1A1 (By
CC similarity). Involved in the synthesis of ATP in the nucleus, together
CC with NMNAT1, PARG and NUDT5 (By similarity). Nuclear ATP generation is
CC required for extensive chromatin remodeling events that are energy-
CC consuming (By similarity). {ECO:0000250|UniProtKB:P09874,
CC ECO:0000269|PubMed:21680843}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142556; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58233;
CC Evidence={ECO:0000250|UniProtKB:P09874};
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:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000250|UniProtKB:P09874};
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:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:58236, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:15092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:46858, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142557; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58237;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- SUBUNIT: Homo- and heterodimer with PARP2 (By similarity). Interacts
CC with APTX (By similarity). Component of a base excision repair (BER)
CC complex, containing at least XRCC1, PARP1, PARP2, POLB and LRIG3
CC (PubMed:11948190). Interacts with SRY (By similarity). The SWAP complex
CC consists of NPM1, NCL, PARP1 and SWAP70 (PubMed:9642267). Interacts
CC with TIAM2 (PubMed:17320046). Interacts with PARP3; leading to activate
CC PARP1 in absence of DNA (By similarity). Interacts (when poly-ADP-
CC ribosylated) with CHD1L (via macro domain) (By similarity). Interacts
CC with the DNA polymerase alpha catalytic subunit POLA1; this interaction
CC functions as part of the control of replication fork progression (By
CC similarity). Interacts with EEF1A1 and TXK (By similarity). Interacts
CC with RNF4 (PubMed:19779455). Interacts with RNF146 (By similarity).
CC Interacts with ZNF423 (PubMed:14623329). Interacts with APLF (By
CC similarity). Interacts with SNAI1 (via zinc fingers); the interaction
CC requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated
CC (active) by GSK3B (PubMed:21577210). Interacts (when poly-ADP-
CC ribosylated) with PARP9 (By similarity). Interacts with NR4A3;
CC activates PARP1 by improving acetylation of PARP1 and suppressing the
CC interaction between PARP1 and SIRT1 (By similarity). Interacts (via
CC catalytic domain) with PUM3; the interaction inhibits the poly-ADP-
CC ribosylation activity of PARP1 and the degradation of PARP1 by CASP3
CC following genotoxic stress (By similarity). Interacts (via the PARP
CC catalytic domain) with HPF1 (By similarity). Interacts with ZNF365 (By
CC similarity). Interacts with RRP1B (By similarity). Interacts with
CC TIMELESS; the interaction is direct (By similarity). Interacts with
CC CGAS; leading to impede the formation of the PARP1-TIMELESS complex (By
CC similarity). Interacts with KHDC3, the interaction is increased
CC following the formation of DNA double-strand breaks (PubMed:25936915).
CC {ECO:0000250|UniProtKB:P09874, ECO:0000250|UniProtKB:P27008,
CC ECO:0000269|PubMed:11948190, ECO:0000269|PubMed:14623329,
CC ECO:0000269|PubMed:17320046, ECO:0000269|PubMed:19779455,
CC ECO:0000269|PubMed:21577210, ECO:0000269|PubMed:25936915,
CC ECO:0000269|PubMed:9642267}.
CC -!- INTERACTION:
CC P11103; Q9WTL8: Arntl; NbExp=7; IntAct=EBI-642213, EBI-644534;
CC P11103; P70677: Casp3; NbExp=3; IntAct=EBI-642213, EBI-1790419;
CC P11103; P97864: Casp7; NbExp=3; IntAct=EBI-642213, EBI-5307197;
CC P11103; P70288: Hdac2; NbExp=3; IntAct=EBI-642213, EBI-302251;
CC P11103; P20263: Pou5f1; NbExp=2; IntAct=EBI-642213, EBI-1606219;
CC P11103; Q3TKT4: Smarca4; NbExp=2; IntAct=EBI-642213, EBI-1210244;
CC P11103; P03087; Xeno; NbExp=2; IntAct=EBI-642213, EBI-1555770;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25936915}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P09874}. Chromosome
CC {ECO:0000250|UniProtKB:P09874}. Note=Localizes to sites of DNA damage.
CC {ECO:0000250|UniProtKB:P09874}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=P11103-1; Sequence=Displayed;
CC Name=2; Synonyms=Short {ECO:0000303|PubMed:10809783}, sPARP-1
CC {ECO:0000303|PubMed:10809783};
CC IsoId=P11103-2; Sequence=VSP_018970;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:9642267). Expression is
CC correlated with proliferation, with higher levels occurring during
CC early fetal development and organogenesis and in the highly
CC proliferative cell compartments of adult (PubMed:9642267). Expressed in
CC B-cells that have been induced to switch to various Ig isotypes
CC (PubMed:9642267). {ECO:0000269|PubMed:9642267}.
CC -!- DEVELOPMENTAL STAGE: At stage 12.5 dpc, expressed at high level in the
CC developing liver and kidneys (PubMed:11948190). Expressed at higher
CC level in the genital ridge and the spinal ganglia (PubMed:11948190). At
CC 18.5 dpc, preferentially expressed in the thymus and in regions of the
CC nervous system (PubMed:11948190). Within the developing trunk,
CC preferential expression persisted in the liver and became restricted to
CC the cortical region of the kidney, spleen, adrenal gland, and to
CC stomach and intestinal epithelia (PubMed:11948190). From 14.5 dpc to
CC 18.5 dpc, as well as in the adult, expressed at the highest level in
CC thymus (PubMed:11948190). Expression is particularly high in the
CC subcapsular zone of the thymus where immature lymphocytes proliferate
CC (PubMed:11948190). Expressed at high level in the seminiferous tubules
CC of the developing testis (PubMed:11948190).
CC {ECO:0000269|PubMed:11948190}.
CC -!- DOMAIN: The N-terminal disordered region does not act as a key DNA-
CC binding domain. The WGR and PARP catalytic domains function together to
CC recruit PARP1 to sites of DNA breaks. The N-terminal disordered region
CC is only required for activation on specific types of DNA damage.
CC {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- DOMAIN: The WGR domain bridges two nucleosomes, with the broken DNA
CC aligned in a position suitable for ligation. The bridging induces
CC structural changes in PARP1 that signal the recognition of a DNA break
CC to the catalytic domain of PARP1, promoting HPF1 recruitment and
CC subsequent activation of PARP1, licensing serine ADP-ribosylation of
CC target proteins. {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- PTM: Poly-ADP-ribosylated on glutamate and aspartate residues by
CC autocatalysis (By similarity). Poly-ADP-ribosylated by PARP2; poly-ADP-
CC ribosylation mediates the recruitment of CHD1L to DNA damage sites (By
CC similarity). ADP-ribosylated on serine by autocatalysis; serine ADP-
CC ribosylation takes place following interaction with HPF1 (By
CC similarity). Auto poly-ADP-ribosylated on serine residues, leading to
CC dissociation of the PARP1-HPF1 complex from chromatin (By similarity).
CC Mono-ADP-ribosylated at Lys-520 by SIRT6 in response to oxidative
CC stress, promoting recruitment to double-strand breaks (DSBs) sites
CC (PubMed:21680843). {ECO:0000250|UniProtKB:P09874,
CC ECO:0000250|UniProtKB:Q9UGN5, ECO:0000269|PubMed:21680843}.
CC -!- PTM: S-nitrosylated, leading to inhibit transcription regulation
CC activity. {ECO:0000269|PubMed:16464859}.
CC -!- PTM: Phosphorylated by PRKDC and TXK. {ECO:0000250|UniProtKB:P09874}.
CC -!- DISRUPTION PHENOTYPE: Mice show a complete lack of nuclear poly-ADP-
CC ribosylation (PubMed:7578427). Mice are however viable and fertile
CC (PubMed:7578427). Moreover, repair of UV and MNNG induced DNA damage
CC are not affected (PubMed:7578427). However, about 30% of the mutant
CC mice developed pathological skin aberrations on a mixed 129/Sv x
CC C57B1/6 genetic background (PubMed:7578427). Mice lacking both Parp1
CC and Parp2 are not viable and die at the onset of gastrulation
CC (PubMed:12727891). {ECO:0000269|PubMed:12727891,
CC ECO:0000269|PubMed:7578427}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF61293.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X14206; CAA32421.1; -; mRNA.
DR EMBL; AF126717; AAF61293.1; ALT_INIT; mRNA.
DR PIR; S04200; S04200.
DR AlphaFoldDB; P11103; -.
DR SMR; P11103; -.
DR CORUM; P11103; -.
DR DIP; DIP-39371N; -.
DR IntAct; P11103; 20.
DR MINT; P11103; -.
DR STRING; 10090.ENSMUSP00000027777; -.
DR BindingDB; P11103; -.
DR ChEMBL; CHEMBL3740; -.
DR iPTMnet; P11103; -.
DR PhosphoSitePlus; P11103; -.
DR SwissPalm; P11103; -.
DR EPD; P11103; -.
DR MaxQB; P11103; -.
DR PaxDb; P11103; -.
DR PeptideAtlas; P11103; -.
DR PRIDE; P11103; -.
DR ProteomicsDB; 288064; -. [P11103-1]
DR ProteomicsDB; 288065; -. [P11103-2]
DR MGI; MGI:1340806; Parp1.
DR eggNOG; KOG1037; Eukaryota.
DR InParanoid; P11103; -.
DR PhylomeDB; P11103; -.
DR Reactome; R-MMU-110362; POLB-Dependent Long Patch Base Excision Repair.
DR Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR ChiTaRS; Parp1; mouse.
DR PRO; PR:P11103; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P11103; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051287; F:NAD binding; ISO:MGI.
DR GO; GO:0140294; F:NAD DNA ADP-ribosyltransferase activity; ISO:MGI.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:MGI.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; IMP:MGI.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR GO; GO:0071451; P:cellular response to superoxide; IDA:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0030592; P:DNA ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0006259; P:DNA metabolic process; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; TAS:MGI.
DR GO; GO:0006302; P:double-strand break repair; IGI:MGI.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; ISO:MGI.
DR GO; GO:0043504; P:mitochondrial DNA repair; ISO:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:2001170; P:negative regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; IMP:MGI.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; IMP:BHF-UCL.
DR GO; GO:0018424; P:peptidyl-glutamic acid poly-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; ISO:MGI.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:MGI.
DR GO; GO:1904762; P:positive regulation of myofibroblast differentiation; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:1903518; P:positive regulation of single strand break repair; IGI:UniProtKB.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; ISO:MGI.
DR GO; GO:0036211; P:protein modification process; ISO:MGI.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:MGI.
DR GO; GO:0050790; P:regulation of catalytic activity; ISO:MGI.
DR GO; GO:0044030; P:regulation of DNA methylation; ISO:MGI.
DR GO; GO:0040009; P:regulation of growth rate; IMP:MGI.
DR GO; GO:1903376; P:regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:1903516; P:regulation of single strand break repair; IMP:MGI.
DR GO; GO:0010990; P:regulation of SMAD protein complex assembly; ISO:MGI.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; IGI:UniProtKB.
DR Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.30.1740.10; -; 2.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR012982; PADR1.
DR InterPro; IPR038650; PADR1_dom_sf.
DR InterPro; IPR008288; PARP.
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 InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08063; PADR1; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR Pfam; PF00645; zf-PARP; 2.
DR PIRSF; PIRSF000489; NAD_ADPRT; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 2.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS00347; PARP_ZN_FINGER_1; 2.
DR PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
DR PROSITE; PS51977; WGR; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Alternative initiation; Chromosome;
KW Direct protein sequencing; DNA damage; DNA repair; DNA-binding;
KW Glycosyltransferase; Isopeptide bond; Metal-binding; NAD;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; S-nitrosylation; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CHAIN 2..1013
FT /note="Poly [ADP-ribose] polymerase 1"
FT /id="PRO_0000023259"
FT DOMAIN 385..476
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 541..637
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 661..778
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 787..1013
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ZN_FING 9..93
FT /note="PARP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT ZN_FING 113..203
FT /note="PARP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT REGION 200..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..523
FT /note="Automodification domain"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT REGION 489..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 207..209
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOTIF 221..226
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT ACT_SITE 987
FT /note="For poly [ADP-ribose] polymerase activity"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT BINDING 861..863
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 870
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 877
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 903
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 387
FT /note="PolyADP-ribosyl aspartic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 407
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 413
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 435
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 437
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 444
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 445
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 448
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 456
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 484
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 488
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 491
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 499
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 503
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 506
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 512
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 513
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 518
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 519
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 520
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000269|PubMed:21680843"
FT MOD_RES 599
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 620
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 511
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 527
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 747
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 747
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT VAR_SEQ 1..521
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10809783"
FT /id="VSP_018970"
FT MUTAGEN 387
FT /note="D->A: Does not affect mono-ADP-ribosylation by
FT SIRT6."
FT /evidence="ECO:0000269|PubMed:21680843"
FT MUTAGEN 488
FT /note="E->A: Does not affect mono-ADP-ribosylation by
FT SIRT6."
FT /evidence="ECO:0000269|PubMed:21680843"
FT MUTAGEN 491
FT /note="E->A: Does not affect mono-ADP-ribosylation by
FT SIRT6."
FT /evidence="ECO:0000269|PubMed:21680843"
FT MUTAGEN 498
FT /note="K->A: Does not affect mono-ADP-ribosylation by
FT SIRT6."
FT /evidence="ECO:0000269|PubMed:21680843"
FT MUTAGEN 520
FT /note="K->A: Abolished mono-ADP-ribosylation by SIRT6."
FT /evidence="ECO:0000269|PubMed:21680843"
FT MUTAGEN 523
FT /note="K->A: Does not affect mono-ADP-ribosylation by
FT SIRT6."
FT /evidence="ECO:0000269|PubMed:21680843"
FT CONFLICT 114
FT /note="A -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="L -> V (in Ref. 2; AAF61293)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="E -> D (in Ref. 2; AAF61293)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="Q -> H (in Ref. 2; AAF61293)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="N -> D (in Ref. 2; AAF61293)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="D -> E (in Ref. 2; AAF61293)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="Q -> E (in Ref. 2; AAF61293)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="Q -> L (in Ref. 2; AAF61293)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="A -> C (in Ref. 2; AAF61293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1013 AA; 113100 MW; 5E54C3E5F60BB922 CRC64;
MAEASERLYR VQYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV
GQSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD GSGGKAEKTL GDFAAEYAKS
NRSMCKGCLE KIEKGQMRLS KKMVDPEKPQ LGMIDRWYHP TCFVKKRDEL GFRPEYSASQ
LKGFSLLSAE DKEALKKQLP AIKNEGKRKG DEVDGTDEVA KKKSRKETDK YSKLEKALKA
QNELIWNIKD ELKKACSTND LKELLIFNQQ QVPSGESAIL DRVADGMAFG ALLPCKECSG
QLVFKSDAYY CTGDVTAWTK CMVKTQNPSR KEWVTPKEFR EISYLKKLKV KKQDRIFPPE
SSAPITVHWP LSVTSAPTAV NSSAPADKPL SNMKILTLGK LSQNKDEAKA VIEKLGGKLT
GSANKASLCI SIKKEVEKMN KKMEEVKEAN IRVVSEDFLQ DVSASTKSLQ DLLSAHSLSP
WGAEVKAEPG EVVAPRGKSA APSKKSKGCF KEEGVNKSEK RMKLTLKGGA AVDPDSGLEH
SAHVLEKGGK VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR LGTVIGSNKL
EQMPSKEEAV EQFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA VKKLTVKPGT
KSKLPKPVQE LVGMIFDVDS MKKALVEYEI DLQKMPLGKL SRRQIQAAYS ILSEVQQPVS
QGSSESQILD LSNRFYTLIP HDFGMKKPPL LNNADSVQAK VEMLDNLLDI EVAYSLLRGG
SDDSSKDPID VNYEKLKTDI KVVDRDSEEA EVIRKYVKNT HATTHNAYDL EVIDIFKIER
EGESQRYKPF RQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV
SKSANYCHTS QGDPIGLIML GEVALGNMYE LKHASHISKL PKGKHSVKGL GKTTPDPSAS
ITLEGVEVPL GTGIPSGVND TALLYNEYIV YDIAQVNLKY LLKLKFNFKT SLW
