PARP2_MOUSE
ID PARP2_MOUSE Reviewed; 559 AA.
AC O88554; Q99N29;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Poly [ADP-ribose] polymerase 2;
DE Short=PARP-2;
DE Short=mPARP-2;
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:Q9UGN5};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 2;
DE Short=ARTD2;
DE AltName: Full=DNA ADP-ribosyltransferase PARP2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9UGN5};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 2;
DE Short=ADPRT-2;
DE AltName: Full=Poly[ADP-ribose] synthase 2 {ECO:0000303|PubMed:10338144};
DE Short=pADPRT-2 {ECO:0000303|PubMed:10338144};
DE AltName: Full=Protein poly-ADP-ribosyltransferase PARP2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9UGN5};
GN Name=Parp2; Synonyms=Adprt2, Adprtl2, Aspartl2;
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], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC TISSUE=Embryo;
RX PubMed=10364231; DOI=10.1074/jbc.274.25.17860;
RA Ame J.-C., Rolli V., Schreiber V., Niedergang C., Apiou F., Decker P.,
RA Muller S., Hoeger T., Menissier-de Murcia J., de Murcia G.M.;
RT "PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose)
RT polymerase.";
RL J. Biol. Chem. 274:17860-17868(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=129/Sv;
RX PubMed=11133988; DOI=10.1074/jbc.m007870200;
RA Ame J.-C., Schreiber V., Fraulob V., Dolle P., de Murcia G.M.,
RA Niedergang C.P.;
RT "A bidirectional promoter connects the poly(ADP-ribose) polymerase 2 (PARP-
RT 2) gene to the gene for RNase P RNA. Structure and expression of the mouse
RT PARP-2 gene.";
RL J. Biol. Chem. 276:11092-11099(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-559.
RC STRAIN=C57BL/6 X 129/Sv;
RX PubMed=10338144; DOI=10.1016/s0014-5793(99)00448-2;
RA Berghammer H., Ebner M., Marksteiner R., Auer B.;
RT "pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene
RT related to truncated pADPRT homologues in plants and Caenorhabditis
RT elegans.";
RL FEBS Lett. 449:259-263(1999).
RN [5]
RP INTERACTION WITH PARP1; XRCC1; POLB AND LRIG3, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND POLY-ADP-RIBOSYLATION.
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 ACETYLATION AT LYS-36 AND LYS-37, ADP-RIBOSYLATION AT LYS-36 AND LYS-37,
RP AND MUTAGENESIS OF LYS-36 AND LYS-37.
RX PubMed=18436469; DOI=10.1016/j.biocel.2008.03.008;
RA Haenni S.S., Hassa P.O., Altmeyer M., Fey M., Imhof R., Hottiger M.O.;
RT "Identification of lysines 36 and 37 of PARP-2 as targets for acetylation
RT and auto-ADP-ribosylation.";
RL Int. J. Biochem. Cell Biol. 40:2274-2283(2008).
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).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-
CC ribosylation of proteins and plays a key role in DNA repair
CC (PubMed:10364231). Mediates glutamate, aspartate or serine ADP-
CC 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). Mediates glutamate and
CC aspartate ADP-ribosylation of target proteins in absence of HPF1 (By
CC similarity). Following interaction with HPF1, catalyzes serine ADP-
CC ribosylation of target proteins; HPF1 conferring serine specificity by
CC completing the PARP2 active site (By similarity). PARP2 initiates the
CC repair of double-strand DNA breaks: recognizes and binds DNA breaks
CC within chromatin and recruits HPF1, licensing serine ADP-ribosylation
CC of target proteins, such as histones, thereby promoting decompaction of
CC chromatin and the recruitment of repair factors leading to the
CC reparation of DNA strand breaks (By similarity). In addition to
CC proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-
CC terminal phosphates at DNA strand breaks termini in nicked duplex (By
CC similarity). {ECO:0000250|UniProtKB:Q9UGN5,
CC ECO:0000269|PubMed:10364231}.
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:Q9UGN5};
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:Q9UGN5};
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:Q9UGN5};
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:Q9UGN5};
CC -!- SUBUNIT: Component of a base excision repair (BER) complex, containing
CC at least XRCC1, PARP1, POLB and LRIG3 (PubMed:11948190). Interacts (via
CC the PARP catalytic domain) with HPF1 (By similarity). Interacts with
CC core nucleosomes. Homo- and heterodimer with PARP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UGN5, ECO:0000269|PubMed:11948190}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10364231}. Chromosome
CC {ECO:0000250|UniProtKB:Q9UGN5}. Note=Recruited to DNA damage sites.
CC {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- TISSUE SPECIFICITY: Widely expressed; the highest levels were in testis
CC followed by ovary (PubMed:11133988). Expression is correlated with
CC proliferation, with higher levels occurring during early fetal
CC development and organogenesis and in the highly proliferative cell
CC compartments of adult (PubMed:11948190). {ECO:0000269|PubMed:11133988,
CC ECO:0000269|PubMed:11948190}.
CC -!- DEVELOPMENTAL STAGE: At stage 12.5 dpc, expressed at high level in the
CC developing liver and kidneys (PubMed:11948190). At 18.5 dpc,
CC preferentially expressed in the thymus and in regions of the nervous
CC system (PubMed:11948190). Within the developing trunk, preferential
CC expression persisted in the liver and became restricted to the cortical
CC region of the kidney, spleen, adrenal gland, and to stomach and
CC intestinal epithelia (PubMed:11948190). From 14.5 dpc to 18.5 dpc, as
CC well as in the adult, expressed at the highest level in thymus
CC (PubMed:11948190). Expression is particularly high in the subcapsular
CC zone of the thymus where immature lymphocytes proliferate
CC (PubMed:11948190). {ECO:0000269|PubMed:11948190}.
CC -!- INDUCTION: By high levels of DNA-damaging agents.
CC {ECO:0000269|PubMed:10364231}.
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 PARP2 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 PARP2 that signal the recognition of a DNA break
CC to the catalytic domain of PARP2, promoting HPF1 recruitment and
CC subsequent activation of PARP2, licensing serine ADP-ribosylation of
CC target proteins. {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- PTM: Auto poly-ADP-ribosylated on serine residues, leading to
CC dissociation of the PARP2-HPF1 complex from chromatin (By similarity).
CC Poly-ADP-ribosylated by PARP1 (PubMed:11948190).
CC {ECO:0000250|UniProtKB:Q9UGN5, ECO:0000269|PubMed:11948190}.
CC -!- PTM: Acetylation reduces DNA binding and enzymatic activity.
CC {ECO:0000269|PubMed:18436469}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in normal conditions, but
CC mutant mice are sensitive to ionizing radiation (PubMed:12727891).
CC Following alkylating agent treatment, cells show increased post-
CC replicative genomic instability, G2/M accumulation and chromosome
CC missegregation accompanying kinetochore defects (PubMed:12727891). Mice
CC lacking both Parp1 and Parp2 are not viable and die at the onset of
CC gastrulation (PubMed:12727891). {ECO:0000269|PubMed:12727891}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC25415.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ007780; CAA07679.1; -; mRNA.
DR EMBL; AF191547; AAK13253.1; -; Genomic_DNA.
DR EMBL; BC062150; AAH62150.1; -; mRNA.
DR EMBL; AF072521; AAC25415.1; ALT_INIT; mRNA.
DR CCDS; CCDS27025.1; -.
DR RefSeq; NP_033762.1; NM_009632.2.
DR RefSeq; XP_006518505.1; XM_006518442.3.
DR PDB; 1GS0; X-ray; 2.80 A; A/B=207-557.
DR PDBsum; 1GS0; -.
DR AlphaFoldDB; O88554; -.
DR SMR; O88554; -.
DR BioGRID; 197999; 10.
DR IntAct; O88554; 1.
DR MINT; O88554; -.
DR STRING; 10090.ENSMUSP00000048877; -.
DR BindingDB; O88554; -.
DR ChEMBL; CHEMBL2794; -.
DR iPTMnet; O88554; -.
DR PhosphoSitePlus; O88554; -.
DR EPD; O88554; -.
DR MaxQB; O88554; -.
DR PaxDb; O88554; -.
DR PeptideAtlas; O88554; -.
DR PRIDE; O88554; -.
DR ProteomicsDB; 294329; -.
DR Antibodypedia; 4794; 312 antibodies from 38 providers.
DR DNASU; 11546; -.
DR Ensembl; ENSMUST00000036126; ENSMUSP00000048877; ENSMUSG00000036023.
DR GeneID; 11546; -.
DR KEGG; mmu:11546; -.
DR UCSC; uc007tlq.1; mouse.
DR CTD; 10038; -.
DR MGI; MGI:1341112; Parp2.
DR VEuPathDB; HostDB:ENSMUSG00000036023; -.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000158452; -.
DR HOGENOM; CLU_004841_2_2_1; -.
DR InParanoid; O88554; -.
DR OMA; SANYCCP; -.
DR OrthoDB; 909382at2759; -.
DR PhylomeDB; O88554; -.
DR TreeFam; TF315407; -.
DR Reactome; R-MMU-110362; POLB-Dependent Long Patch Base Excision Repair.
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 BioGRID-ORCS; 11546; 4 hits in 110 CRISPR screens.
DR ChiTaRS; Parp2; mouse.
DR EvolutionaryTrace; O88554; -.
DR PRO; PR:O88554; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O88554; protein.
DR Bgee; ENSMUSG00000036023; Expressed in embryonic post-anal tail and 264 other tissues.
DR ExpressionAtlas; O88554; baseline and differential.
DR Genevisible; O88554; MM.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140294; F:NAD DNA ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:MGI.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; IMP:MGI.
DR GO; GO:0030592; P:DNA ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:MGI.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0016570; P:histone modification; ISS:UniProtKB.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISO:MGI.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; ISS:UniProtKB.
DR Gene3D; 1.20.142.10; -; 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 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Chromosome; DNA damage;
KW DNA repair; DNA-binding; Glycosyltransferase; NAD; Nucleotidyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..559
FT /note="Poly [ADP-ribose] polymerase 2"
FT /id="PRO_0000211328"
FT DOMAIN 84..181
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 207..324
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 332..559
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 19..20
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT MOTIF 33..39
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT COMPBIAS 10..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 534
FT /note="For poly [ADP-ribose] polymerase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 404..406
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 413
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 420
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 446
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT MOD_RES 36
FT /note="N6-(ADP-ribosyl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:18436469"
FT MOD_RES 36
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:18436469"
FT MOD_RES 37
FT /note="N6-(ADP-ribosyl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:18436469"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:18436469"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT MUTAGEN 36
FT /note="K->R: Decreases levels of mono-ADP-ribosylation
FT without loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:18436469"
FT MUTAGEN 37
FT /note="K->R: Decreases levels of mono-ADP-ribosylation
FT without loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:18436469"
FT CONFLICT 82
FT /note="L -> V (in Ref. 2; AAK13253)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="V -> I (in Ref. 2; AAK13253)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="R -> Q (in Ref. 2; AAK13253)"
FT /evidence="ECO:0000305"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:1GS0"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 248..266
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 300..320
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 333..340
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 353..364
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 372..385
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 399..406
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 458..467
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 534..538
FT /evidence="ECO:0007829|PDB:1GS0"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:1GS0"
FT STRAND 543..555
FT /evidence="ECO:0007829|PDB:1GS0"
SQ 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
