ID DPOG2_HUMAN Reviewed; 485 AA. AC Q9UHN1; O00419; Q0IJ81; Q96GW2; Q9UK35; Q9UK94; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 193. DE RecName: Full=DNA polymerase subunit gamma-2; DE AltName: Full=DNA polymerase gamma accessory 55 kDa subunit; DE Short=p55 {ECO:0000303|PubMed:10608893}; DE AltName: Full=Mitochondrial DNA polymerase accessory subunit; DE AltName: Full=MtPolB; DE AltName: Full=PolG-beta; DE Flags: Precursor; GN Name=POLG2 {ECO:0000303|PubMed:30157269, ECO:0000312|HGNC:HGNC:9180}; GN Synonyms=MTPOLB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cerebellum; RX PubMed=10608893; DOI=10.1074/jbc.274.53.38197; RA Lim S.E., Longley M.J., Copeland W.C.; RT "The mitochondrial p55 accessory subunit of human DNA polymerase gamma RT enhances DNA binding, promotes processive DNA synthesis, and confers N- RT ethylmaleimide resistance."; RL J. Biol. Chem. 274:38197-38203(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-169. RX PubMed=10666468; DOI=10.1093/nar/28.5.1237; RA Carrodeguas J.A., Bogenhagen D.F.; RT "Protein sequences conserved in prokaryotic aminoacyl-tRNA synthetases are RT important for the activity of the processivity factor of human RT mitochondrial DNA polymerase."; RL Nucleic Acids Res. 28:1237-1244(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10677218; DOI=10.1021/bi992104w; RA Johnson A.A., Tsai Y.-C., Graves S.W., Johnson K.A.; RT "Human mitochondrial DNA polymerase holoenzyme: reconstitution and RT characterization."; RL Biochemistry 39:1702-1708(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-169 AND ALA-416. RC TISSUE=Cervix, and Ovary; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 114-485. RX PubMed=9153213; DOI=10.1074/jbc.272.21.13640; RA Wang Y., Farr C.L., Kaguni L.S.; RT "Accessory subunit of mitochondrial DNA polymerase from Drosophila embryos. RT Cloning, molecular analysis, and association in the native enzyme."; RL J. Biol. Chem. 272:13640-13646(1997). RN [6] RP FUNCTION, AND SUBUNIT. RX PubMed=11477093; DOI=10.1074/jbc.m106045200; RA Johnson A.A., Johnson K.A.; RT "Fidelity of nucleotide incorporation by human mitochondrial DNA RT polymerase."; RL J. Biol. Chem. 276:38090-38096(2001). RN [7] RP FUNCTION, AND SUBUNIT. RX PubMed=11477094; DOI=10.1074/jbc.m106046200; RA Johnson A.A., Johnson K.A.; RT "Exonuclease proofreading by human mitochondrial DNA polymerase."; RL J. Biol. Chem. 276:38097-38107(2001). RN [8] RP FUNCTION, AND SUBUNIT. RX PubMed=11504725; DOI=10.1074/jbc.m105230200; RA Longley M.J., Nguyen D., Kunkel T.A., Copeland W.C.; RT "The fidelity of human DNA polymerase gamma with and without exonucleolytic RT proofreading and the p55 accessory subunit."; RL J. Biol. Chem. 276:38555-38562(2001). RN [9] RP FUNCTION, AND SUBUNIT. RX PubMed=15167897; DOI=10.1038/sj.emboj.7600257; RA Korhonen J.A., Pham X.H., Pellegrini M., Falkenberg M.; RT "Reconstitution of a minimal mtDNA replisome in vitro."; RL EMBO J. 23:2423-2429(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [12] RP FUNCTION, AND CHARACTERIZATION OF VARIANT MTDPS16 TRP-182. RX PubMed=30157269; DOI=10.1371/journal.pone.0203198; RA Hoff K.E., DeBalsi K.L., Sanchez-Quintero M.J., Longley M.J., Hirano M., RA Naini A.B., Copeland W.C.; RT "Characterization of the human homozygous R182W POLG2 mutation in RT mitochondrial DNA depletion syndrome."; RL PLoS ONE 13:e0203198-e0203198(2018). RN [13] RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-146 AND 181-485, FUNCTION, AND RP SUBUNIT. RX PubMed=19837034; DOI=10.1016/j.cell.2009.07.050; RA Lee Y.S., Kennedy W.D., Yin Y.W.; RT "Structural insight into processive human mitochondrial DNA synthesis and RT disease-related polymerase mutations."; RL Cell 139:312-324(2009). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 26-485, FUNCTION, AND SUBUNIT. RX PubMed=26056153; DOI=10.15252/embj.201591520; RA Szymanski M.R., Kuznetsov V.B., Shumate C., Meng Q., Lee Y.S., Patel G., RA Patel S., Yin Y.W.; RT "Structural basis for processivity and antiviral drug toxicity in human RT mitochondrial DNA replicase."; RL EMBO J. 34:1959-1970(2015). RN [15] RP STRUCTURE BY ELECTRON MICROSCOPY (2.46 ANGSTROMS), FUNCTION, AND SUBUNIT. RX PubMed=37202477; DOI=10.1038/s41594-023-00980-2; RA Park J., Herrmann G.K., Mitchell P.G., Sherman M.B., Yin Y.W.; RT "Polgamma coordinates DNA synthesis and proofreading to ensure RT mitochondrial genome integrity."; RL Nat. Struct. Mol. Biol. 30:812-823(2023). RN [16] RP VARIANT PEOA4 GLU-451, AND CHARACTERIZATION OF VARIANT PEOA4 GLU-451. RX PubMed=16685652; DOI=10.1086/504303; RA Longley M.J., Clark S., Man C.Y.W., Hudson G., Durham S.E., Taylor R.W., RA Nightingale S., Turnbull D.M., Copeland W.C., Chinnery P.F.; RT "Mutant POLG2 disrupts DNA polymerase gamma subunits and causes progressive RT external ophthalmoplegia."; RL Am. J. Hum. Genet. 78:1026-1034(2006). RN [17] RP VARIANT ALA-416, AND CHARACTERIZATION OF VARIANT ALA-416. RX PubMed=18195150; DOI=10.1001/archneurol.2007.9; RA Ferraris S., Clark S., Garelli E., Davidzon G., Moore S.A., Kardon R.H., RA Bienstock R.J., Longley M.J., Mancuso M., Gutierrez Rios P., Hirano M., RA Copeland W.C., DiMauro S.; RT "Progressive external ophthalmoplegia and vision and hearing loss in a RT patient with mutations in POLG2 and OPA1."; RL Arch. Neurol. 65:125-131(2008). RN [18] RP VARIANT MTDPS16 TRP-182, AND INVOLVEMENT IN MTDPS16. RX PubMed=27592148; DOI=10.1016/j.ejmg.2016.08.012; RA Varma H., Faust P.L., Iglesias A.D., Lagana S.M., Wou K., Hirano M., RA DiMauro S., Mansukani M.M., Hoff K.E., Nagy P.L., Copeland W.C., RA Naini A.B.; RT "Whole exome sequencing identifies a homozygous POLG2 missense variant in RT an infant with fulminant hepatic failure and mitochondrial DNA depletion."; RL Eur. J. Med. Genet. 59:540-545(2016). RN [19] RP VARIANT MTDPS16B TYR-433, INVOLVEMENT IN MTDPS16B, CHARACTERIZATION OF RP VARIANT MTDPS16B TYR-433, AND FUNCTION. RX PubMed=31778857; DOI=10.1016/j.ejmg.2019.103821; RA Dosekova P., Dubiel A., Karlowicz A., Zietkiewicz S., Rydzanicz M., RA Habalova V., Pienkowski V.M., Skirkova M., Han V., Mosejova A., RA Gdovinova Z., Kaliszewska M., Tonska K., Szymanski M.R., Skorvanek M., RA Ploski R.; RT "Whole exome sequencing identifies a homozygous POLG2 missense variant in RT an adult patient presenting with optic atrophy, movement disorders, RT premature ovarian failure and mitochondrial DNA depletion."; RL Eur. J. Med. Genet. 63:103821-103821(2020). CC -!- FUNCTION: Accessory subunit of DNA polymerase gamma solely responsible CC for replication of mitochondrial DNA (mtDNA). Acts as an allosteric CC regulator of the holoenzyme activities. Enhances the polymerase CC activity and the processivity of POLG by increasing its interactions CC with the DNA template. Suppresses POLG exonucleolytic proofreading CC especially toward homopolymeric templates bearing mismatched termini. CC Binds to single-stranded DNA. {ECO:0000269|PubMed:11477093, CC ECO:0000269|PubMed:11477094, ECO:0000269|PubMed:11504725, CC ECO:0000269|PubMed:15167897, ECO:0000269|PubMed:19837034, CC ECO:0000269|PubMed:26056153, ECO:0000269|PubMed:30157269, CC ECO:0000269|PubMed:31778857, ECO:0000269|PubMed:37202477}. CC -!- SUBUNIT: Heterotrimer composed of a catalytic subunit and a homodimer CC of accessory subunits (POLG:POLG2). {ECO:0000269|PubMed:11477093, CC ECO:0000269|PubMed:11477094, ECO:0000269|PubMed:11504725, CC ECO:0000269|PubMed:15167897, ECO:0000269|PubMed:19837034, CC ECO:0000269|PubMed:26056153, ECO:0000269|PubMed:37202477}. CC -!- INTERACTION: CC Q9UHN1; P54098: POLG; NbExp=11; IntAct=EBI-852642, EBI-852624; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P54098}. CC Mitochondrion matrix, mitochondrion nucleoid CC {ECO:0000250|UniProtKB:P54098}. CC -!- DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA CC deletions, autosomal dominant, 4 (PEOA4) [MIM:610131]: A disorder CC characterized by progressive weakness of ocular muscles and levator CC muscle of the upper eyelid. In a minority of cases, it is associated CC with skeletal myopathy, which predominantly involves axial or proximal CC muscles and which causes abnormal fatigability and even permanent CC muscle weakness. Ragged-red fibers and atrophy are found on muscle CC biopsy. A large proportion of chronic ophthalmoplegias are associated CC with other symptoms, leading to a multisystemic pattern of this CC disease. Additional symptoms are variable, and may include cataracts, CC hearing loss, sensory axonal neuropathy, ataxia, depression, CC hypogonadism, and parkinsonism. {ECO:0000269|PubMed:16685652}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Mitochondrial DNA depletion syndrome 16, hepatic type CC (MTDPS16) [MIM:618528]: An autosomal recessive disorder characterized CC by poor feeding, difficulty breathing, abdominal distention, an CC abnormal carnitine profile, metabolic acidosis and hepatic failure in CC the neonatal period. Severe mtDNA depletion is observed in liver and CC muscle biopsies. {ECO:0000269|PubMed:27592148, CC ECO:0000269|PubMed:30157269}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Mitochondrial DNA depletion syndrome 16B, neuroophthalmic type CC (MTDPS16B) [MIM:619425]: An autosomal recessive disorder characterized CC by childhood onset of progressive neuroophthalmic manifestations with CC optic atrophy, mixed polyneuropathy, spinal and cerebellar ataxia, and CC generalized chorea associated with mtDNA depletion. CC {ECO:0000269|PubMed:31778857}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; AF142992; AAD50382.1; -; mRNA. DR EMBL; AF177201; AAD56640.1; -; mRNA. DR EMBL; AF184344; AAD56542.1; -; mRNA. DR EMBL; BC000913; AAH00913.2; -; mRNA. DR EMBL; BC009194; AAH09194.1; -; mRNA. DR EMBL; U94703; AAC51321.1; -; mRNA. DR CCDS; CCDS32706.1; -. DR RefSeq; NP_009146.2; NM_007215.3. DR PDB; 2G4C; X-ray; 3.15 A; A/B/C/D=26-485. DR PDB; 3IKL; X-ray; 3.10 A; A/B=1-146, A/B=181-485. DR PDB; 3IKM; X-ray; 3.24 A; B/C/E/F=59-485. DR PDB; 4ZTU; X-ray; 3.30 A; B/C=26-485. DR PDB; 4ZTZ; X-ray; 3.44 A; B/C=26-485. DR PDB; 5C51; X-ray; 3.43 A; B/C=1-485. DR PDB; 5C52; X-ray; 3.64 A; B/C=1-485. DR PDB; 5C53; X-ray; 3.57 A; B/C=1-485. DR PDB; 8D33; EM; 2.46 A; B/C=1-485. DR PDB; 8D37; EM; 2.65 A; B/C=1-485. DR PDB; 8D3R; EM; 3.04 A; B/C=1-485. DR PDB; 8D42; EM; 2.91 A; B/C=1-485. DR PDBsum; 2G4C; -. DR PDBsum; 3IKL; -. DR PDBsum; 3IKM; -. DR PDBsum; 4ZTU; -. DR PDBsum; 4ZTZ; -. DR PDBsum; 5C51; -. DR PDBsum; 5C52; -. DR PDBsum; 5C53; -. DR PDBsum; 8D33; -. DR PDBsum; 8D37; -. DR PDBsum; 8D3R; -. DR PDBsum; 8D42; -. DR AlphaFoldDB; Q9UHN1; -. DR EMDB; EMD-27163; -. DR EMDB; EMD-27172; -. DR SMR; Q9UHN1; -. DR BioGRID; 116398; 37. DR ComplexPortal; CPX-2093; Mitochondrial DNA polymerase gamma complex. DR IntAct; Q9UHN1; 15. DR MINT; Q9UHN1; -. DR STRING; 9606.ENSP00000442563; -. DR ChEMBL; CHEMBL3430903; -. DR iPTMnet; Q9UHN1; -. DR PhosphoSitePlus; Q9UHN1; -. DR BioMuta; POLG2; -. DR DMDM; 17367139; -. DR EPD; Q9UHN1; -. DR jPOST; Q9UHN1; -. DR MassIVE; Q9UHN1; -. DR MaxQB; Q9UHN1; -. DR PaxDb; 9606-ENSP00000442563; -. DR PeptideAtlas; Q9UHN1; -. DR ProteomicsDB; 84382; -. DR Pumba; Q9UHN1; -. DR Antibodypedia; 50586; 190 antibodies from 28 providers. DR DNASU; 11232; -. DR Ensembl; ENST00000539111.7; ENSP00000442563.2; ENSG00000256525.8. DR GeneID; 11232; -. DR KEGG; hsa:11232; -. DR MANE-Select; ENST00000539111.7; ENSP00000442563.2; NM_007215.4; NP_009146.2. DR UCSC; uc002jei.4; human. DR AGR; HGNC:9180; -. DR CTD; 11232; -. DR DisGeNET; 11232; -. DR GeneCards; POLG2; -. DR HGNC; HGNC:9180; POLG2. DR HPA; ENSG00000256525; Low tissue specificity. DR MalaCards; POLG2; -. DR MIM; 604983; gene. DR MIM; 610131; phenotype. DR MIM; 618528; phenotype. DR MIM; 619425; phenotype. DR neXtProt; NX_Q9UHN1; -. DR OpenTargets; ENSG00000256525; -. DR Orphanet; 254892; Autosomal dominant progressive external ophthalmoplegia. DR PharmGKB; PA33501; -. DR VEuPathDB; HostDB:ENSG00000256525; -. DR eggNOG; KOG2298; Eukaryota. DR GeneTree; ENSGT00940000153759; -. DR HOGENOM; CLU_055833_0_0_1; -. DR InParanoid; Q9UHN1; -. DR OMA; WGQEVLE; -. DR OrthoDB; 2901447at2759; -. DR PhylomeDB; Q9UHN1; -. DR TreeFam; TF103005; -. DR BRENDA; 2.7.7.7; 2681. DR PathwayCommons; Q9UHN1; -. DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis. DR SignaLink; Q9UHN1; -. DR SIGNOR; Q9UHN1; -. DR BioGRID-ORCS; 11232; 326 hits in 1164 CRISPR screens. DR ChiTaRS; POLG2; human. DR EvolutionaryTrace; Q9UHN1; -. DR GeneWiki; POLG2; -. DR GenomeRNAi; 11232; -. DR Pharos; Q9UHN1; Tbio. DR PRO; PR:Q9UHN1; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9UHN1; Protein. DR Bgee; ENSG00000256525; Expressed in secondary oocyte and 177 other cell types or tissues. DR ExpressionAtlas; Q9UHN1; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005760; C:gamma DNA polymerase complex; IDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; IDA:ComplexPortal. DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0070182; F:DNA polymerase binding; IPI:UniProtKB. DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IDA:UniProtKB. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:Ensembl. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0006264; P:mitochondrial DNA replication; IDA:ComplexPortal. DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:UniProtKB. DR CDD; cd02426; Pol_gamma_b_Cterm; 1. DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR036621; Anticodon-bd_dom_sf. DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2. DR InterPro; IPR042064; POLG2_C. DR PANTHER; PTHR10745:SF8; DNA POLYMERASE SUBUNIT GAMMA-2, MITOCHONDRIAL; 1. DR PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR Genevisible; Q9UHN1; HS. PE 1: Evidence at protein level; KW 3D-structure; Disease variant; DNA replication; DNA-binding; Mitochondrion; KW Mitochondrion nucleoid; Phosphoprotein; Primary mitochondrial disease; KW Progressive external ophthalmoplegia; Reference proteome; Transit peptide. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..485 FT /note="DNA polymerase subunit gamma-2" FT /id="PRO_0000007314" FT REGION 28..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..54 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 38 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VARIANT 169 FT /note="A -> T (in dbSNP:rs1427463)" FT /evidence="ECO:0000269|PubMed:10666468, FT ECO:0000269|PubMed:15489334" FT /id="VAR_032028" FT VARIANT 182 FT /note="R -> W (in MTDPS16; decreased function in FT mitochondrial DNA replication; decreased protein stability; FT no effect on DNA binding; dbSNP:rs886037843)" FT /evidence="ECO:0000269|PubMed:27592148, FT ECO:0000269|PubMed:30157269" FT /id="VAR_078773" FT VARIANT 416 FT /note="G -> A (no functional deficit; dbSNP:rs17850455)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:18195150" FT /id="VAR_032029" FT VARIANT 433 FT /note="D -> Y (in MTDPS16B; decreased DNA polymerase FT processivity factor activity; results in decreased FT stability; affects the secondary structure as shown by FT circular dichroism spectroscopy)" FT /evidence="ECO:0000269|PubMed:31778857" FT /id="VAR_086017" FT VARIANT 451 FT /note="G -> E (in PEOA4; affects stimulation of the FT catalytic subunit; dbSNP:rs104894632)" FT /evidence="ECO:0000269|PubMed:16685652" FT /id="VAR_029364" FT CONFLICT 114..124 FT /note="WWTSVVVFREQ -> MVDLGGGVHGA (in Ref. 5; AAC51321)" FT /evidence="ECO:0000305" FT CONFLICT 122 FT /note="R -> T (in Ref. 3; AAD56542)" FT /evidence="ECO:0000305" FT CONFLICT 136 FT /note="G -> S (in Ref. 3; AAD56542 and 5; AAC51321)" FT /evidence="ECO:0000305" FT CONFLICT 287..292 FT /note="NKLYYN -> TNFTTI (in Ref. 5; AAC51321)" FT /evidence="ECO:0000305" FT HELIX 65..75 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:3IKM" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 88..93 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 101..118 FT /evidence="ECO:0007829|PDB:8D33" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:8D33" FT TURN 135..137 FT /evidence="ECO:0007829|PDB:3IKM" FT STRAND 138..141 FT /evidence="ECO:0007829|PDB:3IKM" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:8D33" FT TURN 154..160 FT /evidence="ECO:0007829|PDB:8D33" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 166..177 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:2G4C" FT HELIX 186..190 FT /evidence="ECO:0007829|PDB:8D33" FT TURN 191..194 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:8D33" FT TURN 198..202 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 206..218 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:3IKM" FT STRAND 229..243 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 248..265 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 273..279 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 281..284 FT /evidence="ECO:0007829|PDB:3IKL" FT STRAND 285..293 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 296..307 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 309..314 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 319..322 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 324..326 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 329..331 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 334..341 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 342..354 FT /evidence="ECO:0007829|PDB:8D33" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:3IKM" FT HELIX 362..366 FT /evidence="ECO:0007829|PDB:8D33" FT TURN 376..378 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 380..387 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 392..408 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 416..418 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 419..421 FT /evidence="ECO:0007829|PDB:3IKL" FT HELIX 425..435 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 437..443 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 445..450 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 452..457 FT /evidence="ECO:0007829|PDB:8D33" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:8D33" FT STRAND 463..467 FT /evidence="ECO:0007829|PDB:8D33" FT HELIX 468..482 FT /evidence="ECO:0007829|PDB:8D33" SQ SEQUENCE 485 AA; 54911 MW; B99734BFEA249192 CRC64; MRSRVAVRAC HKVCRCLLSG FGGRVDAGQP ELLTERSSPK GGHVKSHAEL EGNGEHPEAP GSGEGSEALL EICQRRHFLS GSKQQLSRDS LLSGCHPGFG PLGVELRKNL AAEWWTSVVV FREQVFPVDA LHHKPGPLLP GDSAFRLVSA ETLREILQDK ELSKEQLVAF LENVLKTSGK LRENLLHGAL EHYVNCLDLV NKRLPYGLAQ IGVCFHPVFD TKQIRNGVKS IGEKTEASLV WFTPPRTSNQ WLDFWLRHRL QWWRKFAMSP SNFSSSDCQD EEGRKGNKLY YNFPWGKELI ETLWNLGDHE LLHMYPGNVS KLHGRDGRKN VVPCVLSVNG DLDRGMLAYL YDSFQLTENS FTRKKNLHRK VLKLHPCLAP IKVALDVGRG PTLELRQVCQ GLFNELLENG ISVWPGYLET MQSSLEQLYS KYDEMSILFT VLVTETTLEN GLIHLRSRDT TMKEMMHISK LKDFLIKYIS SAKNV //