DPOG2_HUMAN
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 03-AUG-2022, entry version 184.
DE RecName: Full=DNA polymerase subunit gamma-2, mitochondrial;
DE AltName: Full=DNA polymerase gamma accessory 55 kDa subunit;
DE Short=p55;
DE AltName: Full=Mitochondrial DNA polymerase accessory subunit;
DE AltName: Full=MtPolB;
DE AltName: Full=PolG-beta;
DE Flags: Precursor;
GN Name=POLG2; 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 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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: Mitochondrial polymerase processivity subunit. It regulates
CC the polymerase and exonuclease activities promoting processive DNA
CC synthesis. Binds to ss-DNA. {ECO:0000269|PubMed:30157269,
CC ECO:0000269|PubMed:31778857}.
CC -!- SUBUNIT: Heterotrimer composed of a catalytic subunit and a homodimer
CC of accessory subunits.
CC -!- INTERACTION:
CC Q9UHN1; P54098: POLG; NbExp=11; IntAct=EBI-852642, EBI-852624;
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
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.
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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 PDBsum; 2G4C; -.
DR PDBsum; 3IKL; -.
DR PDBsum; 3IKM; -.
DR PDBsum; 4ZTU; -.
DR PDBsum; 4ZTZ; -.
DR PDBsum; 5C51; -.
DR PDBsum; 5C52; -.
DR PDBsum; 5C53; -.
DR AlphaFoldDB; Q9UHN1; -.
DR SMR; Q9UHN1; -.
DR BioGRID; 116398; 30.
DR ComplexPortal; CPX-2093; Mitochondrial DNA polymerase gamma complex.
DR IntAct; Q9UHN1; 14.
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; Q9UHN1; -.
DR PeptideAtlas; Q9UHN1; -.
DR PRIDE; Q9UHN1; -.
DR ProteomicsDB; 84382; -.
DR Antibodypedia; 50586; 172 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 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; AFREHIF; -.
DR OrthoDB; 1183820at2759; -.
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; 297 hits in 1085 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 175 other tissues.
DR ExpressionAtlas; Q9UHN1; baseline and differential.
DR Genevisible; Q9UHN1; HS.
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:0006281; P:DNA repair; IEA:InterPro.
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:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
DR CDD; cd02426; Pol_gamma_b_Cterm; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR027030; POLG2.
DR InterPro; IPR042064; POLG2_C.
DR PANTHER; PTHR10745; PTHR10745; 1.
DR PANTHER; PTHR10745:SF8; PTHR10745:SF8; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; DNA replication; DNA-binding; Mitochondrion;
KW 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, mitochondrial"
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 60..66
FT /evidence="ECO:0007829|PDB:3IKM"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3IKM"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:3IKL"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:2G4C"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2G4C"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2G4C"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:3IKM"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:3IKM"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2G4C"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:2G4C"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2G4C"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2G4C"
FT TURN 161..165
FT /evidence="ECO:0007829|PDB:2G4C"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2G4C"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:2G4C"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2G4C"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:3IKL"
FT TURN 193..197
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 203..215
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:3IKM"
FT STRAND 233..243
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 248..266
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 342..351
FT /evidence="ECO:0007829|PDB:3IKL"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:3IKM"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:3IKM"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:3IKM"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 395..408
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:2G4C"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:3IKL"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:2G4C"
FT STRAND 450..457
FT /evidence="ECO:0007829|PDB:3IKL"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:3IKL"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:3IKM"
FT HELIX 470..484
FT /evidence="ECO:0007829|PDB:3IKL"
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
