DPOLN_HUMAN
ID DPOLN_HUMAN Reviewed; 900 AA.
AC Q7Z5Q5; A2A336; B4E158; Q4TTW4; Q6ZNF4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=DNA polymerase nu;
DE EC=2.7.7.7 {ECO:0000269|PubMed:12794064, ECO:0000269|PubMed:16787914};
GN Name=POLN;
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] (ISOFORM 1), CATALYTIC ACTIVITY, VARIANT
RP HIS-121, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF ASP-623.
RX PubMed=12794064; DOI=10.1074/jbc.m305646200;
RA Marini F., Kim N., Schuffert A., Wood R.D.;
RT "POLN, a nuclear PolA family DNA polymerase homologous to the DNA cross-
RT link sensitivity protein Mus308.";
RL J. Biol. Chem. 278:32014-32019(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP CYS-425.
RC TISSUE=Brain, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-121; GLY-201; LEU-310;
RP SER-315; SER-336; CYS-425; GLY-502 AND LEU-711.
RG NIEHS SNPs program;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF ASP-623.
RX PubMed=16787914; DOI=10.1074/jbc.m604317200;
RA Takata K., Shimizu T., Iwai S., Wood R.D.;
RT "Human DNA polymerase N (POLN) is a low fidelity enzyme capable of error-
RT free bypass of 5S-thymine glycol.";
RL J. Biol. Chem. 281:23445-23455(2006).
RN [7]
RP FUNCTION.
RX PubMed=17118716; DOI=10.1016/j.dnarep.2006.09.012;
RA Arana M.E., Takata K., Garcia-Diaz M., Wood R.D., Kunkel T.A.;
RT "A unique error signature for human DNA polymerase nu.";
RL DNA Repair 6:213-223(2007).
RN [8]
RP FUNCTION.
RX PubMed=19908865; DOI=10.1021/bi9015346;
RA Zietlow L., Smith L.A., Bessho M., Bessho T.;
RT "Evidence for the involvement of human DNA polymerase N in the repair of
RT DNA interstrand cross-links.";
RL Biochemistry 48:11817-11824(2009).
RN [9]
RP FUNCTION.
RX PubMed=20102227; DOI=10.1021/tx900449u;
RA Yamanaka K., Minko I.G., Takata K., Kolbanovskiy A., Kozekov I.D.,
RA Wood R.D., Rizzo C.J., Lloyd R.S.;
RT "Novel enzymatic function of DNA polymerase nu in translesion DNA synthesis
RT past major groove DNA-peptide and DNA-DNA cross-links.";
RL Chem. Res. Toxicol. 23:689-695(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH FANCD2; FANCI; PCNA; RAD51 AND HELQ.
RX PubMed=19995904; DOI=10.1128/mcb.01124-09;
RA Moldovan G.L., Madhavan M.V., Mirchandani K.D., McCaffrey R.M.,
RA Vinciguerra P., D'Andrea A.D.;
RT "DNA polymerase POLN participates in cross-link repair and homologous
RT recombination.";
RL Mol. Cell. Biol. 30:1088-1096(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 194-859, AND MUTAGENESIS OF
RP GLU-675 AND LYS-679.
RX PubMed=25775266; DOI=10.1038/nsmb.2985;
RA Lee Y.S., Gao Y., Yang W.;
RT "How a homolog of high-fidelity replicases conducts mutagenic DNA
RT synthesis.";
RL Nat. Struct. Mol. Biol. 22:298-303(2015).
CC -!- FUNCTION: DNA polymerase with very low fidelity that catalyzes
CC considerable misincorporation by inserting dTTP opposite a G template,
CC and dGTP opposite a T template (PubMed:16787914, PubMed:17118716). Is
CC the least accurate of the DNA polymerase A family (i.e. POLG, POLN and
CC POLQ) (PubMed:17118716). Can perform accurate translesion DNA synthesis
CC (TLS) past a 5S-thymine glycol. Can perform efficient strand
CC displacement past a nick or a gap and gives rise to an amount of
CC product similar to that on non-damaged template. Has no exonuclease
CC activity (PubMed:16787914). Error-prone DNA polymerase that
CC preferentially misincorporates dT regardless of template sequence
CC (PubMed:25775266). May play a role in TLS during interstrand cross-link
CC (ICL) repair (PubMed:19908865). May be involved in TLS when genomic
CC replication is blocked by extremely large major groove DNA lesions. May
CC function in the bypass of some DNA-protein and DNA-DNA cross-links. May
CC have a role in cellular tolerance to DNA cross-linking agents
CC (PubMed:20102227). Involved in the repair of DNA cross-links and
CC double-strand break (DSB) resistance. Participates in FANCD2-mediated
CC repair. Forms a complex with HELQ helicase that participates in
CC homologous recombination (HR) repair and is essential for cellular
CC protection against DNA cross-links (PubMed:19995904).
CC {ECO:0000269|PubMed:16787914, ECO:0000269|PubMed:17118716,
CC ECO:0000269|PubMed:19908865, ECO:0000269|PubMed:19995904,
CC ECO:0000269|PubMed:20102227, ECO:0000269|PubMed:25775266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000269|PubMed:12794064, ECO:0000269|PubMed:16787914};
CC -!- ACTIVITY REGULATION: Inhibited by ddTTP. {ECO:0000269|PubMed:16787914}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.0 uM for dATP:T {ECO:0000269|PubMed:16787914};
CC KM=8.2 uM for dCTP:G {ECO:0000269|PubMed:16787914};
CC KM=7.7 uM for dGTP:C {ECO:0000269|PubMed:16787914};
CC KM=7.3 uM for dTTP:A {ECO:0000269|PubMed:16787914};
CC pH dependence:
CC Optimum pH is 8.8. {ECO:0000269|PubMed:16787914};
CC -!- SUBUNIT: Interacts with FANCD2, FANCI, PCNA, RAD51 and HELQ.
CC {ECO:0000269|PubMed:19995904}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12794064}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z5Q5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z5Q5-3; Sequence=VSP_054402, VSP_054403;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and heart. Weakly
CC expressed in skeletal muscle. {ECO:0000269|PubMed:12794064}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD18421.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/poln/";
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DR EMBL; AY136549; AAN52116.1; -; mRNA.
DR EMBL; AK131239; BAD18421.1; ALT_SEQ; mRNA.
DR EMBL; AK303673; BAG64670.1; -; mRNA.
DR EMBL; DQ060036; AAY43130.1; -; Genomic_DNA.
DR EMBL; AL136360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471131; EAW82539.1; -; Genomic_DNA.
DR CCDS; CCDS3360.1; -. [Q7Z5Q5-1]
DR RefSeq; NP_861524.2; NM_181808.3. [Q7Z5Q5-1]
DR PDB; 4XVI; X-ray; 3.10 A; A=194-859.
DR PDB; 4XVK; X-ray; 2.95 A; A=194-859.
DR PDB; 4XVL; X-ray; 3.30 A; A=194-859.
DR PDB; 4XVM; X-ray; 3.20 A; A=194-859.
DR PDBsum; 4XVI; -.
DR PDBsum; 4XVK; -.
DR PDBsum; 4XVL; -.
DR PDBsum; 4XVM; -.
DR AlphaFoldDB; Q7Z5Q5; -.
DR SMR; Q7Z5Q5; -.
DR BioGRID; 131695; 31.
DR STRING; 9606.ENSP00000435506; -.
DR BindingDB; Q7Z5Q5; -.
DR ChEMBL; CHEMBL2010628; -.
DR iPTMnet; Q7Z5Q5; -.
DR PhosphoSitePlus; Q7Z5Q5; -.
DR BioMuta; POLN; -.
DR DMDM; 90101282; -.
DR MassIVE; Q7Z5Q5; -.
DR PaxDb; Q7Z5Q5; -.
DR PeptideAtlas; Q7Z5Q5; -.
DR PRIDE; Q7Z5Q5; -.
DR ProteomicsDB; 69348; -. [Q7Z5Q5-1]
DR Antibodypedia; 22333; 70 antibodies from 16 providers.
DR DNASU; 353497; -.
DR Ensembl; ENST00000382865.5; ENSP00000372316.1; ENSG00000130997.16. [Q7Z5Q5-1]
DR Ensembl; ENST00000511885.6; ENSP00000435506.1; ENSG00000130997.16. [Q7Z5Q5-1]
DR GeneID; 353497; -.
DR KEGG; hsa:353497; -.
DR MANE-Select; ENST00000511885.6; ENSP00000435506.1; NM_181808.4; NP_861524.2.
DR UCSC; uc003ger.3; human. [Q7Z5Q5-1]
DR CTD; 353497; -.
DR DisGeNET; 353497; -.
DR GeneCards; POLN; -.
DR HGNC; HGNC:18870; POLN.
DR HPA; ENSG00000130997; Tissue enhanced (adipose tissue, testis).
DR MIM; 610887; gene.
DR neXtProt; NX_Q7Z5Q5; -.
DR OpenTargets; ENSG00000130997; -.
DR PharmGKB; PA134979866; -.
DR VEuPathDB; HostDB:ENSG00000130997; -.
DR eggNOG; KOG0950; Eukaryota.
DR GeneTree; ENSGT00940000159015; -.
DR HOGENOM; CLU_015708_0_0_1; -.
DR InParanoid; Q7Z5Q5; -.
DR OMA; NDPCIYI; -.
DR OrthoDB; 931773at2759; -.
DR PhylomeDB; Q7Z5Q5; -.
DR TreeFam; TF337202; -.
DR PathwayCommons; Q7Z5Q5; -.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR SignaLink; Q7Z5Q5; -.
DR BioGRID-ORCS; 353497; 8 hits in 1079 CRISPR screens.
DR ChiTaRS; POLN; human.
DR GeneWiki; DNA_polymerase_nu; -.
DR GenomeRNAi; 353497; -.
DR Pharos; Q7Z5Q5; Tbio.
DR PRO; PR:Q7Z5Q5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q7Z5Q5; protein.
DR Bgee; ENSG00000130997; Expressed in caudate nucleus and 99 other tissues.
DR ExpressionAtlas; Q7Z5Q5; baseline and differential.
DR Genevisible; Q7Z5Q5; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB.
DR GO; GO:0019985; P:translesion synthesis; IDA:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR040940; DNA_pol_P_Exo.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF18049; DNA_pol_P_Exo; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA repair;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..900
FT /note="DNA polymerase nu"
FT /id="PRO_0000227938"
FT REGION 60..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 578..610
FT /note="NIQGISKHPIQITTPKNFKGKEDKILTISPRAM -> ICARQVASDFQKCVE
FT VSDAMMNSSIFWWLLKLY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054402"
FT VAR_SEQ 611..899
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054403"
FT VARIANT 121
FT /note="Q -> H (in dbSNP:rs2353552)"
FT /evidence="ECO:0000269|PubMed:12794064, ECO:0000269|Ref.3"
FT /id="VAR_025647"
FT VARIANT 201
FT /note="R -> G (in dbSNP:rs35884361)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025648"
FT VARIANT 310
FT /note="M -> L (in dbSNP:rs10018786)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025649"
FT VARIANT 315
FT /note="P -> S (in dbSNP:rs11725880)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025650"
FT VARIANT 336
FT /note="G -> S (in dbSNP:rs10011549)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025651"
FT VARIANT 425
FT /note="R -> C (in dbSNP:rs9328764)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3"
FT /id="VAR_025652"
FT VARIANT 502
FT /note="S -> G (in dbSNP:rs34574483)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025653"
FT VARIANT 711
FT /note="F -> L (in dbSNP:rs34554757)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025654"
FT MUTAGEN 623
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:12794064,
FT ECO:0000269|PubMed:16787914"
FT MUTAGEN 675
FT /note="E->R: Reduces polymerase activity. No effect on
FT accuracy."
FT /evidence="ECO:0000269|PubMed:25775266"
FT MUTAGEN 679
FT /note="K->A: No effect on polymerase activity. Increases
FT accuracy by ten-fold."
FT /evidence="ECO:0000269|PubMed:25775266"
FT CONFLICT 8
FT /note="V -> A (in Ref. 2; BAG64670)"
FT /evidence="ECO:0000305"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:4XVM"
FT HELIX 205..217
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:4XVK"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:4XVM"
FT STRAND 244..253
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 293..311
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 349..356
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:4XVL"
FT HELIX 365..372
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 390..417
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 421..426
FT /evidence="ECO:0007829|PDB:4XVK"
FT TURN 427..430
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 431..440
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 447..472
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 481..488
FT /evidence="ECO:0007829|PDB:4XVK"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:4XVI"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:4XVI"
FT HELIX 516..521
FT /evidence="ECO:0007829|PDB:4XVK"
FT TURN 522..525
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 528..545
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 547..550
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 573..577
FT /evidence="ECO:0007829|PDB:4XVK"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:4XVM"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 607..610
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 618..624
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 627..636
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 639..643
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 654..662
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:4XVM"
FT HELIX 671..685
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 690..696
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 701..714
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 717..732
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 733..736
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:4XVL"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 746..749
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 753..788
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 796..801
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 804..809
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 811..813
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 814..826
FT /evidence="ECO:0007829|PDB:4XVK"
FT HELIX 827..829
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 832..834
FT /evidence="ECO:0007829|PDB:4XVK"
FT STRAND 844..853
FT /evidence="ECO:0007829|PDB:4XVK"
SQ SEQUENCE 900 AA; 100307 MW; D44758D71BCD3F02 CRC64;
MENYEALVGF DLCNTPLSSV AQKIMSAMHS GDLVDSKTWG KSTETMEVIN KSSVKYSVQL
EDRKTQSPEK KDLKSLRSQT SRGSAKLSPQ SFSVRLTDQL SADQKQKSIS SLTLSSCLIP
QYNQEASVLQ KKGHKRKHFL MENINNENKG SINLKRKHIT YNNLSEKTSK QMALEEDTDD
AEGYLNSGNS GALKKHFCDI RHLDDWAKSQ LIEMLKQAAA LVITVMYTDG STQLGADQTP
VSSVRGIVVL VKRQAEGGHG CPDAPACGPV LEGFVSDDPC IYIQIEHSAI WDQEQEAHQQ
FARNVLFQTM KCKCPVICFN AKDFVRIVLQ FFGNDGSWKH VADFIGLDPR IAAWLIDPSD
ATPSFEDLVE KYCEKSITVK VNSTYGNSSR NIVNQNVREN LKTLYRLTMD LCSKLKDYGL
WQLFRTLELP LIPILAVMES HAIQVNKEEM EKTSALLGAR LKELEQEAHF VAGERFLITS
NNQLREILFG KLKLHLLSQR NSLPRTGLQK YPSTSEAVLN ALRDLHPLPK IILEYRQVHK
IKSTFVDGLL ACMKKGSISS TWNQTGTVTG RLSAKHPNIQ GISKHPIQIT TPKNFKGKED
KILTISPRAM FVSSKGHTFL AADFSQIELR ILTHLSGDPE LLKLFQESER DDVFSTLTSQ
WKDVPVEQVT HADREQTKKV VYAVVYGAGK ERLAACLGVP IQEAAQFLES FLQKYKKIKD
FARAAIAQCH QTGCVVSIMG RRRPLPRIHA HDQQLRAQAE RQAVNFVVQG SAADLCKLAM
IHVFTAVAAS HTLTARLVAQ IHDELLFEVE DPQIPECAAL VRRTMESLEQ VQALELQLQV
PLKVSLSAGR SWGHLVPLQE AWGPPPGPCR TESPSNSLAA PGSPASTQPP PLHFSPSFCL
