DPOE2_HUMAN
ID DPOE2_HUMAN Reviewed; 527 AA.
AC P56282; A0AV55; A4FU92; A4LBB7; A6NH58; B4DDE6; O43560;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=DNA polymerase epsilon subunit 2;
DE AltName: Full=DNA polymerase II subunit 2;
DE AltName: Full=DNA polymerase epsilon subunit B;
GN Name=POLE2; Synonyms=DPE2;
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).
RX PubMed=9405441; DOI=10.1074/jbc.272.51.32337;
RA Li Y., Asahara H., Patel V.S., Zhou S., Linn S.;
RT "Purification, cDNA cloning, and gene mapping of the small subunit of human
RT DNA polymerase epsilon.";
RL J. Biol. Chem. 272:32337-32344(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9443964; DOI=10.1093/nar/26.3.730;
RA Jokela M., Makiniemi M., Lehtonen S., Szpirer C., Hellman U.,
RA Syvaeoja J.E.;
RT "The small subunits of human and mouse DNA polymerase epsilon are
RT homologous to the second largest subunit of the yeast Saccharomyces
RT cerevisiae DNA polymerase epsilon.";
RL Nucleic Acids Res. 26:730-734(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11433027; DOI=10.1093/nar/29.13.2810;
RA Huang D., Jokela M., Tuusa J., Skog S., Poikonen K., Syvaoja J.E.;
RT "E2F mediates induction of the Sp1-controlled promoter of the human DNA
RT polymerase varepsilon B-subunit gene POLE2.";
RL Nucleic Acids Res. 29:2810-2821(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-84 AND LEU-514.
RG NIEHS SNPs program;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Embryonic stem cell;
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 [8]
RP FUNCTION, AND IDENTIFICATION IN EPSILON DNA POLYMERASE COMPLEX.
RC TISSUE=Cervix carcinoma;
RX PubMed=10801849; DOI=10.1074/jbc.m002548200;
RA Li Y., Pursell Z.F., Linn S.;
RT "Identification and cloning of two histone fold motif-containing subunits
RT of HeLa DNA polymerase epsilon.";
RL J. Biol. Chem. 275:23247-23252(2000).
CC -!- FUNCTION: Accessory component of the DNA polymerase epsilon complex
CC (PubMed:10801849). Participates in DNA repair and in chromosomal DNA
CC replication (By similarity). {ECO:0000250|UniProtKB:P24482,
CC ECO:0000269|PubMed:10801849}.
CC -!- SUBUNIT: Component of the DNA polymerase epsilon complex consisting of
CC four subunits: the catalytic subunit POLE and the accessory subunits
CC POLE2, POLE3 and POLE4. {ECO:0000269|PubMed:10801849}.
CC -!- INTERACTION:
CC P56282; P52594: AGFG1; NbExp=3; IntAct=EBI-713847, EBI-996560;
CC P56282; Q9NPD3: EXOSC4; NbExp=5; IntAct=EBI-713847, EBI-371823;
CC P56282; V9HWB8: HEL-S-30; NbExp=3; IntAct=EBI-713847, EBI-10215395;
CC P56282; Q15691: MAPRE1; NbExp=6; IntAct=EBI-713847, EBI-1004115;
CC P56282; Q07864: POLE; NbExp=8; IntAct=EBI-713847, EBI-348526;
CC P56282; Q04864: REL; NbExp=3; IntAct=EBI-713847, EBI-307352;
CC P56282; O60504: SORBS3; NbExp=3; IntAct=EBI-713847, EBI-741237;
CC P56282; Q96SF7: TBX15; NbExp=3; IntAct=EBI-713847, EBI-10191361;
CC P56282; P14373: TRIM27; NbExp=7; IntAct=EBI-713847, EBI-719493;
CC P56282; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-713847, EBI-947187;
CC P56282; O96006: ZBED1; NbExp=3; IntAct=EBI-713847, EBI-740037;
CC P56282; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-713847, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P56282-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P56282-2; Sequence=VSP_042551;
CC Name=3;
CC IsoId=P56282-3; Sequence=VSP_043796;
CC -!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha,
CC beta, gamma, delta, and epsilon which are responsible for different
CC reactions of DNA synthesis.
CC -!- SIMILARITY: Belongs to the DNA polymerase epsilon subunit B family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/pole2/";
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DR EMBL; AF025840; AAC51920.1; -; mRNA.
DR EMBL; AF036899; AAC39610.1; -; mRNA.
DR EMBL; AF387034; AAK72254.1; -; Genomic_DNA.
DR EMBL; AF387021; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387022; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387023; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387024; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387025; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387026; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387027; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387028; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387029; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387030; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387031; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387032; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; AF387033; AAK72254.1; JOINED; Genomic_DNA.
DR EMBL; EF506887; ABO43040.1; -; Genomic_DNA.
DR EMBL; AK293163; BAG56707.1; -; mRNA.
DR EMBL; AL139099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC112962; AAI12963.1; -; mRNA.
DR EMBL; BC126218; AAI26219.1; -; mRNA.
DR EMBL; BC126220; AAI26221.1; -; mRNA.
DR CCDS; CCDS32073.1; -. [P56282-1]
DR CCDS; CCDS55914.1; -. [P56282-2]
DR CCDS; CCDS55915.1; -. [P56282-3]
DR RefSeq; NP_001184259.1; NM_001197330.1. [P56282-2]
DR RefSeq; NP_001184260.1; NM_001197331.1. [P56282-3]
DR RefSeq; NP_001335313.1; NM_001348384.1.
DR RefSeq; NP_002683.2; NM_002692.3. [P56282-1]
DR PDB; 2V6Z; NMR; -; M=1-73.
DR PDB; 5VBN; X-ray; 2.35 A; A/E=1-527.
DR PDB; 7PFO; EM; 3.20 A; A=1-527.
DR PDB; 7PLO; EM; 2.80 A; A=1-527.
DR PDBsum; 2V6Z; -.
DR PDBsum; 5VBN; -.
DR PDBsum; 7PFO; -.
DR PDBsum; 7PLO; -.
DR AlphaFoldDB; P56282; -.
DR BMRB; P56282; -.
DR SMR; P56282; -.
DR BioGRID; 111423; 61.
DR ComplexPortal; CPX-2108; DNA polymerase epsilon complex.
DR CORUM; P56282; -.
DR IntAct; P56282; 32.
DR STRING; 9606.ENSP00000216367; -.
DR ChEMBL; CHEMBL2363042; -.
DR DrugBank; DB00242; Cladribine.
DR iPTMnet; P56282; -.
DR PhosphoSitePlus; P56282; -.
DR BioMuta; POLE2; -.
DR DMDM; 3915676; -.
DR EPD; P56282; -.
DR jPOST; P56282; -.
DR MassIVE; P56282; -.
DR MaxQB; P56282; -.
DR PaxDb; P56282; -.
DR PeptideAtlas; P56282; -.
DR PRIDE; P56282; -.
DR ProteomicsDB; 56911; -. [P56282-1]
DR ProteomicsDB; 56912; -. [P56282-2]
DR ProteomicsDB; 56913; -. [P56282-3]
DR Antibodypedia; 23530; 134 antibodies from 23 providers.
DR DNASU; 5427; -.
DR Ensembl; ENST00000216367.10; ENSP00000216367.5; ENSG00000100479.13. [P56282-1]
DR Ensembl; ENST00000539565.6; ENSP00000446313.2; ENSG00000100479.13. [P56282-2]
DR Ensembl; ENST00000554396.5; ENSP00000451621.1; ENSG00000100479.13. [P56282-3]
DR GeneID; 5427; -.
DR KEGG; hsa:5427; -.
DR MANE-Select; ENST00000216367.10; ENSP00000216367.5; NM_002692.4; NP_002683.2.
DR UCSC; uc001wwu.4; human. [P56282-1]
DR CTD; 5427; -.
DR DisGeNET; 5427; -.
DR GeneCards; POLE2; -.
DR HGNC; HGNC:9178; POLE2.
DR HPA; ENSG00000100479; Tissue enhanced (bone).
DR MIM; 602670; gene.
DR neXtProt; NX_P56282; -.
DR OpenTargets; ENSG00000100479; -.
DR PharmGKB; PA278; -.
DR VEuPathDB; HostDB:ENSG00000100479; -.
DR eggNOG; KOG3818; Eukaryota.
DR GeneTree; ENSGT00390000012435; -.
DR HOGENOM; CLU_010628_2_0_1; -.
DR InParanoid; P56282; -.
DR OMA; CRLQYCT; -.
DR OrthoDB; 375960at2759; -.
DR PhylomeDB; P56282; -.
DR TreeFam; TF103007; -.
DR BRENDA; 2.7.7.7; 2681.
DR PathwayCommons; P56282; -.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-68952; DNA replication initiation.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR SignaLink; P56282; -.
DR SIGNOR; P56282; -.
DR BioGRID-ORCS; 5427; 765 hits in 1066 CRISPR screens.
DR ChiTaRS; POLE2; human.
DR EvolutionaryTrace; P56282; -.
DR GeneWiki; POLE2; -.
DR GenomeRNAi; 5427; -.
DR Pharos; P56282; Tbio.
DR PRO; PR:P56282; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P56282; protein.
DR Bgee; ENSG00000100479; Expressed in ventricular zone and 119 other tissues.
DR ExpressionAtlas; P56282; baseline and differential.
DR Genevisible; P56282; HS.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; TAS:ProtInc.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:ComplexPortal.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR InterPro; IPR024639; DNA_pol_e_bsu_N.
DR InterPro; IPR016266; POLE2.
DR PANTHER; PTHR12708; PTHR12708; 1.
DR Pfam; PF04042; DNA_pol_E_B; 1.
DR Pfam; PF12213; Dpoe2NT; 1.
DR PIRSF; PIRSF000799; DNA_pol_eps_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA replication; DNA-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..527
FT /note="DNA polymerase epsilon subunit 2"
FT /id="PRO_0000071562"
FT VAR_SEQ 83..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042551"
FT VAR_SEQ 500..527
FT /note="GSFPRSGFSFKVFYPSNKTVEDSKLQGF -> VRM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043796"
FT VARIANT 84
FT /note="H -> P (in dbSNP:rs34857719)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_044379"
FT VARIANT 456
FT /note="L -> V (in dbSNP:rs34574266)"
FT /id="VAR_044380"
FT VARIANT 514
FT /note="P -> L (in dbSNP:rs45515094)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_044381"
FT CONFLICT 11
FT /note="L -> P (in Ref. 1; AAC51920)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="Missing (in Ref. 1; AAC51920)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:2V6Z"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:2V6Z"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2V6Z"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2V6Z"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:2V6Z"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2V6Z"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:2V6Z"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:5VBN"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 123..142
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 178..191
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 273..281
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 298..311
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 334..350
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:5VBN"
FT TURN 370..374
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 410..417
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 419..424
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 437..448
FT /evidence="ECO:0007829|PDB:5VBN"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 463..469
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:5VBN"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:5VBN"
FT TURN 514..517
FT /evidence="ECO:0007829|PDB:5VBN"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:5VBN"
SQ SEQUENCE 527 AA; 59537 MW; AFA7AF7C2C0BFF15 CRC64;
MAPERLRSRA LSAFKLRGLL LRGEAIKYLT EALQSISELE LEDKLEKIIN AVEKQPLSSN
MIERSVVEAA VQECSQSVDE TIEHVFNIIG AFDIPRFVYN SERKKFLPLL MTNHPAPNLF
GTPRDKAEMF RERYTILHQR THRHELFTPP VIGSHPDESG SKFQLKTIET LLGSTTKIGD
AIVLGMITQL KEGKFFLEDP TGTVQLDLSK AQFHSGLYTE ACFVLAEGWF EDQVFHVNAF
GFPPTEPSST TRAYYGNINF FGGPSNTSVK TSAKLKQLEE ENKDAMFVFL SDVWLDQVEV
LEKLRIMFAG YSPAPPTCFI LCGNFSSAPY GKNQVQALKD SLKTLADIIC EYPDIHQSSR
FVFVPGPEDP GFGSILPRPP LAESITNEFR QRVPFSVFTT NPCRIQYCTQ EITVFREDLV
NKMCRNCVRF PSSNLAIPNH FVKTILSQGH LTPLPLYVCP VYWAYDYALR VYPVPDLLVI
ADKYDPFTTT NTECLCINPG SFPRSGFSFK VFYPSNKTVE DSKLQGF
