TDT_HUMAN
ID TDT_HUMAN Reviewed; 509 AA.
AC P04053; Q53FH1; Q5W103; Q96E50;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=DNA nucleotidylexotransferase;
DE EC=2.7.7.31 {ECO:0000269|PubMed:11473582, ECO:0000269|PubMed:16371131, ECO:0000269|PubMed:8163485};
DE AltName: Full=Terminal addition enzyme;
DE AltName: Full=Terminal deoxynucleotidyltransferase;
DE Short=Terminal transferase {ECO:0000303|PubMed:11473582};
GN Name=DNTT; Synonyms=TDT {ECO:0000303|PubMed:11473582};
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 2), AND VARIANT GLY-112.
RX PubMed=2863268; DOI=10.1016/s0021-9258(19)85111-6;
RA Peterson R.C., Cheung L.C., Mattaliano R.J., White S.T., Chang L.M.S.,
RA Bollum F.J.;
RT "Expression of human terminal deoxynucleotidyl transferase in Escherichia
RT coli.";
RL J. Biol. Chem. 260:10495-10502(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-112.
RX PubMed=2833741; DOI=10.1073/pnas.85.8.2489;
RA Riley L.K., Morrow J.K., Danton M.J., Coleman M.S.;
RT "Human terminal deoxyribonucleotidyltransferase: molecular cloning and
RT structural analysis of the gene and 5' flanking region.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2489-2493(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-112.
RX PubMed=11554927; DOI=10.1046/j.1365-2443.2001.00460.x;
RA Ibe S., Fujita K., Toyomoto T., Shimazaki N., Kaneko R., Tanabe A.,
RA Takebe I., Kuroda S., Kobayashi T., Toji S., Tamai K., Yamamoto H.,
RA Koiwai O.;
RT "Terminal deoxynucleotidyltransferase is negatively regulated by direct
RT interaction with proliferating cell nuclear antigen.";
RL Genes Cells 6:815-824(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-112.
RC TISSUE=Thymus;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-112.
RC TISSUE=Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
RX PubMed=3395350; DOI=10.1016/0006-291x(88)90654-7;
RA Koiwai O., Morita A.;
RT "Isolation of putative promoter region for human terminal
RT deoxynucleotidyltransferase gene.";
RL Biochem. Biophys. Res. Commun. 154:91-100(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 271-508 (ISOFORM 2).
RX PubMed=6087320; DOI=10.1073/pnas.81.14.4363;
RA Peterson R.C., Cheung L.C., Mattaliano R.J., Chang L.M.S., Bollum F.J.;
RT "Molecular cloning of human terminal deoxynucleotidyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4363-4367(1984).
RN [9]
RP MUTAGENESIS OF ASP-343, AND CATALYTIC ACTIVITY.
RX PubMed=8163485; DOI=10.1016/s0021-9258(17)32652-2;
RA Yang B., Gathy K.N., Coleman M.S.;
RT "Mutational analysis of residues in the nucleotide binding domain of human
RT terminal deoxynucleotidyl transferase.";
RL J. Biol. Chem. 269:11859-11868(1994).
RN [10]
RP INTERACTION WITH DNTTIP1, CATALYTIC ACTIVITY, AND COFACTOR.
RC TISSUE=Thymus;
RX PubMed=11473582; DOI=10.1046/j.1365-2443.2001.00449.x;
RA Yamashita N., Shimazaki N., Ibe S., Kaneko R., Tanabe A., Toyomoto T.,
RA Fujita K., Hasegawa T., Toji S., Tamai K., Yamamoto H., Koiwai O.;
RT "Terminal deoxynucleotidyltransferase directly interacts with a novel
RT nuclear protein that is homologous to p65.";
RL Genes Cells 6:641-652(2001).
RN [11]
RP INTERACTION WITH DNTTIP2 AND CORE HISTONE.
RX PubMed=12786946; DOI=10.1046/j.1365-2443.2003.00656.x;
RA Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K.,
RA Fujisaki S., Hayano T., Koiwai O.;
RT "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel
RT chromatin remodeling protein with 82 kDa and core histone.";
RL Genes Cells 8:559-571(2003).
RN [12]
RP INTERACTION WITH PRP19.
RX PubMed=12960389; DOI=10.1073/pnas.1631060100;
RA Mahajan K.N., Mitchell B.S.;
RT "Role of human Pso4 in mammalian DNA repair and association with terminal
RT deoxynucleotidyl transferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003).
RN [13]
RP INTERACTION WITH DNTTIP1 AND TRERF1, SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=16371131; DOI=10.1111/j.1365-2443.2005.00916.x;
RA Fujisaki S., Sato A., Toyomoto T., Hayano T., Sugai M., Kubota T.,
RA Koiwai O.;
RT "Direct binding of TReP-132 with TdT results in reduction of TdT
RT activity.";
RL Genes Cells 11:47-57(2006).
RN [14]
RP STRUCTURE BY NMR OF 19-125.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of BRCT domain of terminal
RT deoxynucleotidyltransferase.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Template-independent DNA polymerase which catalyzes the
CC random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a
CC DNA initiator. One of the in vivo functions of this enzyme is the
CC addition of nucleotides at the junction (N region) of rearranged Ig
CC heavy chain and T-cell receptor gene segments during the maturation of
CC B- and T-cells. {ECO:0000250|UniProtKB:P09838}.
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=2.7.7.31;
CC Evidence={ECO:0000269|PubMed:11473582, ECO:0000269|PubMed:16371131,
CC ECO:0000269|PubMed:8163485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:11473582};
CC Note=Can also utilize other divalent cations, such as Mn(2+) and Co(2+)
CC (in vitro). {ECO:0000250|UniProtKB:P09838, ECO:0000305};
CC -!- SUBUNIT: Interacts with PRP19 and DNTTIP1. Forms a ternary complex with
CC DNTTIP2 and core histone. Released from this complex by PCNA. Interacts
CC with TRERF1 (PubMed:16371131). {ECO:0000269|PubMed:11473582,
CC ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:12960389,
CC ECO:0000269|PubMed:16371131}.
CC -!- INTERACTION:
CC P04053; A8MW99: MEI4; NbExp=3; IntAct=EBI-1220259, EBI-19944212;
CC P04053; Q04864: REL; NbExp=3; IntAct=EBI-1220259, EBI-307352;
CC P04053; P15884-3: TCF4; NbExp=3; IntAct=EBI-1220259, EBI-13636688;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16371131}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04053-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04053-2; Sequence=VSP_038397;
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR EMBL; M11722; AAA36726.1; -; mRNA.
DR EMBL; M20703; AAA53100.1; -; mRNA.
DR EMBL; M22968; AAA53100.1; JOINED; mRNA.
DR EMBL; M20694; AAA53100.1; JOINED; mRNA.
DR EMBL; M20695; AAA53100.1; JOINED; mRNA.
DR EMBL; M20696; AAA53100.1; JOINED; mRNA.
DR EMBL; M20697; AAA53100.1; JOINED; mRNA.
DR EMBL; M20698; AAA53100.1; JOINED; mRNA.
DR EMBL; M20699; AAA53100.1; JOINED; mRNA.
DR EMBL; M20700; AAA53100.1; JOINED; mRNA.
DR EMBL; M20701; AAA53100.1; JOINED; mRNA.
DR EMBL; M20702; AAA53100.1; JOINED; mRNA.
DR EMBL; AB046378; BAB72001.1; -; mRNA.
DR EMBL; AK223317; BAD97037.1; -; mRNA.
DR EMBL; AL136181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012920; AAH12920.1; -; mRNA.
DR EMBL; M21195; AAA61137.1; -; Genomic_DNA.
DR EMBL; K01919; AAA61136.1; -; mRNA.
DR CCDS; CCDS44465.1; -. [P04053-2]
DR CCDS; CCDS7447.1; -. [P04053-1]
DR PIR; A23924; WXHU.
DR RefSeq; NP_001017520.1; NM_001017520.1. [P04053-2]
DR RefSeq; NP_004079.3; NM_004088.3. [P04053-1]
DR PDB; 2COE; NMR; -; A=19-125.
DR PDB; 5W4E; X-ray; 2.18 A; A/D=7-22.
DR PDBsum; 2COE; -.
DR PDBsum; 5W4E; -.
DR AlphaFoldDB; P04053; -.
DR SMR; P04053; -.
DR BioGRID; 108127; 13.
DR CORUM; P04053; -.
DR IntAct; P04053; 6.
DR STRING; 9606.ENSP00000360216; -.
DR BindingDB; P04053; -.
DR ChEMBL; CHEMBL4810; -.
DR DrugBank; DB02189; 2',3'-Dideoxyadenosine triphosphate.
DR iPTMnet; P04053; -.
DR PhosphoSitePlus; P04053; -.
DR BioMuta; DNTT; -.
DR DMDM; 311033533; -.
DR jPOST; P04053; -.
DR MassIVE; P04053; -.
DR MaxQB; P04053; -.
DR PaxDb; P04053; -.
DR PeptideAtlas; P04053; -.
DR PRIDE; P04053; -.
DR ProteomicsDB; 51639; -. [P04053-1]
DR ProteomicsDB; 51640; -. [P04053-2]
DR Antibodypedia; 16924; 603 antibodies from 40 providers.
DR DNASU; 1791; -.
DR Ensembl; ENST00000371174.5; ENSP00000360216.2; ENSG00000107447.8. [P04053-1]
DR Ensembl; ENST00000630152.1; ENSP00000486733.1; ENSG00000107447.8. [P04053-2]
DR GeneID; 1791; -.
DR KEGG; hsa:1791; -.
DR MANE-Select; ENST00000371174.5; ENSP00000360216.2; NM_004088.4; NP_004079.3.
DR UCSC; uc001kmf.4; human. [P04053-1]
DR CTD; 1791; -.
DR DisGeNET; 1791; -.
DR GeneCards; DNTT; -.
DR HGNC; HGNC:2983; DNTT.
DR HPA; ENSG00000107447; Tissue enriched (lymphoid).
DR MIM; 187410; gene.
DR neXtProt; NX_P04053; -.
DR OpenTargets; ENSG00000107447; -.
DR PharmGKB; PA27449; -.
DR VEuPathDB; HostDB:ENSG00000107447; -.
DR eggNOG; KOG2534; Eukaryota.
DR GeneTree; ENSGT00940000158584; -.
DR HOGENOM; CLU_008698_0_0_1; -.
DR InParanoid; P04053; -.
DR OMA; PKVINLW; -.
DR OrthoDB; 1212057at2759; -.
DR PhylomeDB; P04053; -.
DR TreeFam; TF103012; -.
DR BRENDA; 2.7.7.31; 2681.
DR PathwayCommons; P04053; -.
DR SABIO-RK; P04053; -.
DR SignaLink; P04053; -.
DR BioGRID-ORCS; 1791; 13 hits in 1071 CRISPR screens.
DR ChiTaRS; DNTT; human.
DR EvolutionaryTrace; P04053; -.
DR GeneWiki; Terminal_deoxynucleotidyl_transferase; -.
DR GenomeRNAi; 1791; -.
DR Pharos; P04053; Tchem.
DR PRO; PR:P04053; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P04053; protein.
DR Bgee; ENSG00000107447; Expressed in thymus and 28 other tissues.
DR Genevisible; P04053; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003912; F:DNA nucleotidylexotransferase activity; IDA:UniProtKB.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006259; P:DNA metabolic process; IDA:UniProtKB.
DR GO; GO:0006304; P:DNA modification; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 3.30.210.10; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR InterPro; IPR027292; TdT.
DR InterPro; IPR001726; TdT/Mu.
DR PANTHER; PTHR11276; PTHR11276; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PIRSF; PIRSF000817; DNA_NT; 1.
DR PIRSF; PIRSF501175; TDT; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00871; DNAPOLXTDT.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Terminal addition; Transferase.
FT CHAIN 1..509
FT /note="DNA nucleotidylexotransferase"
FT /id="PRO_0000218791"
FT DOMAIN 27..124
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..509
FT /note="Mediates interaction with DNTTIP2"
FT /evidence="ECO:0000269|PubMed:12786946"
FT REGION 258..262
FT /note="Involved in DNA binding"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT MOTIF 11..17
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P06526"
FT BINDING 333..338
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 342..345
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 433
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT BINDING 448..449
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09838"
FT VAR_SEQ 454
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2863268,
FT ECO:0000303|PubMed:6087320"
FT /id="VSP_038397"
FT VARIANT 112
FT /note="R -> G (in dbSNP:rs6584066)"
FT /evidence="ECO:0000269|PubMed:11554927,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2833741,
FT ECO:0000269|PubMed:2863268, ECO:0000269|Ref.4"
FT /id="VAR_058200"
FT MUTAGEN 343
FT /note="D->E: Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:8163485"
FT CONFLICT 51
FT /note="F -> L (in Ref. 4; BAD97037)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="L -> P (in Ref. 4; BAD97037)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="T -> A (in Ref. 4; BAD97037)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="T -> A (in Ref. 4; BAD97037)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="L -> M (in Ref. 4; BAD97037)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="S -> SP (in Ref. 2; AAA53100)"
FT /evidence="ECO:0000305"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:2COE"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2COE"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2COE"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:2COE"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2COE"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:2COE"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2COE"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:2COE"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2COE"
SQ SEQUENCE 509 AA; 58536 MW; 0EC01E380FA7E5A2 CRC64;
MDPPRASHLS PRKKRPRQTG ALMASSPQDI KFQDLVVFIL EKKMGTTRRA FLMELARRKG
FRVENELSDS VTHIVAENNS GSDVLEWLQA QKVQVSSQPE LLDVSWLIEC IRAGKPVEMT
GKHQLVVRRD YSDSTNPGPP KTPPIAVQKI SQYACQRRTT LNNCNQIFTD AFDILAENCE
FRENEDSCVT FMRAASVLKS LPFTIISMKD TEGIPCLGSK VKGIIEEIIE DGESSEVKAV
LNDERYQSFK LFTSVFGVGL KTSEKWFRMG FRTLSKVRSD KSLKFTRMQK AGFLYYEDLV
SCVTRAEAEA VSVLVKEAVW AFLPDAFVTM TGGFRRGKKM GHDVDFLITS PGSTEDEEQL
LQKVMNLWEK KGLLLYYDLV ESTFEKLRLP SRKVDALDHF QKCFLIFKLP RQRVDSDQSS
WQEGKTWKAI RVDLVLCPYE RRAFALLGWT GSRQFERDLR RYATHERKMI LDNHALYDKT
KRIFLKAESE EEIFAHLGLD YIEPWERNA
