TDRKH_HUMAN
ID TDRKH_HUMAN Reviewed; 561 AA.
AC Q9Y2W6; D3DV24; Q5SZR3; Q5SZR5; Q8N582; Q9NYV5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Tudor and KH domain-containing protein;
DE AltName: Full=Tudor domain-containing protein 2;
GN Name=TDRKH; Synonyms=TDRD2;
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).
RC TISSUE=Aorta;
RX PubMed=10767542; DOI=10.1016/s0378-1119(00)00087-1;
RA Lamb F.S., Barna T.J., Goud C., Marenholz I., Mischke D., Schutte B.C.;
RT "Complex RNA processing of TDRKH, a novel gene encoding the putative RNA-
RT binding tudor and KH domains.";
RL Gene 246:209-218(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP UBIQUITINATION AT LYS-65; LYS-76; LYS-110; LYS-112; LYS-152; LYS-175;
RP LYS-181; LYS-187; LYS-193; LYS-256; LYS-267; LYS-479; LYS-510 AND LYS-529.
RX PubMed=25621951; DOI=10.1038/ncb3097;
RA Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
RA Kirkpatrick D.S., Bingol B., Corn J.E.;
RT "USP30 and parkin homeostatically regulate atypical ubiquitin chains on
RT mitochondria.";
RL Nat. Cell Biol. 17:160-169(2015).
RN [8]
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 [9]
RP STRUCTURE BY NMR OF 329-425.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the Tudor domain of Tudor and KH domain-containing
RT protein.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Participates in the primary piRNA biogenesis pathway and is
CC required during spermatogenesis to repress transposable elements and
CC prevent their mobilization, which is essential for the germline
CC integrity. The piRNA metabolic process mediates the repression of
CC transposable elements during meiosis by forming complexes composed of
CC piRNAs and Piwi proteins and govern the methylation and subsequent
CC repression of transposons. Required for the final steps of primary
CC piRNA biogenesis by participating in the processing of 31-37 nt
CC intermediates into mature piRNAs. May act in pi-bodies and piP-bodies
CC by transferring piRNA precursors or intermediates to or between these
CC granules. {ECO:0000250|UniProtKB:Q80VL1}.
CC -!- SUBUNIT: Interacts with (symmetrically methylated) PIWIL1, PIWIL2 and
CC PIWIL4. {ECO:0000250|UniProtKB:Q80VL1}.
CC -!- INTERACTION:
CC Q9Y2W6; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-12842466, EBI-14240149;
CC Q9Y2W6; Q9NS86: LANCL2; NbExp=3; IntAct=EBI-12842466, EBI-2510837;
CC Q9Y2W6; Q9BV90: SNRNP25; NbExp=3; IntAct=EBI-12842466, EBI-9675976;
CC Q9Y2W6; Q8NCN2: ZBTB34; NbExp=3; IntAct=EBI-12842466, EBI-11317716;
CC Q9Y2W6; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-12842466, EBI-11419867;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q80VL1}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q80VL1}. Note=Probable component
CC of the meiotic nuage, also named P granule, a germ-cell-specific
CC organelle required to repress transposon activity during meiosis.
CC Colocalizes with pi- and piP-bodies, a subset of the nuage which
CC contains secondary piRNAs. Associated with mitochondria in the
CC germline. {ECO:0000250|UniProtKB:Q80VL1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2W6-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2W6-3; Sequence=VSP_040981;
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000269|PubMed:25621951}.
CC -!- SIMILARITY: Belongs to the Tdrkh family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30971.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=BC022467; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF119121; AAD30971.1; ALT_SEQ; mRNA.
DR EMBL; AF227192; AAF36701.1; -; mRNA.
DR EMBL; AL589765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53411.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53409.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53410.1; -; Genomic_DNA.
DR EMBL; BC022467; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS41394.1; -. [Q9Y2W6-2]
DR CCDS; CCDS41395.1; -. [Q9Y2W6-3]
DR RefSeq; NP_001077432.1; NM_001083963.1. [Q9Y2W6-2]
DR RefSeq; NP_001077433.1; NM_001083964.1. [Q9Y2W6-3]
DR RefSeq; NP_001077434.1; NM_001083965.1. [Q9Y2W6-2]
DR RefSeq; NP_006853.2; NM_006862.3. [Q9Y2W6-2]
DR RefSeq; XP_016855611.1; XM_017000122.1. [Q9Y2W6-2]
DR RefSeq; XP_016855612.1; XM_017000123.1. [Q9Y2W6-2]
DR RefSeq; XP_016855613.1; XM_017000124.1. [Q9Y2W6-2]
DR RefSeq; XP_016855614.1; XM_017000125.1. [Q9Y2W6-2]
DR RefSeq; XP_016855615.1; XM_017000126.1. [Q9Y2W6-2]
DR RefSeq; XP_016855616.1; XM_017000127.1. [Q9Y2W6-2]
DR PDB; 2DIQ; NMR; -; A=329-425.
DR PDB; 3FDR; X-ray; 1.75 A; A=327-420.
DR PDB; 5J39; X-ray; 1.95 A; A/B=309-498.
DR PDB; 6B57; X-ray; 1.93 A; A/B=309-497.
DR PDB; 6PI7; X-ray; 2.80 A; A/D=305-525.
DR PDBsum; 2DIQ; -.
DR PDBsum; 3FDR; -.
DR PDBsum; 5J39; -.
DR PDBsum; 6B57; -.
DR PDBsum; 6PI7; -.
DR AlphaFoldDB; Q9Y2W6; -.
DR SMR; Q9Y2W6; -.
DR BioGRID; 116212; 72.
DR DIP; DIP-59459N; -.
DR IntAct; Q9Y2W6; 25.
DR MINT; Q9Y2W6; -.
DR STRING; 9606.ENSP00000357812; -.
DR iPTMnet; Q9Y2W6; -.
DR PhosphoSitePlus; Q9Y2W6; -.
DR BioMuta; TDRKH; -.
DR DMDM; 332278122; -.
DR EPD; Q9Y2W6; -.
DR jPOST; Q9Y2W6; -.
DR MassIVE; Q9Y2W6; -.
DR MaxQB; Q9Y2W6; -.
DR PaxDb; Q9Y2W6; -.
DR PeptideAtlas; Q9Y2W6; -.
DR PRIDE; Q9Y2W6; -.
DR ProteomicsDB; 85917; -. [Q9Y2W6-2]
DR ProteomicsDB; 85918; -. [Q9Y2W6-3]
DR ABCD; Q9Y2W6; 6 sequenced antibodies.
DR Antibodypedia; 10583; 84 antibodies from 25 providers.
DR DNASU; 11022; -.
DR Ensembl; ENST00000368822.5; ENSP00000357812.1; ENSG00000182134.17. [Q9Y2W6-2]
DR Ensembl; ENST00000368824.8; ENSP00000357815.3; ENSG00000182134.17. [Q9Y2W6-2]
DR Ensembl; ENST00000368825.7; ENSP00000357817.3; ENSG00000182134.17. [Q9Y2W6-3]
DR Ensembl; ENST00000368827.10; ENSP00000357819.6; ENSG00000182134.17. [Q9Y2W6-2]
DR Ensembl; ENST00000458431.6; ENSP00000395718.2; ENSG00000182134.17. [Q9Y2W6-2]
DR GeneID; 11022; -.
DR KEGG; hsa:11022; -.
DR MANE-Select; ENST00000368824.8; ENSP00000357815.3; NM_001083965.2; NP_001077434.1.
DR UCSC; uc001eza.6; human. [Q9Y2W6-2]
DR CTD; 11022; -.
DR DisGeNET; 11022; -.
DR GeneCards; TDRKH; -.
DR HGNC; HGNC:11713; TDRKH.
DR HPA; ENSG00000182134; Tissue enhanced (parathyroid gland, testis).
DR MIM; 609501; gene.
DR neXtProt; NX_Q9Y2W6; -.
DR OpenTargets; ENSG00000182134; -.
DR PharmGKB; PA36431; -.
DR VEuPathDB; HostDB:ENSG00000182134; -.
DR eggNOG; KOG2279; Eukaryota.
DR GeneTree; ENSGT00940000159364; -.
DR InParanoid; Q9Y2W6; -.
DR OMA; MEVYVSA; -.
DR OrthoDB; 971207at2759; -.
DR PhylomeDB; Q9Y2W6; -.
DR TreeFam; TF318292; -.
DR PathwayCommons; Q9Y2W6; -.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; Q9Y2W6; -.
DR BioGRID-ORCS; 11022; 9 hits in 1083 CRISPR screens.
DR EvolutionaryTrace; Q9Y2W6; -.
DR GeneWiki; TDRKH; -.
DR GenomeRNAi; 11022; -.
DR Pharos; Q9Y2W6; Tbio.
DR PRO; PR:Q9Y2W6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y2W6; protein.
DR Bgee; ENSG00000182134; Expressed in right testis and 120 other tissues.
DR ExpressionAtlas; Q9Y2W6; baseline and differential.
DR Genevisible; Q9Y2W6; HS.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0071547; C:piP-body; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0030719; P:P granule organization; IBA:GO_Central.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00013; KH_1; 2.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00322; KH; 2.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF54791; SSF54791; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Differentiation;
KW Isopeptide bond; Mitochondrion; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; RNA-mediated gene silencing; Spermatogenesis; Ubl conjugation.
FT CHAIN 1..561
FT /note="Tudor and KH domain-containing protein"
FT /id="PRO_0000050141"
FT DOMAIN 52..115
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 124..190
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 353..412
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 219..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 187
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 510
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 529
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT VAR_SEQ 108..152
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040981"
FT VARIANT 257
FT /note="G -> A (in dbSNP:rs17853082)"
FT /id="VAR_055980"
FT CONFLICT 15
FT /note="Q -> H (in Ref. 1; AAF36701)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="F -> S (in Ref. 1; AAF36701)"
FT /evidence="ECO:0000305"
FT STRAND 309..317
FT /evidence="ECO:0007829|PDB:6B57"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:6B57"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:3FDR"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:3FDR"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:3FDR"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:3FDR"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:2DIQ"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:3FDR"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:3FDR"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:3FDR"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:3FDR"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:3FDR"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:6B57"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:6B57"
FT HELIX 433..442
FT /evidence="ECO:0007829|PDB:6B57"
FT TURN 444..448
FT /evidence="ECO:0007829|PDB:5J39"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:6B57"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:6B57"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:5J39"
FT HELIX 482..488
FT /evidence="ECO:0007829|PDB:6B57"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:6B57"
SQ SEQUENCE 561 AA; 62046 MW; F89EBBDC48A8D420 CRC64;
MSTERTSWTS LSTIQKIALG LGIPASATVA YILYRRYRES REERLTFVGE DDIEIEMRVP
QEAVKLIIGR QGANIKQLRK QTGARIDVDT EDVGDERVLL ISGFPVQVCK AKAAIHQILT
ENTPVSEQLS VPQRSVGRII GRGGETIRSI CKASGAKITC DKESEGTLLL SRLIKISGTQ
KEVAAAKHLI LEKVSEDEEL RKRIAHSAET RVPRKQPISV RREDMTEPGG AGEPALWKNT
SSSMEPTAPL VTPPPKGGGD MAVVVSKEGS WEKPSDDSFQ KSEAQAIPEM PMFEIPSPDF
SFHADEYLEV YVSASEHPNH FWIQIVGSRS LQLDKLVNEM TQHYENSVPE DLTVHVGDIV
AAPLPTNGSW YRARVLGTLE NGNLDLYFVD FGDNGDCPLK DLRALRSDFL SLPFQAIECS
LARIAPSGDQ WEEEALDEFD RLTHCADWKP LVAKISSYVQ TGISTWPKIY LYDTSNGKKL
DIGLELVHKG YAIELPEDIE ENRAVPDMLK DMATETDASL STLLTETKKS SGEITHTLSC
LSLSEAASMS GDDNLEDDYL L
