TTKB_DROME
ID TTKB_DROME Reviewed; 643 AA.
AC P17789; A4V3Q4; Q32KE0; Q9V9V1; Q9V9V3;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Protein tramtrack, beta isoform;
DE AltName: Full=Repressor protein fushi tarazu;
DE AltName: Full=Tramtrack p69;
GN Name=ttk; Synonyms=FTZ-F2; ORFNames=CG1856;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=2104801; DOI=10.1002/j.1460-2075.1990.tb08097.x;
RA Harrison S.D., Travers A.A.;
RT "The tramtrack gene encodes a Drosophila finger protein that interacts with
RT the ftz transcriptional regulatory region and shows a novel embryonic
RT expression pattern.";
RL EMBO J. 9:207-216(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8223261; DOI=10.1242/dev.117.1.45;
RA Brown J.L., Wu C.;
RT "Repression of Drosophila pair-rule segmentation genes by ectopic
RT expression of tramtrack.";
RL Development 117:45-58(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8504931; DOI=10.1101/gad.7.6.1085;
RA Xiong W.C., Montell C.;
RT "Tramtrack is a transcriptional repressor required for cell fate
RT determination in the Drosophila eye.";
RL Genes Dev. 7:1085-1096(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP DNA-BINDING.
RX PubMed=1640455; DOI=10.1016/0022-2836(92)90952-g;
RA Fairall L., Harrison S.D., Travers A.A., Rhodes D.;
RT "Sequence-specific DNA binding by a two zinc-finger peptide from the
RT Drosophila melanogaster Tramtrack protein.";
RL J. Mol. Biol. 226:349-366(1992).
RN [9]
RP FUNCTION, INTERACTION WITH TRL, AND HOMODIMERIZATION.
RX PubMed=12384587; DOI=10.1093/nar/gkf570;
RA Pagans S., Ortiz-Lombardia M., Espinas M.L., Bernues J., Azorin F.;
RT "The Drosophila transcription factor tramtrack (TTK) interacts with
RT Trithorax-like (GAGA) and represses GAGA-mediated activation.";
RL Nucleic Acids Res. 30:4406-4413(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH PHYL.
RX PubMed=17962185; DOI=10.1074/jbc.m707765200;
RA Cooper S.E., Murawsky C.M., Lowe N., Travers A.A.;
RT "Two modes of degradation of the tramtrack transcription factors by Siah
RT homologues.";
RL J. Biol. Chem. 283:1076-1083(2008).
RN [11]
RP FUNCTION, AND UBIQUITINATION AT LYS-123; LYS-201; LYS-355; LYS-397;
RP LYS-418; LYS-457; LYS-478; LYS-480 AND LYS-545.
RX PubMed=18160715; DOI=10.1128/mcb.01567-07;
RA Bajpe P.K., van der Knaap J.A., Demmers J.A., Bezstarosti K., Bassett A.,
RA van Beusekom H.M., Travers A.A., Verrijzer C.P.;
RT "Deubiquitylating enzyme UBP64 controls cell fate through stabilization of
RT the transcriptional repressor tramtrack.";
RL Mol. Cell. Biol. 28:1606-1615(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 499-561, AND FUNCTION.
RX PubMed=8247159; DOI=10.1038/366483a0;
RA Fairall L., Schwabe J.W.R., Chapman L., Finch J.T., Rhodes D.;
RT "The crystal structure of a two zinc-finger peptide reveals an extension to
RT the rules for zinc-finger/DNA recognition.";
RL Nature 366:483-487(1993).
CC -!- FUNCTION: Binds to a number of sites in the transcriptional regulatory
CC region of ftz (PubMed:2104801). Isoform beta is required to repress
CC inappropriate segmentation gene transcription and repress genes
CC incompatible with development of photoreceptor cell fates
CC (PubMed:12384587, PubMed:18160715). Probable repressor of the
CC transcription of the segmentation genes ftz, eve, h, odd, run, and en
CC (PubMed:8223261). Inhibits Trl-dependent activation of eve
CC (PubMed:12384587). May bind to the region AGGGC/TGG (PubMed:8247159).
CC Degradation of ttk is directed by binding of sinah or sina, via the
CC adapter molecule phyl which binds to the BTB domain of ttk
CC (PubMed:18160715, PubMed:17962185). A second method of degradation
CC exists that is phyl-independent, this is mediated by recognition of
CC motifs in the C-terminus of ttk (PubMed:17962185).
CC {ECO:0000269|PubMed:12384587, ECO:0000269|PubMed:17962185,
CC ECO:0000269|PubMed:18160715, ECO:0000269|PubMed:2104801,
CC ECO:0000269|PubMed:8223261, ECO:0000269|PubMed:8247159,
CC ECO:0000269|PubMed:8504931}.
CC -!- SUBUNIT: Can form homodimers (PubMed:12384587). Interacts with Trl in
CC vivo via the BTB domain (PubMed:12384587). Interacts with phyl
CC (PubMed:17962185). Interacts with Usp47 (PubMed:18160715).
CC {ECO:0000269|PubMed:12384587, ECO:0000269|PubMed:17962185,
CC ECO:0000269|PubMed:18160715}.
CC -!- INTERACTION:
CC P17789; Q3KN55: Ank2; NbExp=4; IntAct=EBI-6173284, EBI-15122666;
CC P17789; O62531: AP-1mu; NbExp=4; IntAct=EBI-6173284, EBI-3423007;
CC P17789; Q0E8J0: MEP-1; NbExp=6; IntAct=EBI-6173284, EBI-91014;
CC P17789; Q8T3Y0: sinah; NbExp=4; IntAct=EBI-6173284, EBI-152023;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta; Synonyms=p69, C, D, F;
CC IsoId=P17789-1; Sequence=Displayed;
CC Name=Alpha; Synonyms=p88, A, E;
CC IsoId=P42282-1; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed in preblastoderm embryos, followed by complete decay upon
CC formation of the cellular blastoderm when ftz striped expression is at
CC its peak. {ECO:0000269|PubMed:2104801, ECO:0000269|PubMed:8223261}.
CC -!- PTM: Polyubiquitinated by sina. Polyubiquitin linkage is mainly through
CC 'Lys-48', but linkage through 'Lys-63' also occurs. Deubiquitination by
CC Usp47 leads to its stabilization. {ECO:0000269|PubMed:18160715}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28544.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABB36443.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA34981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X17121; CAA34981.1; ALT_INIT; mRNA.
DR EMBL; M62856; AAA28544.1; ALT_INIT; mRNA.
DR EMBL; X71627; CAA50634.1; -; mRNA.
DR EMBL; AE014297; AAF57181.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF57182.3; -; Genomic_DNA.
DR EMBL; AE014297; AAN14283.1; -; Genomic_DNA.
DR EMBL; AY122169; AAM52681.1; -; mRNA.
DR EMBL; BT001723; AAN71478.1; -; mRNA.
DR EMBL; BT023939; ABB36443.1; ALT_FRAME; mRNA.
DR PIR; S36017; S36017.
DR RefSeq; NP_001189330.1; NM_001202401.1. [P17789-1]
DR RefSeq; NP_524911.3; NM_080172.4. [P17789-1]
DR RefSeq; NP_733446.1; NM_170567.3. [P17789-1]
DR RefSeq; NP_733447.1; NM_170568.3. [P17789-1]
DR PDB; 2DRP; X-ray; 2.80 A; A/D=501-563.
DR PDBsum; 2DRP; -.
DR AlphaFoldDB; P17789; -.
DR SMR; P17789; -.
DR BioGRID; 71315; 84.
DR ELM; P17789; -.
DR IntAct; P17789; 32.
DR iPTMnet; P17789; -.
DR PRIDE; P17789; -.
DR DNASU; 48317; -.
DR EnsemblMetazoa; FBtr0085826; FBpp0085187; FBgn0003870. [P17789-1]
DR EnsemblMetazoa; FBtr0085828; FBpp0085189; FBgn0003870. [P17789-1]
DR EnsemblMetazoa; FBtr0085830; FBpp0085191; FBgn0003870. [P17789-1]
DR EnsemblMetazoa; FBtr0303228; FBpp0292320; FBgn0003870. [P17789-1]
DR GeneID; 48317; -.
DR CTD; 7272; -.
DR FlyBase; FBgn0003870; ttk.
DR VEuPathDB; VectorBase:FBgn0003870; -.
DR GeneTree; ENSGT00940000175057; -.
DR OMA; NQHLNEQ; -.
DR SignaLink; P17789; -.
DR BioGRID-ORCS; 48317; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; P17789; -.
DR GenomeRNAi; 48317; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003870; Expressed in presumptive embryonic/larval digestive system (Drosophila) and 66 other tissues.
DR ExpressionAtlas; P17789; baseline and differential.
DR Genevisible; P17789; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0017053; C:transcription repressor complex; IPI:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR GO; GO:0060446; P:branching involved in open tracheal system development; IMP:FlyBase.
DR GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR GO; GO:0048750; P:compound eye corneal lens morphogenesis; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0035001; P:dorsal trunk growth, open tracheal system; IMP:FlyBase.
DR GO; GO:0048626; P:myoblast fate specification; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0007422; P:peripheral nervous system development; TAS:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0048053; P:R1/R6 development; IMP:FlyBase.
DR GO; GO:0045467; P:R7 cell development; IMP:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR GO; GO:0042682; P:regulation of compound eye cone cell fate specification; IMP:FlyBase.
DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035151; P:regulation of tube size, open tracheal system; IMP:FlyBase.
DR GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IMP:FlyBase.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..643
FT /note="Protein tramtrack, beta isoform"
FT /id="PRO_0000047079"
FT DOMAIN 33..98
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 508..531
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 538..561
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 118..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18160715"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18160715"
FT CROSSLNK 355
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18160715"
FT CROSSLNK 397
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18160715"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18160715"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18160715"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18160715"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18160715"
FT CROSSLNK 545
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18160715"
FT CONFLICT 255
FT /note="T -> M (in Ref. 2; AAA28544)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="H -> Q (in Ref. 2; AAA28544)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="T -> I (in Ref. 2; AAA28544)"
FT /evidence="ECO:0000305"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:2DRP"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:2DRP"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:2DRP"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:2DRP"
FT HELIX 520..530
FT /evidence="ECO:0007829|PDB:2DRP"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:2DRP"
FT TURN 541..543
FT /evidence="ECO:0007829|PDB:2DRP"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:2DRP"
FT HELIX 550..560
FT /evidence="ECO:0007829|PDB:2DRP"
SQ SEQUENCE 643 AA; 68771 MW; 98DAEA1A5E97DC59 CRC64;
MKMASQRFCL RWNNHQSNLL SVFDQLLHAE TFTDVTLAVE GQHLKAHKMV LSACSPYFNT
LFVSHPEKHP IVILKDVPYS DMKSLLDFMY RGEVSVDQER LTAFLRVAES LRIKGLTEVN
DDKPSPAAAA AGAGATGSES TATTPQLQRI QPYLVPQRNR SQAGGLLASA ANAGNTPTLP
VQPSLLSSAL MPKRKRGRPR KLSGSSNGTG NDYDDFDREN MMNDSSDLGN GKMCNESYSG
NDDGSDDNQP NAGHTDDLNE SRDSLPSKRS KNSKDHRVVS HHEDNSTSDG NDSDGEGLDT
SYMEPQLMLD EYDEPVEFKY NPLTDNSSPT QDHTDGSHLN EQARQQAFLI AAQRKHQVET
AAAAAASGIK LNIIGMAAGG AQVKSMVSIP KLTPIGKVNA ASTPLVSPAG SFSTATVKPR
VQKRPKLGKQ NGDVKPAVFS SQEYLDIYNS NDGFKLKAAG LSGSTPNLSA GLGTPSVKTK
LNLSSNVGEG EAEGSVRDYC TKEGEHTYRC KVCSRVYTHI SNFCRHYVTS HKRNVKVYPC
PFCFKEFTRK DNMTAHVKII HKIENPSTAL ATVAAANLAG QPLGVSGAST PPPPDLSGQN
SNQSLPATSN ALSTSSSSST SSSSGSLGPL TTSAPPAPAA AAQ
