PTK7_DROME
ID PTK7_DROME Reviewed; 1033 AA.
AC Q6AWJ9; C4IXZ4; Q24327;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Tyrosine-protein kinase-like otk {ECO:0000303|PubMed:11604138, ECO:0000303|PubMed:1371458, ECO:0000303|PubMed:15456725};
DE AltName: Full=Gp160-Dtrk {ECO:0000312|EMBL:CAA45053.1};
DE Short=Dtrk {ECO:0000312|EMBL:CAA45053.1};
DE AltName: Full=Off-track {ECO:0000312|EMBL:AAF58596.1};
DE AltName: Full=Tyrosine-protein kinase-like 7 homolog;
DE Flags: Precursor;
GN Name=otk {ECO:0000312|EMBL:AAT94478.1, ECO:0000312|FlyBase:FBgn0004839};
GN ORFNames=CG8967;
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] {ECO:0000305, ECO:0000312|EMBL:CAA45053.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S {ECO:0000312|EMBL:CAA45053.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:1371458};
RX PubMed=1371458; DOI=10.1002/j.1460-2075.1992.tb05067.x;
RA Pulido D., Campuzano S., Koda T., Modolell J., Barbacid M.;
RT "Dtrk, a Drosophila gene related to the trk family of neurotrophin
RT receptors, encodes a novel class of neural cell adhesion molecule.";
RL EMBO J. 11:391-404(1992).
RN [2] {ECO:0000312|EMBL:AAF58596.1}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF58596.1}
RP GENOME REANNOTATION.
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 [4] {ECO:0000312|EMBL:AAT94478.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAT94478.1}; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PLEXA, AND DISRUPTION PHENOTYPE.
RX PubMed=11604138; DOI=10.1016/s0896-6273(01)00446-9;
RA Winberg M.L., Tamagnone L., Bai J., Comoglio P.M., Montell D.,
RA Goodman C.S.;
RT "The transmembrane protein Off-track associates with Plexins and functions
RT downstream of Semaphorin signaling during axon guidance.";
RL Neuron 32:53-62(2001).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15456725; DOI=10.1242/dev.01406;
RA Cafferty P., Yu L., Rao Y.;
RT "The receptor tyrosine kinase Off-track is required for layer-specific
RT neuronal connectivity in Drosophila.";
RL Development 131:5287-5295(2004).
RN [7] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:18327897};
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8] {ECO:0000305}
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-524, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
CC -!- FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion
CC molecule that regulates neural recognition during the development of
CC the nervous system. Component of the repulsive Plexin signaling
CC response to regulate motor axon guidance at the embryonic stage. Also
CC component of a receptor complex that is required in the adult visual
CC system to innervate the lamina layer; specific targeting of R1-R6
CC axons. {ECO:0000269|PubMed:11604138, ECO:0000269|PubMed:1371458,
CC ECO:0000269|PubMed:15456725}.
CC -!- SUBUNIT: Interacts with plexA; component of a receptor complex that
CC mediates the repulsive signaling in response to Semaphorin ligands.
CC {ECO:0000269|PubMed:11604138}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1371458};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:1371458}.
CC -!- TISSUE SPECIFICITY: Dynamically expressed during embryogenesis in
CC several areas of the developing nervous system, including neurons and
CC fasciculating axons. Expression in stage 7 embryos is seen in the
CC anterior midgut primordia, cephalic furrow and along the germinal band.
CC At stage 11, expression is in 15 stripes over the trunk region, and in
CC the anterior and posterior midgut primordia. Stage 12 shows expression
CC in the developing nervous system, procephalic lobe and maxillar bud.
CC Stage 13 shows expression in the ventral cord, maxillar segment and in
CC three regions of the gut. At stage 16 expression is preferentially
CC detected throughout the nervous system, including the neuromers in the
CC ventral cord and the supraesophageal ganglion (at protein level). In
CC larva, expression is seen in developing R cells and is localized
CC predominantly to R1-R6 growth cones. {ECO:0000269|PubMed:1371458,
CC ECO:0000269|PubMed:15456725}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically, during
CC early to mid embryogenesis and early pupation.
CC {ECO:0000269|PubMed:1371458}.
CC -!- DISRUPTION PHENOTYPE: Axon guidance defects. R-cell differentiation and
CC cell fate determination are normal, but many R1-R6 axons connect
CC abnormally to medulla instead of innervating lamina.
CC {ECO:0000269|PubMed:11604138, ECO:0000269|PubMed:15456725}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- CAUTION: This protein has been proposed to undergo autophosphorylation
CC on tyrosine residues which is induced in response to cell adhesion
CC (PubMed:1371458). However, as mammalian orthologs of this protein seem
CC to lack kinase activity this protein may associate with, and be
CC phosphorylated by, an unknown active tyrosine kinase.
CC {ECO:0000305|PubMed:1371458}.
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DR EMBL; X63453; CAA45053.1; -; mRNA.
DR EMBL; AE013599; AAF58596.1; -; Genomic_DNA.
DR EMBL; BT015249; AAT94478.1; -; mRNA.
DR EMBL; BT083425; ACQ91629.1; -; mRNA.
DR PIR; S19247; S19247.
DR RefSeq; NP_523705.2; NM_078981.3.
DR PDB; 6S9F; X-ray; 1.97 A; A/B=24-580.
DR PDBsum; 6S9F; -.
DR AlphaFoldDB; Q6AWJ9; -.
DR SMR; Q6AWJ9; -.
DR BioGRID; 62067; 10.
DR IntAct; Q6AWJ9; 5.
DR MINT; Q6AWJ9; -.
DR STRING; 7227.FBpp0087135; -.
DR GlyGen; Q6AWJ9; 8 sites.
DR iPTMnet; Q6AWJ9; -.
DR PaxDb; Q6AWJ9; -.
DR PRIDE; Q6AWJ9; -.
DR DNASU; 36283; -.
DR EnsemblMetazoa; FBtr0088028; FBpp0087135; FBgn0004839.
DR GeneID; 36283; -.
DR KEGG; dme:Dmel_CG8967; -.
DR UCSC; CG8967-RA; d. melanogaster.
DR CTD; 36283; -.
DR FlyBase; FBgn0004839; otk.
DR VEuPathDB; VectorBase:FBgn0004839; -.
DR eggNOG; KOG1026; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000157908; -.
DR HOGENOM; CLU_012268_0_0_1; -.
DR InParanoid; Q6AWJ9; -.
DR OMA; AYDKRVY; -.
DR PhylomeDB; Q6AWJ9; -.
DR SignaLink; Q6AWJ9; -.
DR BioGRID-ORCS; 36283; 0 hits in 3 CRISPR screens.
DR ChiTaRS; otk; fly.
DR GenomeRNAi; 36283; -.
DR PRO; PR:Q6AWJ9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004839; Expressed in wing disc and 13 other tissues.
DR ExpressionAtlas; Q6AWJ9; baseline and differential.
DR Genevisible; Q6AWJ9; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR GO; GO:0030215; F:semaphorin receptor binding; TAS:FlyBase.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IDA:FlyBase.
DR GO; GO:0048804; P:imaginal disc-derived female genitalia morphogenesis; IGI:FlyBase.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IGI:FlyBase.
DR GO; GO:0035260; P:internal genitalia morphogenesis; IGI:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 5.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1033
FT /note="Tyrosine-protein kinase-like otk"
FT /evidence="ECO:0000255"
FT /id="PRO_5000145927"
FT TOPO_DOM 23..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..1033
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..114
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 113..199
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 251..365
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 368..463
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 468..558
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255"
FT DOMAIN 692..1028
FT /note="Protein kinase; inactive"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 617..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 46..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 137..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 399..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 490..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 221
FT /note="E -> Q (in Ref. 1; CAA45053)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="G -> S (in Ref. 4; ACQ91629)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="P -> H (in Ref. 1; CAA45053)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="I -> F (in Ref. 1; CAA45053)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="Q -> L (in Ref. 4; ACQ91629)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="V -> I (in Ref. 1; CAA45053)"
FT /evidence="ECO:0000305"
FT CONFLICT 772
FT /note="D -> E (in Ref. 1; CAA45053)"
FT /evidence="ECO:0000305"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:6S9F"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:6S9F"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:6S9F"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 350..358
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:6S9F"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 443..451
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 454..472
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:6S9F"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:6S9F"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:6S9F"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 538..545
FT /evidence="ECO:0007829|PDB:6S9F"
FT STRAND 550..560
FT /evidence="ECO:0007829|PDB:6S9F"
SQ SEQUENCE 1033 AA; 114267 MW; 559659540BDE66F5 CRC64;
MTARMISICG LVMALMMASV LASSSRFQRV PQSQSVVENE SVKFECESTD SYSELHYDWL
HNGHRIAYDK RVHQIGSNLH IEAVRRTEDV GNYVCIATNL ASGAREASPP AKLSVIYLES
ASVQLLGSNR NELLLKCHVE GASGDLEPLE IEWYRNSEKL STWKNVQLDQ HRLIIRQPGS
EDDGLYRCTA SNAAGRVMSK QGYVYQSSVK CLPRLPRRKN EKMMESWDKQ TFLCRGKRGG
AAGLEALPAA PEDLRIVQGP IGQSIIKEGE PTALTCLYEL PDELKNQRIQ LRWRKDGKLL
RQVELGGSAP IPGHSFDSGK DALLREDARL VLHKQNGTLS FASIIASDAG QYQCQLQLEA
HAPINSSPGI LEVIEQLKFV PQPTSKNLEL DAVVAKVHCK AQGTPTPQVQ WVRDGENTTL
PDHVEVDANG TLIFRNVNSE HRGNYTCLAT NSQGQINATV AINVVVTPKF SVPPVGPIET
SEQGTVVMHC QAIGDPKPTI QWDKDLKYLS ENNTDRERFR FLENGTLEIR NVQVEDEGSY
GCTIGNSAGL KREDVQLVVK TTGDGFAPEE SGGDGFLVTR AVLITMTVAL AYIVLVVGLM
LWCRYRRQAR KARLNDLSTK EAGGDQPDVA GNGKGSEQEP CLSKQHNGHS KSRSKSSGDA
QKSDDTACSQ QSRASKKSAH IYEQLALPRS GLSELIQIGR GEFGDVFVGK LKATLVTSPS
DKDADTEKQH SNSENGSGGS GSGSTTLSTL NEKRRSKTSM DDIEEIKEEE QDQHNQSGLE
QLVLVKALNK VKDEQACQEF RRQLDLLRAI SHKGVVRLFG LCREKDPHYM VLEYTDWGDL
KQFLLATAGK VNTATAGSSS PPPLTTSQVL AVAYQIARGM DAIYRARFTH RDLATRNCVI
SSEFIVKVSY PALCKDKYSR EYHKHRNTLL PIRWLAPECI QEDEYTTKSD IFAYGVVVWE
LFNQATKLPH EELTNEQVVQ RSQAGSLEWS VAEATPDSLR EILLSCWVSN PKERPSFSQL
GAALSKAMQS AEK
