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   02-SEP-2026, entry version 153.
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,
GN   ECO:0000312|FlyBase:FBgn0004839}; ORFNames=CG8967;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; 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};
RC   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   AlphaFoldDB; Q6AWJ9; -.
DR   SMR; Q6AWJ9; -.
DR   BioGRID; 62067; 10.
DR   FunCoup; Q6AWJ9; 259.
DR   IntAct; Q6AWJ9; 5.
DR   MINT; Q6AWJ9; -.
DR   STRING; 7227.FBpp0087135; -.
DR   GlyCosmos; Q6AWJ9; 8 sites, No reported glycans.
DR   GlyGen; Q6AWJ9; 8 sites.
DR   iPTMnet; Q6AWJ9; -.
DR   PaxDb; 7227-FBpp0087135; -.
DR   PeptideAtlas; Q6AWJ9; -.
DR   DNASU; 36283; -.
DR   EnsemblMetazoa; FBtr0088028; FBpp0087135; FBgn0004839.
DR   GeneID; 36283; -.
DR   KEGG; dme:Dmel_CG8967; -.
DR   UCSC; CG8967-RA; d. melanogaster.
DR   AGR; FB:FBgn0004839; -.
DR   CTD; 36283; -.
DR   FlyBase; FBgn0004839; otk.
DR   VEuPathDB; VectorBase:FBgn0004839; -.
DR   eggNOG; KOG1026; Eukaryota.
DR   eggNOG; KOG4475; Eukaryota.
DR   HOGENOM; CLU_012268_0_0_1; -.
DR   InParanoid; Q6AWJ9; -.
DR   OMA; SHLHIEA; -.
DR   OrthoDB; 2413561at2759; -.
DR   PhylomeDB; Q6AWJ9; -.
DR   Reactome; R-DME-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-DME-210991; Basigin interactions.
DR   Reactome; R-DME-216083; Integrin cell surface interactions.
DR   Reactome; R-DME-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR   Reactome; R-DME-433692; Proton-coupled monocarboxylate transport.
DR   Reactome; R-DME-9749641; Aspirin ADME.
DR   SignaLink; Q6AWJ9; -.
DR   BioGRID-ORCS; 36283; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 36283; -.
DR   PRO; PR:Q6AWJ9; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0004839; Expressed in escort cell (Drosophila) in ovary and 61 other cell types or tissues.
DR   ExpressionAtlas; Q6AWJ9; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:FlyBase.
DR   GO; GO:0016020; C: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:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
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:0004888; F:transmembrane signaling receptor activity; IGI: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:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell-cell adhesion; IBA:GO_Central.
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   CDD; cd00096; Ig; 2.
DR   CDD; cd05046; PTK_CCK4; 1.
DR   FunFam; 1.10.510.10:FF:000954; Tyrosine-protein kinase-like otk; 1.
DR   FunFam; 2.60.40.10:FF:001805; Tyrosine-protein kinase-like otk; 1.
DR   FunFam; 2.60.40.10:FF:002027; Tyrosine-protein kinase-like otk; 1.
DR   FunFam; 2.60.40.10:FF:002086; Tyrosine-protein kinase-like otk; 1.
DR   FunFam; 2.60.40.10:FF:002809; Tyrosine-protein kinase-like otk; 1.
DR   FunFam; 3.30.200.20:FF:001776; Tyrosine-protein kinase-like otk; 1.
DR   FunFam; 2.60.40.10:FF:002127; tyrosine-protein kinase-like otk; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR050122; RTK.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   PANTHER; PTHR24416:SF349; TYROSINE-PROTEIN KINASE RYK; 1.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF13927; Ig_3; 1.
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; Immunoglobulin; 4.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 5.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PDBsum; 6S9F; -.
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        655..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..731
FT                   /note="Basic and acidic 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   HELIX           247..251
FT                   /evidence="ECO:0007829|PDB:6S9F"
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   HELIX           366..368
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
//