RAB6_DROME
ID RAB6_DROME Reviewed; 208 AA.
AC O18334;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Ras-related protein Rab6 {ECO:0000312|EMBL:AAF53168.1};
DE AltName: Full=Protein warthog {ECO:0000303|PubMed:10459009};
GN Name=Rab6 {ECO:0000312|EMBL:AAF53168.1, ECO:0000312|FlyBase:FBgn0015797};
GN Synonyms=wrt {ECO:0000303|PubMed:10459009}; ORFNames=CG6601;
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:0000312|EMBL:BAA21707.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R {ECO:0000312|EMBL:BAA21707.1};
RC TISSUE=Head {ECO:0000312|EMBL:BAA21707.1};
RX PubMed=9074639; DOI=10.1016/s0014-5793(97)00094-x;
RA Satoh A.K., Tokunaga F., Ozaki K.;
RT "Rab proteins of Drosophila melanogaster: novel members of the Rab-protein
RT family.";
RL FEBS Lett. 404:65-69(1997).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF GLN-71 AND
RP ASN-125.
RX PubMed=9685396; DOI=10.1074/jbc.273.32.20425;
RA Shetty K.M., Kurada P., O'Tousa J.E.;
RT "Rab6 regulation of rhodopsin transport in Drosophila.";
RL J. Biol. Chem. 273:20425-20430(1998).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF ARG-62 AND GLN-71.
RC TISSUE=Embryo {ECO:0000269|PubMed:10459009}, and
RC Imaginal disk {ECO:0000269|PubMed:10459009};
RX PubMed=10459009; DOI=10.1083/jcb.146.4.731;
RA Purcell K., Artavanis-Tsakonas S.;
RT "The developmental role of warthog, the notch modifier encoding Drab6.";
RL J. Cell Biol. 146:731-740(1999).
RN [4] {ECO:0000312|EMBL:AAF53168.1}
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 [5] {ECO:0000312|EMBL:AAF53168.1}
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 [6] {ECO:0000312|EMBL:AAL25300.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL25300.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH BICD.
RX PubMed=17329360; DOI=10.1242/dev.02821;
RA Coutelis J.B., Ephrussi A.;
RT "Rab6 mediates membrane organization and determinant localization during
RT Drosophila oogenesis.";
RL Development 134:1419-1430(2007).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BICD.
RX PubMed=17827179; DOI=10.1242/dev.008078;
RA Januschke J., Nicolas E., Compagnon J., Formstecher E., Goud B.,
RA Guichet A.;
RT "Rab6 and the secretory pathway affect oocyte polarity in Drosophila.";
RL Development 134:3419-3425(2007).
RN [9] {ECO:0000305}
RP INTERACTION WITH GCC1/CG10703 AND CBS.
RX PubMed=19001129; DOI=10.1083/jcb.200808018;
RA Sinka R., Gillingham A.K., Kondylis V., Munro S.;
RT "Golgi coiled-coil proteins contain multiple binding sites for Rab family G
RT proteins.";
RL J. Cell Biol. 183:607-615(2008).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=18833296; DOI=10.1371/journal.ppat.1000168;
RA Jin L.H., Shim J., Yoon J.S., Kim B., Kim J., Kim-Ha J., Kim Y.J.;
RT "Identification and functional analysis of antifungal immune response genes
RT in Drosophila.";
RL PLoS Pathog. 4:E1000168-E1000168(2008).
RN [11] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=22000105; DOI=10.1016/j.cub.2011.08.058;
RA Chan C.C., Scoggin S., Wang D., Cherry S., Dembo T., Greenberg B.,
RA Jin E.J., Kuey C., Lopez A., Mehta S.Q., Perkins T.J., Brankatschk M.,
RA Rothenfluh A., Buszczak M., Hiesinger P.R.;
RT "Systematic discovery of Rab GTPases with synaptic functions in
RT Drosophila.";
RL Curr. Biol. 21:1704-1715(2011).
RN [12] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RICH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-26 AND GLN-71.
RX PubMed=21835342; DOI=10.1016/j.neuron.2011.06.040;
RA Tong C., Ohyama T., Tien A.C., Rajan A., Haueter C.M., Bellen H.J.;
RT "Rich regulates target specificity of photoreceptor cells and N-cadherin
RT trafficking in the Drosophila visual system via Rab6.";
RL Neuron 71:447-459(2011).
RN [13] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH ACT5C.
RX PubMed=22928698; DOI=10.1021/pr300274k;
RA Ye T., Tang W., Zhang X.;
RT "Involvement of Rab6 in the regulation of phagocytosis against virus
RT infection in invertebrates.";
RL J. Proteome Res. 11:4834-4846(2012).
RN [14]
RP FUNCTION, AND INTERACTION WITH GORAB.
RX PubMed=33704067; DOI=10.7554/elife.57241;
RA Fatalska A., Stepinac E., Richter M., Kovacs L., Pietras Z., Puchinger M.,
RA Dong G., Dadlez M., Glover D.M.;
RT "The dimeric Golgi protein Gorab binds to Sas6 as a monomer to mediate
RT centriole duplication.";
RL Elife 10:0-0(2021).
RN [15] {ECO:0000312|PDB:2Y8E}
RP X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 1-177 IN COMPLEX WITH GTP-ANALOG.
RX PubMed=21795785; DOI=10.1107/s1744309111017453;
RA Walden M., Jenkins H.T., Edwards T.A.;
RT "Structure of the Drosophila melanogaster Rab6 GTPase at 1.4A resolution.";
RL Acta Crystallogr. F 67:744-748(2011).
CC -!- FUNCTION: Protein transport (PubMed:17329360, PubMed:17827179,
CC PubMed:18833296, PubMed:21835342, PubMed:22928698, PubMed:33704067,
CC PubMed:9685396). Regulator of membrane traffic from the Golgi apparatus
CC towards the endoplasmic reticulum (ER) (PubMed:21795785). Mediates
CC membrane trafficking during egg chamber growth and organization,
CC possibly upstream of exocyst component Sec5. Also during oogenesis,
CC plays a role, together with BicD but independently of Sec5, in the
CC polarization of the oocyte microtubule cytoskeleton, in the
CC localization of oskar mRNA and in the anterodorsal secretion of grk.
CC Required for anterograde opsin transport through the ER-Golgi complex.
CC Plays a role, together with Rich, in regulating CadN transport in
CC photoreceptor cells which is required for the formation of normal
CC synaptic connections between axons from the inner photoreceptor cells
CC in the eye and postsynaptic cells in the brain medulla layer M6
CC (PubMed:21835342). Necessary for proper development of bristle shafts
CC of macrochaete and microchaete on the head, thorax and scutellum.
CC Modulates Notch signaling (PubMed:10459009). As a key regulator of
CC vesicular traffic, plays a critical role in the regulation of actin
CC organization and is required for normal rates of phagocytic uptake
CC during phagocytosis involved in defense against viral and fungal
CC infection. {ECO:0000269|PubMed:10459009, ECO:0000269|PubMed:17329360,
CC ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:18833296,
CC ECO:0000269|PubMed:21795785, ECO:0000269|PubMed:21835342,
CC ECO:0000269|PubMed:22928698, ECO:0000269|PubMed:33704067,
CC ECO:0000269|PubMed:9685396}.
CC -!- SUBUNIT: Interacts with Rich and Act5C (PubMed:21835342,
CC PubMed:22928698). Interacts with BicD (via C-terminal domain)
CC (PubMed:17329360, PubMed:17827179). Interacts (in GTP-bound) with
CC GCC1/CG10703 and cbs (PubMed:19001129). Interacts with Gorab (via C-
CC terminus); binds to a Gorab homodimer, this interaction seems to be
CC required for trans-Golgi localization of Gorab (PubMed:33704067).
CC {ECO:0000269|PubMed:17329360, ECO:0000269|PubMed:17827179,
CC ECO:0000269|PubMed:19001129, ECO:0000269|PubMed:21835342,
CC ECO:0000269|PubMed:22928698, ECO:0000269|PubMed:33704067}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342,
CC ECO:0000269|PubMed:22000105}. Synapse {ECO:0000269|PubMed:17827179,
CC ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}. Perikaryon
CC {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342,
CC ECO:0000269|PubMed:22000105}. Note=Colocalizes with Rich at the Golgi
CC apparatus. During oogenesis, first accumulates transiently in a central
CC position during stages 7-8, then is uniformly distributed at the
CC beginning of stage 9 to end up juxtaposed to the entire oocyte cortex.
CC {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342,
CC ECO:0000269|PubMed:22000105}.
CC -!- TISSUE SPECIFICITY: Expressed in larval eye, wing and leg imaginal
CC disks and in salivary gland. Expressed in the larval optic lobe,
CC showing an enrichment in the neuropil. In the adult brain, expressed in
CC photoreceptors and mushroom body. {ECO:0000269|PubMed:21835342,
CC ECO:0000269|PubMed:22000105}.
CC -!- DISRUPTION PHENOTYPE: Larval lethal. {ECO:0000269|PubMed:10459009,
CC ECO:0000269|PubMed:21835342}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000255}.
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DR EMBL; D84314; BAA21707.1; -; mRNA.
DR EMBL; AE014134; AAF53168.1; -; Genomic_DNA.
DR EMBL; AY060261; AAL25300.1; -; mRNA.
DR RefSeq; NP_001285869.1; NM_001298940.1.
DR RefSeq; NP_477172.1; NM_057824.5.
DR PDB; 2Y8E; X-ray; 1.39 A; A/B=1-177.
DR PDBsum; 2Y8E; -.
DR AlphaFoldDB; O18334; -.
DR SMR; O18334; -.
DR BioGRID; 60686; 85.
DR STRING; 7227.FBpp0079943; -.
DR PaxDb; O18334; -.
DR PRIDE; O18334; -.
DR EnsemblMetazoa; FBtr0080361; FBpp0079943; FBgn0015797.
DR EnsemblMetazoa; FBtr0346437; FBpp0312096; FBgn0015797.
DR GeneID; 34636; -.
DR KEGG; dme:Dmel_CG6601; -.
DR UCSC; CG6601-RA; d. melanogaster.
DR CTD; 34636; -.
DR FlyBase; FBgn0015797; Rab6.
DR VEuPathDB; VectorBase:FBgn0015797; -.
DR eggNOG; KOG0094; Eukaryota.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; O18334; -.
DR OMA; PVSNDGC; -.
DR OrthoDB; 1277051at2759; -.
DR PhylomeDB; O18334; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-6811438; Intra-Golgi traffic.
DR Reactome; R-DME-8854214; TBC/RABGAPs.
DR Reactome; R-DME-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 34636; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; O18334; -.
DR GenomeRNAi; 34636; -.
DR PRO; PR:O18334; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0015797; Expressed in saliva-secreting gland and 37 other tissues.
DR ExpressionAtlas; O18334; baseline and differential.
DR Genevisible; O18334; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005776; C:autophagosome; IDA:FlyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; HDA:FlyBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; HDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IGI:FlyBase.
DR GO; GO:0050832; P:defense response to fungus; IMP:FlyBase.
DR GO; GO:0006887; P:exocytosis; IMP:FlyBase.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0140450; P:protein targeting to Golgi apparatus; IMP:UniProtKB.
DR GO; GO:0045467; P:R7 cell development; IMP:FlyBase.
DR GO; GO:0032482; P:Rab protein signal transduction; ISS:FlyBase.
DR GO; GO:0001881; P:receptor recycling; IMP:FlyBase.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IMP:FlyBase.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ER-Golgi transport; Golgi apparatus;
KW GTP-binding; Membrane; Nucleotide-binding; Reference proteome; Synapse;
KW Transport.
FT CHAIN 1..208
FT /note="Ras-related protein Rab6"
FT /id="PRO_0000425445"
FT REGION 176..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..49
FT /note="Effector region"
FT /evidence="ECO:0000250|UniProtKB:P20340"
FT COMPBIAS 182..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 155..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MUTAGEN 26
FT /note="T->N: Does not affect interaction with Rich."
FT /evidence="ECO:0000269|PubMed:21835342"
FT MUTAGEN 62
FT /note="R->C: Produces short bristles but does not alter the
FT direction of their growth."
FT /evidence="ECO:0000269|PubMed:10459009"
FT MUTAGEN 71
FT /note="Q->L: Impairs maturation of ninaE and Rh3. Causes
FT accumulation of membranes at the base of the rhabdomeres
FT and retinal degeneration. Abolishes interaction with Rich.
FT Alters direction of bristle growth and produces aberrations
FT in the circumferential ridges."
FT /evidence="ECO:0000269|PubMed:10459009,
FT ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:9685396"
FT MUTAGEN 125
FT /note="N->I: Does not affect maturation of ninaE or Rh3.
FT Does not cause accumulation of membranes at the base of the
FT rhabdomeres or retinal degeneration."
FT /evidence="ECO:0000269|PubMed:9685396"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:2Y8E"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:2Y8E"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:2Y8E"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:2Y8E"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:2Y8E"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:2Y8E"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2Y8E"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:2Y8E"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:2Y8E"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:2Y8E"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:2Y8E"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:2Y8E"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:2Y8E"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:2Y8E"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:2Y8E"
SQ SEQUENCE 208 AA; 23480 MW; 5812E7A7CB16B133 CRC64;
MSSGDFGNPL RKFKLVFLGE QSVGKTSLIT RFMYDSFDNT YQATIGIDFL SKTMYLEDRT
VRLQLWDTAG QERFRSLIPS YIRDSTVAVV VYDITNTNSF HQTSKWIDDV RTERGSDVII
MLVGNKTDLS DKRQVSTEEG ERKAKELNVM FIETSAKAGY NVKQLFRRVA AALPGMDSTE
NKPSEDMQEV VLKDSPNETK DPEGGCAC
