MIRO_DROME
ID MIRO_DROME Reviewed; 652 AA.
AC Q8IMX7; Q8IMX6; Q95TT1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Mitochondrial Rho GTPase;
DE Short=Miro;
DE Short=dMiro;
DE EC=3.6.5.-;
GN Name=Miro; ORFNames=CG5410;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-652 (ISOFORM A).
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16055062; DOI=10.1016/j.neuron.2005.06.027;
RA Guo X., Macleod G.T., Wellington A., Hu F., Panchumarthi S.,
RA Schoenfield M., Marin L., Charlton M.P., Atwood H.L., Zinsmaier K.E.;
RT "The GTPase dMiro is required for axonal transport of mitochondria to
RT Drosophila synapses.";
RL Neuron 47:379-393(2005).
RN [6]
RP INTERACTION WITH MILT.
RX PubMed=14605208; DOI=10.1126/science.1090289;
RA Giot L., Bader J.S., Brouwer C., Chaudhuri A., Kuang B., Li Y., Hao Y.L.,
RA Ooi C.E., Godwin B., Vitols E., Vijayadamodar G., Pochart P., Machineni H.,
RA Welsh M., Kong Y., Zerhusen B., Malcolm R., Varrone Z., Collis A.,
RA Minto M., Burgess S., McDaniel L., Stimpson E., Spriggs F., Williams J.,
RA Neurath K., Ioime N., Agee M., Voss E., Furtak K., Renzulli R.,
RA Aanensen N., Carrolla S., Bickelhaupt E., Lazovatsky Y., DaSilva A.,
RA Zhong J., Stanyon C.A., Finley R.L. Jr., White K.P., Braverman M.,
RA Jarvie T., Gold S., Leach M., Knight J., Shimkets R.A., McKenna M.P.,
RA Chant J., Rothberg J.M.;
RT "A protein interaction map of Drosophila melanogaster.";
RL Science 302:1727-1736(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH MILT.
RX PubMed=16717129; DOI=10.1083/jcb.200601067;
RA Glater E.E., Megeath L.J., Stowers R.S., Schwarz T.L.;
RT "Axonal transport of mitochondria requires milton to recruit kinesin heavy
RT chain and is light chain independent.";
RL J. Cell Biol. 173:545-557(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22396657; DOI=10.1371/journal.pgen.1002537;
RA Liu S., Sawada T., Lee S., Yu W., Silverio G., Alapatt P., Millan I.,
RA Shen A., Saxton W., Kanao T., Takahashi R., Hattori N., Imai Y., Lu B.;
RT "Parkinson's disease-associated kinase PINK1 regulates Miro protein level
RT and axonal transport of mitochondria.";
RL PLoS Genet. 8:E1002537-E1002537(2012).
RN [9]
RP FUNCTION, INTERACTION WITH VIMAR, AND DISRUPTION PHENOTYPE.
RX PubMed=27716788; DOI=10.1371/journal.pgen.1006359;
RA Ding L., Lei Y., Han Y., Li Y., Ji X., Liu L.;
RT "Vimar Is a Novel Regulator of Mitochondrial Fission through Miro.";
RL PLoS Genet. 12:e1006359-e1006359(2016).
CC -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking
CC (PubMed:16055062, PubMed:16717129, PubMed:22396657). Forms an essential
CC protein complex with Milt that links Khc to mitochondria for light
CC chain-independent, anterograde transport of mitochondria
CC (PubMed:16717129). Required for axonal transport to synapses within
CC nerve terminals (PubMed:16055062, PubMed:22396657). Required
CC presynaptically but not postsynaptically at neuromuscular junctions
CC (NMJs) (PubMed:16055062). Also involved in the regulation of
CC mitochondrial dynamics by promoting drp1-mediated mitochondrial fission
CC during high calcium conditions, and negatively regulating fission
CC during normal conditions (PubMed:27716788).
CC {ECO:0000269|PubMed:16055062, ECO:0000269|PubMed:16717129,
CC ECO:0000269|PubMed:22396657, ECO:0000269|PubMed:27716788}.
CC -!- SUBUNIT: Interacts with kinesin-associated protein milt
CC (PubMed:14605208, PubMed:16717129). Interacts with vimar
CC (PubMed:27716788). {ECO:0000269|PubMed:14605208,
CC ECO:0000269|PubMed:16717129, ECO:0000269|PubMed:27716788}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000305|PubMed:16055062}; Single-pass type IV membrane protein
CC {ECO:0000305|PubMed:16055062}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=D;
CC IsoId=Q8IMX7-1; Sequence=Displayed;
CC Name=B; Synonyms=E;
CC IsoId=Q8IMX7-2; Sequence=VSP_019165;
CC -!- DISRUPTION PHENOTYPE: Flies die at early pupal stage and exhibit
CC abnormal locomotion (PubMed:16055062). Mitochondria in muscles and
CC neurons are abnormally distributed (PubMed:16055062). Instead of being
CC transported into axons and dendrites, mitochondria accumulate in
CC parallel rows in neuronal somata (PubMed:16055062). Mutant NMJs lack
CC presynaptic mitochondria, but neurotransmitter release and acute Ca(2+)
CC buffering is only impaired during prolonged stimulation
CC (PubMed:16055062). RNAi-mediated knockdown perturbs mitochondrial
CC distribution and dynamics (PubMed:27716788). RNAi-mediated knockdown in
CC the dopaminergic (DA) neurons decreases mitochondrial length and
CC mitochondrial flux, and mitochondria accumulate in the most distal
CC boutons of the DA motor neuron nerve terminals (PubMed:22396657).
CC {ECO:0000269|PubMed:16055062, ECO:0000269|PubMed:22396657,
CC ECO:0000269|PubMed:27716788}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13784.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAN13971.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13972.1; -; Genomic_DNA.
DR EMBL; BT016011; AAV36896.1; -; mRNA.
DR EMBL; AY058555; AAL13784.1; ALT_INIT; mRNA.
DR RefSeq; NP_001262895.1; NM_001275966.1. [Q8IMX7-2]
DR RefSeq; NP_651205.2; NM_142948.4. [Q8IMX7-2]
DR RefSeq; NP_732936.1; NM_170111.3. [Q8IMX7-1]
DR PDB; 4C0J; X-ray; 2.82 A; A=201-617.
DR PDB; 4C0K; X-ray; 2.80 A; A=201-617.
DR PDB; 4C0L; X-ray; 3.00 A; A=201-617.
DR PDBsum; 4C0J; -.
DR PDBsum; 4C0K; -.
DR PDBsum; 4C0L; -.
DR AlphaFoldDB; Q8IMX7; -.
DR SMR; Q8IMX7; -.
DR BioGRID; 67780; 25.
DR IntAct; Q8IMX7; 6.
DR STRING; 7227.FBpp0302814; -.
DR PaxDb; Q8IMX7; -.
DR PRIDE; Q8IMX7; -.
DR DNASU; 42845; -.
DR EnsemblMetazoa; FBtr0084595; FBpp0083980; FBgn0039140. [Q8IMX7-1]
DR EnsemblMetazoa; FBtr0084596; FBpp0083981; FBgn0039140. [Q8IMX7-2]
DR EnsemblMetazoa; FBtr0321262; FBpp0302814; FBgn0039140. [Q8IMX7-2]
DR GeneID; 42845; -.
DR KEGG; dme:Dmel_CG5410; -.
DR CTD; 42845; -.
DR FlyBase; FBgn0039140; Miro.
DR VEuPathDB; VectorBase:FBgn0039140; -.
DR eggNOG; KOG1707; Eukaryota.
DR GeneTree; ENSGT00940000173880; -.
DR HOGENOM; CLU_014255_3_1_1; -.
DR InParanoid; Q8IMX7; -.
DR OMA; HVSVTWN; -.
DR PhylomeDB; Q8IMX7; -.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-9013419; RHOT2 GTPase cycle.
DR Reactome; R-DME-9013425; RHOT1 GTPase cycle.
DR SignaLink; Q8IMX7; -.
DR BioGRID-ORCS; 42845; 0 hits in 3 CRISPR screens.
DR ChiTaRS; cpa; fly.
DR GenomeRNAi; 42845; -.
DR PRO; PR:Q8IMX7; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039140; Expressed in embryonic/larval hemocyte (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q8IMX7; baseline and differential.
DR Genevisible; Q8IMX7; DM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IDA:FlyBase.
DR GO; GO:0003924; F:GTPase activity; ISM:FlyBase.
DR GO; GO:0000287; F:magnesium ion binding; IDA:FlyBase.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IMP:UniProtKB.
DR GO; GO:0019725; P:cellular homeostasis; ISS:UniProtKB.
DR GO; GO:0034643; P:establishment of mitochondrion localization, microtubule-mediated; IMP:FlyBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
DR GO; GO:0051646; P:mitochondrion localization; IMP:FlyBase.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:FlyBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR013566; EF_hand_assoc_1.
DR InterPro; IPR013567; EF_hand_assoc_2.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR021181; Miro.
DR InterPro; IPR020860; MIRO_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF08355; EF_assoc_1; 1.
DR Pfam; PF08356; EF_assoc_2; 1.
DR Pfam; PF00071; Ras; 2.
DR PIRSF; PIRSF037488; Mt_Rho_GTPase; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51423; MIRO; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; GTP-binding; Hydrolase;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..652
FT /note="Mitochondrial Rho GTPase"
FT /id="PRO_0000239327"
FT TOPO_DOM 1..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..641
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..652
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 9..194
FT /note="Miro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT DOMAIN 210..245
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 330..365
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 444..607
FT /note="Miro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 144..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 453..460
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 491..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 558..561
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT VAR_SEQ 608
FT /note="P -> PRFQAAWILFYKHRLVQLWESA (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_019165"
FT HELIX 209..222
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:4C0K"
FT TURN 285..288
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 329..341
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:4C0K"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:4C0K"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 388..401
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 415..419
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 459..464
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:4C0J"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:4C0L"
FT STRAND 484..492
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 495..503
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 515..518
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 520..530
FT /evidence="ECO:0007829|PDB:4C0K"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 535..545
FT /evidence="ECO:0007829|PDB:4C0K"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 568..571
FT /evidence="ECO:0007829|PDB:4C0K"
FT HELIX 573..579
FT /evidence="ECO:0007829|PDB:4C0K"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:4C0J"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:4C0J"
FT HELIX 596..606
FT /evidence="ECO:0007829|PDB:4C0K"
SQ SEQUENCE 652 AA; 73776 MW; 5F2F9623EF6CCB19 CRC64;
MGQYTASQRK NVRILLVGDA GVGKTSLILS LVSEEYPEEV PPRAEEITIP ANVTPEQVPT
SIVDFSAVEQ SEDALAAEIN KAHVVCIVYA VDDDDTLDRI TSHWLPLVRA KCNPSLDGEG
DAEAEAEGDT QREPIRKPIV LVGNKIDLIE YSTMDSVLAI MEDYPEIESC VECSAKSLHN
ISEMFYYAQK AVLHPTSPLY MMEEQELTSA CKKSLVRIFK ICDIDGDNLL NDYELNLFQR
RCFNTPLQPQ ILDEVKAVIQ KNVPDGIYND AVTLKGFLFL HCLFIQRGRN ETTWAVLRRF
GYNDQLEMCQ EYLRPPLKIP PGSSTELSHR GQQFLIAVFE RYDRDGDGAL SPEEHKMLFS
TCPAAPWSYS TDIRKSCPIN ETTGWVTLHG WLCRWTLMTL IDVVKTMEYL AYLGFNVHEN
DSQLAAIHVT RERRIDLAKR QSSRSVYKCH VIGPKGSGKT GMCRGFLVED MHKLIGKEFK
TNVVNCINSV QVYGQEKHLI LRDIDVRHAL DPLQPQEVNC DVACLVYDSS NPRSFEYVAR
IYIKYYAESK IPVMIVGTKC DMDERRQDYL MQPSEFCDKY KLLPPHLFSL KTNKKELYTK
LATMAAFPHL RQFGLMTEDP KLWLKAGLGV AAATMLGFIV LKTISAAGAH TR
