MGM1_YEAST
ID MGM1_YEAST Reviewed; 881 AA.
AC P32266; D6W2R7; Q02609; Q08627;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Dynamin-like GTPase MGM1, mitochondrial;
DE AltName: Full=Mitochondrial division and morphology protein 17;
DE AltName: Full=Mitochondrial genome maintenance protein 1;
DE Contains:
DE RecName: Full=Dynamin-like GTPase MGM1 large isoform;
DE Short=l-MGM1;
DE Contains:
DE RecName: Full=Dynamin-like GTPase MGM1 small isoform;
DE Short=s-MGM1;
DE Flags: Precursor;
GN Name=MGM1; Synonyms=MDM17; OrderedLocusNames=YOR211C; ORFNames=YOR50-1;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BJ41-8C;
RX PubMed=1532158; DOI=10.1101/gad.6.3.380;
RA Jones B.A., Fangman W.L.;
RT "Mitochondrial DNA maintenance in yeast requires a protein containing a
RT region related to the GTP-binding domain of dynamin.";
RL Genes Dev. 6:380-389(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7916673; DOI=10.1007/bf00324678;
RA Guan K., Farh L., Marshall T., Deschenes R.J.;
RT "Normal mitochondrial structure and genome maintenance in yeast requires
RT the dynamin-like product of the MGM1 gene.";
RL Curr. Genet. 24:141-148(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-784.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840505;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA Galisson F., Dujon B.;
RT "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT XV of the yeast Saccharomyces cerevisiae.";
RL Yeast 12:877-885(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 713-881.
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=8516295; DOI=10.1073/pnas.90.12.5524;
RA Lalo D., Carles C., Sentenac A., Thuriaux P.;
RT "Interactions between three common subunits of yeast RNA polymerases I and
RT III.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5524-5528(1993).
RN [7]
RP PROTEIN SEQUENCE OF 60-67 AND 140-147, FUNCTION, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=12707284; DOI=10.1074/jbc.m211311200;
RA Herlan M., Vogel F., Bornhoevd C., Neupert W., Reichert A.S.;
RT "Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for
RT maintenance of mitochondrial morphology and of mitochondrial DNA.";
RL J. Biol. Chem. 278:27781-27788(2003).
RN [8]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF SER-224 AND GLU-294, AND IDENTIFICATION
RP OF THE TRANSLATION INITIATION CODON.
RX PubMed=10037792; DOI=10.1083/jcb.144.4.711;
RA Shepard K.A., Yaffe M.P.;
RT "The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial
RT outer membrane to mediate mitochondrial inheritance.";
RL J. Cell Biol. 144:711-720(1999).
RN [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-223;
RP SER-224; THR-244; ARG-824 AND LYS-854.
RX PubMed=12566426; DOI=10.1083/jcb.200209015;
RA Wong E.D., Wagner J.A., Scott S.V., Okreglak V., Holewinske T.J.,
RA Cassidy-Stone A., Nunnari J.;
RT "The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a
RT protein complex that mediates mitochondrial fusion.";
RL J. Cell Biol. 160:303-311(2003).
RN [10]
RP INTERACTION WITH FZO1 AND UGO1.
RX PubMed=12808034; DOI=10.1091/mbc.e02-12-0788;
RA Sesaki H., Southard S.M., Yaffe M.P., Jensen R.E.;
RT "Mgm1p, a dynamin-related GTPase, is essential for fusion of the
RT mitochondrial outer membrane.";
RL Mol. Biol. Cell 14:2342-2356(2003).
RN [11]
RP FUNCTION, AND INTERACTION WITH UGO1.
RX PubMed=15087460; DOI=10.1074/jbc.m401363200;
RA Sesaki H., Jensen R.E.;
RT "Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion.";
RL J. Biol. Chem. 279:28298-28303(2004).
RN [12]
RP PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-79.
RX PubMed=15096522; DOI=10.1083/jcb.200403022;
RA Herlan M., Bornhoevd C., Hell K., Neupert W., Reichert A.S.;
RT "Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP
RT and a functional import motor.";
RL J. Cell Biol. 165:167-173(2004).
RN [13]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
CC -!- FUNCTION: Dynamin-related GTPase required for mitochondrial fusion.
CC Coordinates interaction between the inner and outer mitochondrial
CC membrane to promote the formation of the double membrane.
CC {ECO:0000269|PubMed:10037792, ECO:0000269|PubMed:12566426,
CC ECO:0000269|PubMed:12707284, ECO:0000269|PubMed:15087460}.
CC -!- SUBUNIT: Homooligomer. Associates with FZO1 through interaction with
CC the intermembrane space domain of UGO1 which binds FZO1 through its
CC cytoplasmic domain. {ECO:0000269|PubMed:10037792,
CC ECO:0000269|PubMed:12566426, ECO:0000269|PubMed:16407407}.
CC -!- INTERACTION:
CC P32266; P38297: FZO1; NbExp=2; IntAct=EBI-10865, EBI-20900;
CC P32266; Q03327: UGO1; NbExp=2; IntAct=EBI-10865, EBI-32955;
CC -!- SUBCELLULAR LOCATION: [Dynamin-like GTPase MGM1 large isoform]:
CC Mitochondrion inner membrane {ECO:0000269|PubMed:15096522}; Single-pass
CC type II membrane protein {ECO:0000255}; Intermembrane side
CC {ECO:0000305|PubMed:15096522}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289}.
CC -!- SUBCELLULAR LOCATION: [Dynamin-like GTPase MGM1 small isoform]:
CC Mitochondrion inner membrane {ECO:0000269|PubMed:15096522}; Peripheral
CC membrane protein {ECO:0000269|PubMed:15096522}; Intermembrane side.
CC -!- PTM: Cleavage of the transit peptide by mitochondrial processing
CC protease (MPP) produces a long integral membrane form of MGM1 (l-MGM1).
CC Further processing by the rhomboid protease PCP1 produces a short
CC peripheral membrane form of MGM1 (s-MGM1). Both isoforms are required
CC for full activity. {ECO:0000269|PubMed:15096522}.
CC -!- MISCELLANEOUS: Deletion of MGM1 causes the mitochondria to fragment and
CC aggregate, and subsequently to lose their mitochondrial DNA and become
CC respiration deficient.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA44637.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA63174.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA99426.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA99428.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X62834; CAA44637.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L07419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z75119; CAA99426.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z75120; CAA99428.1; ALT_INIT; Genomic_DNA.
DR EMBL; X92441; CAA63174.1; ALT_INIT; Genomic_DNA.
DR EMBL; L11274; AAB59316.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10983.1; -; Genomic_DNA.
DR PIR; S33918; S33918.
DR RefSeq; NP_014854.2; NM_001183630.1.
DR PDB; 6JSJ; X-ray; 3.20 A; A/B/C=184-881.
DR PDBsum; 6JSJ; -.
DR AlphaFoldDB; P32266; -.
DR SMR; P32266; -.
DR BioGRID; 34606; 240.
DR ComplexPortal; CPX-161; FZO1-MGM1-UGO1 complex.
DR DIP; DIP-8008N; -.
DR IntAct; P32266; 6.
DR MINT; P32266; -.
DR STRING; 4932.YOR211C; -.
DR TCDB; 1.N.6.1.1; the mitochondrial inner/outer membrane fusion (mmf) family.
DR iPTMnet; P32266; -.
DR MaxQB; P32266; -.
DR PaxDb; P32266; -.
DR PRIDE; P32266; -.
DR EnsemblFungi; YOR211C_mRNA; YOR211C; YOR211C.
DR GeneID; 854386; -.
DR KEGG; sce:YOR211C; -.
DR SGD; S000005737; MGM1.
DR VEuPathDB; FungiDB:YOR211C; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00550000074851; -.
DR HOGENOM; CLU_008640_0_1_1; -.
DR InParanoid; P32266; -.
DR OMA; PLKMGYV; -.
DR BioCyc; YEAST:G3O-33713-MON; -.
DR Reactome; R-SCE-169911; Regulation of Apoptosis.
DR Reactome; R-SCE-196025; Formation of annular gap junctions.
DR PRO; PR:P32266; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32266; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030061; C:mitochondrial crista; IDA:SGD.
DR GO; GO:0097002; C:mitochondrial inner boundary membrane; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:1901612; F:cardiolipin binding; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:SGD.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:SGD.
DR GO; GO:0015886; P:heme transport; IMP:SGD.
DR GO; GO:0061025; P:membrane fusion; IDA:SGD.
DR GO; GO:0008053; P:mitochondrial fusion; IDA:UniProtKB.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IDA:UniProtKB.
DR GO; GO:1990627; P:mitochondrial inner membrane fusion; IMP:ComplexPortal.
DR GO; GO:0007006; P:mitochondrial membrane organization; IDA:UniProtKB.
DR GO; GO:1990626; P:mitochondrial outer membrane fusion; IMP:ComplexPortal.
DR GO; GO:0000001; P:mitochondrion inheritance; IDA:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; GTP-binding; Hydrolase; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Signal-anchor; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:12707284"
FT CHAIN 60..881
FT /note="Dynamin-like GTPase MGM1 large isoform"
FT /id="PRO_0000007400"
FT CHAIN 140..881
FT /note="Dynamin-like GTPase MGM1 small isoform"
FT /id="PRO_0000007401"
FT TOPO_DOM 60..72
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..92
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..881
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 207..505
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 780..872
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 145..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..224
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 243..245
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 317..320
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 385..388
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 414..417
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COMPBIAS 161..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 217..224
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 317..321
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 385..388
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MUTAGEN 1
FT /note="M->A: Abolishes translation."
FT MUTAGEN 39
FT /note="M->A: No effect on translation."
FT MUTAGEN 79
FT /note="G->D,K: Loss of function; most MGM1 processed to s-
FT MGM1."
FT /evidence="ECO:0000269|PubMed:15096522"
FT MUTAGEN 81
FT /note="M->A: No effect on translation."
FT MUTAGEN 92
FT /note="M->A: No effect on translation."
FT MUTAGEN 223
FT /note="K->A: Loss of stability."
FT /evidence="ECO:0000269|PubMed:12566426"
FT MUTAGEN 224
FT /note="S->A: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:10037792,
FT ECO:0000269|PubMed:12566426"
FT MUTAGEN 224
FT /note="S->N: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:10037792,
FT ECO:0000269|PubMed:12566426"
FT MUTAGEN 244
FT /note="T->A: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:12566426"
FT MUTAGEN 294
FT /note="E->K: In mdm17; loss of function at 37 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:10037792"
FT MUTAGEN 824
FT /note="R->A: Loss of GED function."
FT /evidence="ECO:0000269|PubMed:12566426"
FT MUTAGEN 854
FT /note="K->A: Loss of GED function."
FT /evidence="ECO:0000269|PubMed:12566426"
FT CONFLICT 4
FT /note="S -> T (in Ref. 1; CAA44637)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="G -> C (in Ref. 1; CAA44637)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="E -> A (in Ref. 2; L07419)"
FT /evidence="ECO:0000305"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6JSJ"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 365..373
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 375..384
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 392..399
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 457..473
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 485..502
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 504..525
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 533..553
FT /evidence="ECO:0007829|PDB:6JSJ"
FT TURN 554..557
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 558..578
FT /evidence="ECO:0007829|PDB:6JSJ"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 586..590
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 598..615
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 619..640
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 643..646
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 648..663
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 666..676
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 677..680
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 688..720
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 722..733
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 748..775
FT /evidence="ECO:0007829|PDB:6JSJ"
FT STRAND 780..783
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 787..809
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 811..827
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 831..839
FT /evidence="ECO:0007829|PDB:6JSJ"
FT HELIX 842..871
FT /evidence="ECO:0007829|PDB:6JSJ"
SQ SEQUENCE 881 AA; 99178 MW; 31524B40C5350096 CRC64;
MNASPVRLLI LRRQLATHPA ILYSSPYIKS PLVHLHSRMS NVHRSAHANA LSFVITRRSI
SHFPKIISKI IRLPIYVGGG MAAAGSYIAY KMEEASSFTK DKLDRIKDLG ESMKEKFNKM
FSGDKSQDGG HGNDGTVPTA TLIAATSLDD DESKRQGDPK DDDDEDDDDE DDENDSVDTT
QDEMLNLTKQ MIEIRTILNK VDSSSAHLTL PSIVVIGSQS SGKSSVLESI VGREFLPKGS
NMVTRRPIEL TLVNTPNSNN VTADFPSMRL YNIKDFKEVK RMLMELNMAV PTSEAVSEEP
IQLTIKSSRV PDLSLVDLPG YIQVEAADQP IELKTKIRDL CEKYLTAPNI ILAISAADVD
LANSSALKAS KAADPKGLRT IGVITKLDLV DPEKARSILN NKKYPLSMGY VGVITKTPSS
INRKHLGLFG EAPSSSLSGI FSKGQHGQSS GEENTNGLKQ IVSHQFEKAY FKENKKYFTN
CQVSTKKLRE KLIKILEISM SNALEPTSTL IQQELDDTSY LFKVEFNDRH LTPKSYLLNN
IDVLKLGIKE FQEKFHRNEL KSILRAELDQ KVLDVLATRY WKDDNLQDLS SSKLESDTDM
LYWHKKLELA SSGLTKMGIG RLSTMLTTNA ILKELDNILE STQLKNHELI KDLVSNTAIN
VLNSKYYSTA DQVENCIKPF KYEIDLEERD WSLARQHSIN LIKEELRQCN SRYQAIKNAV
GSKKLANVMG YLENESNLQK ETLGMSKLLL ERGSEAIFLD KRCKVLSFRL KMLKNKCHST
IEKDRCPEVF LSAVSDKLTS TAVLFLNVEL LSDFFYNFPI ELDRRLTLLG DEQVEMFAKE
DPKISRHIEL QKRKELLELA LEKIDSILVF KKSYKGVSKN L
