FLOT_BACSU
ID FLOT_BACSU Reviewed; 509 AA.
AC O32076;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Flotillin-like protein FloT {ECO:0000303|PubMed:20713508};
DE AltName: Full=Bacterial flotillin homolog YuaG {ECO:0000303|PubMed:19383680};
GN Name=floT {ECO:0000303|PubMed:20713508};
GN Synonyms=yuaG {ECO:0000303|PubMed:19383680}, yuaH;
GN OrderedLocusNames=BSU31010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=19383680; DOI=10.1099/mic.0.025312-0;
RA Donovan C., Bramkamp M.;
RT "Characterization and subcellular localization of a bacterial flotillin
RT homologue.";
RL Microbiology 155:1786-1799(2009).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=22753055; DOI=10.1128/jb.00910-12;
RA Dempwolff F., Moeller H.M., Graumann P.L.;
RT "Synthetic motility and cell shape defects associated with deletions of
RT flotillin/reggie paralogs in Bacillus subtilis and interplay of these
RT proteins with NfeD proteins.";
RL J. Bacteriol. 194:4652-4661(2012).
RN [5]
RP INTERACTION WITH FTSH, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=23249255; DOI=10.1186/1471-2180-12-298;
RA Dempwolff F., Wischhusen H.M., Specht M., Graumann P.L.;
RT "The deletion of bacterial dynamin and flotillin genes results in
RT pleiotrophic effects on cell division, cell growth and in cell shape
RT maintenance.";
RL BMC Microbiol. 12:298-298(2012).
RN [7]
RP FUNCTION, SUBUNIT, INTERACTION WITH FLOA; FTSH; FTSX; OPPA; SDHA AND SECY,
RP SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
RN [8]
RP FUNCTION IN CELL DIVISION, AND FUNCTION IN DIFFERENTIATION.
RX PubMed=24222488; DOI=10.1128/mbio.00719-13;
RA Mielich-Suess B., Schneider J., Lopez D.;
RT "Overproduction of flotillin influences cell differentiation and shape in
RT Bacillus subtilis.";
RL MBio 4:0-0(2013).
RN [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=26842743; DOI=10.4161/cib.29578;
RA Dempwolff F., Graumann P.L.;
RT "Genetic links between bacterial dynamin and flotillin proteins.";
RL Commun. Integr. Biol. 7:0-0(2014).
RN [10]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND DOMAIN.
RC STRAIN=168;
RX PubMed=25635948; DOI=10.1371/journal.pone.0116750;
RA Bach J.N., Bramkamp M.;
RT "Dissecting the molecular properties of prokaryotic flotillins.";
RL PLoS ONE 10:e0116750-e0116750(2015).
RN [11]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION IN STATIONARY PHASE, AND
RP MUTAGENESIS OF 342-ALA--ALA-344; 357-ALA--GLU-360; 370-ALA--GLU-373 AND
RP 390-ALA--ALA-394.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=25909364; DOI=10.1371/journal.pgen.1005140;
RA Schneider J., Klein T., Mielich-Suess B., Koch G., Franke C., Kuipers O.P.,
RA Kovacs A.T., Sauer M., Lopez D.;
RT "Spatio-temporal remodeling of functional membrane microdomains organizes
RT the signaling networks of a bacterium.";
RL PLoS Genet. 11:e1005140-e1005140(2015).
RN [12]
RP FUNCTION, INTERACTION WITH FLOA; FTSH; KINC; KIND AND RESE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=26297017; DOI=10.1099/mic.0.000137;
RA Schneider J., Mielich-Suess B., Boehme R., Lopez D.;
RT "In vivo characterization of the scaffold activity of flotillin on the
RT membrane kinase KinC of Bacillus subtilis.";
RL Microbiology 161:1871-1887(2015).
RN [13]
RP FUNCTION, COLOCALIZATION WITH NFED2, AND SUBCELLULAR LOCATION.
RC STRAIN=168, and 168 / PY79;
RX PubMed=27362352; DOI=10.1371/journal.pgen.1006116;
RA Dempwolff F., Schmidt F.K., Hervas A.B., Stroh A., Roesch T.C., Riese C.N.,
RA Dersch S., Heimerl T., Lucena D., Huelsbusch N., Stuermer C.A.,
RA Takeshita N., Fischer R., Eckhardt B., Graumann P.L.;
RT "Super Resolution Fluorescence Microscopy and Tracking of Bacterial
RT Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein
RT Microdomains within the Bacterial Membrane but Absence of Clusters
RT Containing Detergent-Resistant Proteins.";
RL PLoS Genet. 12:e1006116-e1006116(2016).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=32662773; DOI=10.7554/elife.57179;
RA Zielinska A., Savietto A., de Sousa Borges A., Martinez D., Berbon M.,
RA Roelofsen J.R., Hartman A.M., de Boer R., Van der Klei I.J., Hirsch A.K.,
RA Habenstein B., Bramkamp M., Scheffers D.J.;
RT "Flotillin-mediated membrane fluidity controls peptidoglycan synthesis and
RT MreB movement.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Found in functional membrane microdomains (FMM) that may be
CC equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and
CC increase in number as cells age. FloA and FloT function is partially
CC redundant; double deletions have marked synthetic phenotypes
CC (PubMed:20713508, PubMed:22753055, PubMed:25909364, PubMed:27362352).
CC Flotillins are thought to be important factors in membrane fluidity,
CC especially during periods of rapid growth in rich media (Probable).
CC Whether specific proteins are associated with FMMs is controversial; in
CC one study FloT rafts have been shown to include proteins involved in
CC adaptation to stationary phase, while FloA-FloT rafts include proteins
CC involved in differentation including sporulation, biofilm formation and
CC DNA uptake competence. Another (more finely resolved) study only showed
CC association of NfeD2 with FloT rafts of all the proteins examined
CC (PubMed:25909364, PubMed:27362352). Aids homooligomerization of KinC
CC and KinD but not KinB, may prevent incorrect hetero-association of the
CC above kinases (PubMed:26297017). Simultaneous overexpression of both
CC FloA and FloT leads to defects in cell division and differentiation, in
CC part caused by stabilization of FtsH and its subsequent increased
CC ability to degrade proteins. Cells make more biofilm, are about half as
CC long, have less EzrA and more frequent Z-rings (PubMed:24222488).
CC Involved in spatial organization of membranes, perhaps recruiting
CC proteins (e.g. NfeD2) to specific membrane regions (Probable)
CC (PubMed:23651456). Plays a role in phosphorylation of master regulator
CC Spo0A, an early sporulation event (PubMed:19383680). Plays a non-
CC redundant role with dynamin-like protein A (dynA) in membrane dynamics
CC and cell shape (PubMed:23249255). {ECO:0000269|PubMed:19383680,
CC ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055,
CC ECO:0000269|PubMed:23249255, ECO:0000269|PubMed:23651456,
CC ECO:0000269|PubMed:24222488, ECO:0000269|PubMed:25909364,
CC ECO:0000269|PubMed:26297017, ECO:0000269|PubMed:27362352,
CC ECO:0000305|PubMed:22753055, ECO:0000305|PubMed:32662773}.
CC -!- SUBUNIT: Homooligomerizes (PubMed:25909364). Oligomerizes in very large
CC complexes in vitro. Interacts with FloA, FtsH, FtsX, OppA, SdhA and
CC SecY in detergent-resistant membrane (DRM) fractions (PubMed:23651456).
CC Interacts with FtsH at midcell (Probable). Interacts with FloA
CC (PubMed:25909364). Interacts in vivo with KinC, FloA, FtsH and ResE
CC (PubMed:26297017). Interacts with ResE, colocalizes with ResE in FloT-
CC only membrane rafts (PubMed:25909364). Another study shows nearly
CC complete colocalization with NfeD2, but only minor colocalization with
CC FtsH or KinC (PubMed:27362352). {ECO:0000269|PubMed:23651456,
CC ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:26297017,
CC ECO:0000269|PubMed:27362352, ECO:0000305|PubMed:22882210}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19383680,
CC ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456,
CC ECO:0000269|PubMed:25909364, ECO:0000305|PubMed:25635948}. Membrane
CC raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23249255,
CC ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25909364,
CC ECO:0000269|PubMed:27362352, ECO:0000305|PubMed:19383680}.
CC Note=Tethered to the membrane by a hairpin loop that inserts into the
CC cell membrane (PubMed:25635948). A few foci are seen on the cell
CC membrane during exponential growth, more are seen as cells enter
CC stationary phase. Restricted to the mother cell during sporulation.
CC Foci form a spiral track on the cell membrane and move in the cell.
CC Associated with high bouyancy, cardiolipin- and phosphatidylglycerol-
CC rich membrane fractions, association is not obligatory
CC (PubMed:19383680). Present in detergent-resistant membrane (DRM)
CC fractions, approximately 6 dynamic foci per cell; colocalizes with KinC
CC and sometimes with FloA in DRMs. Foci are lost when cells are treated
CC with squalene synthase inhibitor zaragozic acid (PubMed:20713508).
CC Found in discrete, highly mobile foci, often colocalizes with NfeD2 but
CC rarely with FloA (PubMed:22753055). Forms discrete foci on the cell
CC membrane, about 20% of foci are at the septal site. At the septa
CC colocalizes with FloA and FtsH (PubMed:22882210, PubMed:23249255).
CC Colocalizes with FtsX, OppA, SdhA and SecY in DRMs (PubMed:23651456).
CC Careful analysis gives an average of 13 FloA and 6 FloT foci per cell;
CC FloA foci are smaller that FloT foci (PubMed:25909364). Another study
CC shows FloA and FloT foci are similar in size, forming membrane
CC assemblies of 85-110 nm. FloA are more mobile than FloT foci and they
CC do not overlap. This study found no evidence of colocalization of FloA
CC with FloT, and nearly complete colocalization of FloT with NfeD2
CC (PubMed:27362352). {ECO:0000269|PubMed:19383680,
CC ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23249255,
CC ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25635948,
CC ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352}.
CC -!- INDUCTION: Transcription starts during stationary phase. Few foci are
CC seen in exponential phase cells; the number of foci increases as cells
CC enter stationary phase (at protein level) (PubMed:19383680,
CC PubMed:23651456, PubMed:22753055). Few foci are seen on rich media,
CC when cells are grown in minimal medium more foci are seen (at protein
CC level) (PubMed:22753055). Expressed at low levels in rich media during
CC exponential growth, more highly expressed in stationary phase on
CC sporulation/biofilm-inducing media, activated by spo0A probably via
CC AbrB (at protein level). Surfactin induces expression via spo0A
CC (PubMed:25909364). {ECO:0000269|PubMed:19383680,
CC ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:23651456,
CC ECO:0000269|PubMed:25909364}.
CC -!- DOMAIN: A hairpin loop (about residues 4-24) tethers the protein in the
CC inner membrane. The isolated PHB domain (also called SPFH)
CC oligomerizes, but does not bind lipids (PubMed:25635948). The C-
CC terminal 24 residues are not required for correct localization, but the
CC last 300 residues are required (PubMed:22753055). The C-terminus
CC determines the oligomerization state of the protein; there are few
CC large foci for FloT. Swapping with the C-terminus of FloA leads to many
CC smaller foci (PubMed:25909364). {ECO:0000269|PubMed:22753055,
CC ECO:0000269|PubMed:25635948, ECO:0000269|PubMed:25909364}.
CC -!- DISRUPTION PHENOTYPE: Delay in sporulation onset, 65% reduction in
CC sporulation efficiency (PubMed:19383680, PubMed:22882210). No effect on
CC KinC activity, a double floT-floA deletion decreases the number of
CC proteins in the DRM, blocks the ability of KinC to stimulate biofilm
CC formation (PubMed:20713508). Single floT deletion has defective
CC motility, loss of NfeD2 localization, no change in FloA localization.
CC Double floA-floT mutants have marked defects in cell morphology,
CC motility, and transformation efficiency (PubMed:22753055). Double floA-
CC floT deletion makes no biofilm, has greatly reduced FtsH, sporulates
CC less than either single mutant (PubMed:22882210). Double dynA-floT
CC deletions are highly elongated, filamentous and have strong defects in
CC cell shape; cells grow very slowly with an extended lag phase
CC (PubMed:23249255). Single mutation has a decrease in membrane fluidity
CC and 35% decrease in protein secretion, a double floT-floA deletion has
CC a stronger decrease in membrane fluidity and the same decrease in
CC protein secretion (PubMed:23651456). Double dynA-floT deletion strains
CC are less motile than single floT deletions (PubMed:26842743). Double
CC floA-floT deletion has reduced oligomerization of KinC
CC (PubMed:26297017). Double floA-floT deletion cells are somewhat
CC elongated, the site of cell wall synthesis is affected, increasing at
CC division septa. The speed of MreB movement around the cell is
CC significantly decreased in rich medium in the floA-floT mutant
CC (PubMed:32662773). {ECO:0000269|PubMed:19383680,
CC ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23249255,
CC ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:26297017,
CC ECO:0000269|PubMed:26842743, ECO:0000269|PubMed:32662773}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin subfamily.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB15079.1; -; Genomic_DNA.
DR PIR; A70006; A70006.
DR RefSeq; NP_390979.1; NC_000964.3.
DR RefSeq; WP_003228960.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32076; -.
DR SMR; O32076; -.
DR STRING; 224308.BSU31010; -.
DR PaxDb; O32076; -.
DR PRIDE; O32076; -.
DR EnsemblBacteria; CAB15079; CAB15079; BSU_31010.
DR GeneID; 937138; -.
DR KEGG; bsu:BSU31010; -.
DR PATRIC; fig|224308.179.peg.3361; -.
DR eggNOG; COG2268; Bacteria.
DR InParanoid; O32076; -.
DR OMA; ERQYDSE; -.
DR PhylomeDB; O32076; -.
DR BioCyc; BSUB:BSU31010-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR031905; Flotillin_C.
DR InterPro; IPR027705; Flotillin_fam.
DR PANTHER; PTHR13806; PTHR13806; 2.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF15975; Flot; 1.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell shape; Membrane; Reference proteome; Repeat.
FT CHAIN 1..509
FT /note="Flotillin-like protein FloT"
FT /id="PRO_0000049913"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25635948"
FT INTRAMEM 4..24
FT /evidence="ECO:0000305|PubMed:25635948"
FT TOPO_DOM 25..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25635948,
FT ECO:0000305|PubMed:19383680"
FT REGION 119..301
FT /note="PHB domain"
FT /evidence="ECO:0000305|PubMed:25635948"
FT REGION 203..509
FT /note="Required for correct localization"
FT /evidence="ECO:0000269|PubMed:22753055"
FT REGION 485..509
FT /note="Not required for correct localization"
FT /evidence="ECO:0000269|PubMed:22753055"
FT MOTIF 342..344
FT /note="EA repeat 1"
FT /evidence="ECO:0000269|PubMed:25909364"
FT MOTIF 357..360
FT /note="EA repeat 2"
FT /evidence="ECO:0000269|PubMed:25909364"
FT MOTIF 370..373
FT /note="EA repeat 3"
FT /evidence="ECO:0000269|PubMed:25909364"
FT MOTIF 390..394
FT /note="EA repeat 4"
FT /evidence="ECO:0000269|PubMed:25909364"
FT MUTAGEN 342..344
FT /note="AEA->GLG: Homooligomerizes poorly, decreased number
FT of foci."
FT /evidence="ECO:0000269|PubMed:25909364"
FT MUTAGEN 357..360
FT /note="AEAE->GLGL: No longer homooligomerizes, poor
FT aggregation, severe decrease in the number of foci. Protein
FT is dispersed in the cell membrane."
FT /evidence="ECO:0000269|PubMed:25909364"
FT MUTAGEN 370..373
FT /note="AEAE->GLGL: Homooligomerizes, no change in number of
FT foci."
FT /evidence="ECO:0000269|PubMed:25909364"
FT MUTAGEN 390..394
FT /note="AEAEA->GLGLG: No longer homooligomerizes, poor
FT aggregation, severe decrease in the number of foci."
FT /evidence="ECO:0000269|PubMed:25909364"
SQ SEQUENCE 509 AA; 55994 MW; 16209B06D34EFFBB CRC64;
MTMPIIMIIG VVFFLLIALI AVFITKYRTA GPDEALIVTG SYLGNKNVHV DEGGNRIKIV
RGGGTFVLPV FQQAEPLSLL SSKLDVSTPE VYTEQGVPVM ADGTAIIKIG GSIGEIATAA
EQFLGKSKDD REQEAREVLE GHLRSILGSM TVEEIYKNRE KFSQEVQRVA SQDLAKMGLV
IVSFTIKDVR DKNGYLESLG KPRIAQVKRD ADIATAEADK ETRIKRAEAD KDAKKSELER
ATEIAEAEKI NQLKMAEFRR EQDTAKANAD QAYDLETARA RQQVTEQEMQ VKIIERQKQI
ELEEKEILRR ERQYDSEVKK KADADRYSVE QSAAAEKAKQ LAEADAKKYS IEAMAKAEAE
KVRIDGLAKA EAEKAKGETE AEVIRLKGLA EAEAKEKIAA AFEQYGQAAI FDMIVKMLPE
YAKQAAAPLS NIDKITVVDT GGSGESSGAN KVTSYATNLM SSLQESLKAS SGIDVKEMLE
NFSGKGNVKQ SINELTNEIK EAKTIQKSE
