MARF_DROME
ID MARF_DROME Reviewed; 810 AA.
AC Q7YU24; Q0KHV7; Q86DQ3; Q8T3J4; Q9W3Z9;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Transmembrane GTPase Marf;
DE EC=3.6.5.-;
DE AltName: Full=Mitochondrial assembly regulatory factor;
DE AltName: Full=Mitofusin;
GN Name=Marf; Synonyms=dmfn; ORFNames=CG3869;
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 [MRNA] (ISOFORM 1).
RX PubMed=12598526; DOI=10.1074/jbc.m212754200;
RA Bach D., Pich S., Soriano F.X., Vega N., Baumgartner B., Oriola J.,
RA Daugaard J.R., Lloberas J., Camps M., Zierath J.R., Rabasa-Lhoret R.,
RA Wallberg-Henriksson H., Laville M., Palacin M., Vidal H., Rivera F.,
RA Brand M., Zorzano A.;
RT "Mitofusin-2 determines mitochondrial network architecture and
RT mitochondrial metabolism. A novel regulatory mechanism altered in
RT obesity.";
RL J. Biol. Chem. 278:17190-17197(2003).
RN [2]
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12128227; DOI=10.1016/s0925-4773(02)00141-7;
RA Hwa J.J., Hiller M.A., Fuller M.T., Santel A.;
RT "Differential expression of the Drosophila mitofusin genes fuzzy onions
RT (fzo) and dmfn.";
RL Mech. Dev. 116:213-216(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-38; THR-553; SER-554
RP AND THR-555, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18799731; DOI=10.1073/pnas.0803998105;
RA Deng H., Dodson M.W., Huang H., Guo M.;
RT "The Parkinson's disease genes pink1 and parkin promote mitochondrial
RT fission and/or inhibit fusion in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:14503-14508(2008).
RN [8]
RP FUNCTION, UBIQUITINATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20194754; DOI=10.1073/pnas.0913485107;
RA Ziviani E., Tao R.N., Whitworth A.J.;
RT "Drosophila parkin requires PINK1 for mitochondrial translocation and
RT ubiquitinates mitofusin.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5018-5023(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20869429; DOI=10.1016/j.gene.2010.09.003;
RA Ottone C., Galasso A., Gemei M., Pisa V., Gigliotti S., Piccioni F.,
RA Graziani F., Verrotti di Pianella A.;
RT "Diminution of eIF4E activity suppresses parkin mutant phenotypes.";
RL Gene 470:12-19(2011).
RN [10]
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 [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24192653; DOI=10.1161/circresaha.114.302734;
RA Bhandari P., Song M., Chen Y., Burelle Y., Dorn G.W. II;
RT "Mitochondrial contagion induced by Parkin deficiency in Drosophila hearts
RT and its containment by suppressing mitofusin.";
RL Circ. Res. 114:257-265(2014).
RN [12]
RP INTERACTION WITH MUL1, AND UBIQUITINATION.
RX PubMed=24898855; DOI=10.7554/elife.01958;
RA Yun J., Puri R., Yang H., Lizzio M.A., Wu C., Sheng Z.H., Guo M.;
RT "MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin
RT and compensates for loss of PINK1/parkin.";
RL Elife 3:E01958-E01958(2014).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND UBIQUITINATION.
RX PubMed=26214738; DOI=10.1038/nature14601;
RA Senyilmaz D., Virtue S., Xu X., Tan C.Y., Griffin J.L., Miller A.K.,
RA Vidal-Puig A., Teleman A.A.;
RT "Regulation of mitochondrial morphology and function by stearoylation of
RT TFR1.";
RL Nature 525:124-128(2015).
RN [14]
RP MUTAGENESIS OF ILE-221.
RX PubMed=25594180; DOI=10.1016/j.cell.2014.12.019;
RA Liu L., Zhang K., Sandoval H., Yamamoto S., Jaiswal M., Sanz E., Li Z.,
RA Hui J., Graham B.H., Quintana A., Bellen H.J.;
RT "Glial lipid droplets and ROS induced by mitochondrial defects promote
RT neurodegeneration.";
RL Cell 160:177-190(2015).
CC -!- FUNCTION: Mitochondrial outer membrane GTPase that mediates
CC mitochondrial clustering and fusion (PubMed:18799731, PubMed:20869429,
CC PubMed:22396657, PubMed:24192653, PubMed:26214738). Mitochondrial
CC fusion is the physical merging of mitochondria that gives rise to
CC mitochondrial networks, and this process is counterbalanced by
CC mitochondrial fission which fragments networks (PubMed:20869429,
CC PubMed:22396657, PubMed:24192653). Promotes, but is not required for
CC park recruitment to dysfunctional mitochondria (PubMed:20194754).
CC {ECO:0000269|PubMed:18799731, ECO:0000269|PubMed:20194754,
CC ECO:0000269|PubMed:20869429, ECO:0000269|PubMed:22396657,
CC ECO:0000269|PubMed:24192653, ECO:0000269|PubMed:26214738}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC -!- SUBUNIT: Interacts with Mul1. {ECO:0000269|PubMed:24898855}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:26214738}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=B {ECO:0000312|FlyBase:FBgn0029870}, C
CC {ECO:0000312|FlyBase:FBgn0029870};
CC IsoId=Q7YU24-1; Sequence=Displayed;
CC Name=2; Synonyms=D {ECO:0000312|FlyBase:FBgn0029870};
CC IsoId=Q7YU24-2; Sequence=VSP_058137;
CC -!- TISSUE SPECIFICITY: Widely expressed in embryos, accumulating in the
CC mesoderm and endoderm during gut development. In the male germ line, it
CC is expressed in spermatogonia, spermatocytes and early spermatids.
CC {ECO:0000269|PubMed:12128227}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:12128227}.
CC -!- PTM: Ubiquitinated by park and Mul1 (PubMed:24898855, PubMed:20194754).
CC Ubiquitinated, probably by HUWE1, when dietary stearate (C18:0) levels
CC are low; ubiquitination inhibits mitochondrial fusion
CC (PubMed:26214738). {ECO:0000269|PubMed:20194754,
CC ECO:0000269|PubMed:24898855, ECO:0000269|PubMed:26214738}.
CC -!- DISRUPTION PHENOTYPE: Lethal at the early larval stage (L1/L2);
CC mitochondria are fragmented and mitochondrial respiration is impaired
CC (PubMed:26214738). RNAi-mediated knockdown is also lethal
CC (PubMed:20869429). RNAi-mediated knockdown in specific tissues such as
CC cardiomyocytes, muscles and larval neurons produces various phenotypes
CC resulting from adherent, dysfunctional mitochondria (PubMed:18799731,
CC PubMed:20869429, PubMed:22396657, PubMed:24192653). Mitochondria
CC display characteristics such as abnormal cristae, fragmentation,
CC elongation, decreased DNA content, increased ROS and depolarization
CC (PubMed:20869429, PubMed:20194754, PubMed:22396657, PubMed:24192653).
CC Mitochondria in larval muscles display increased mitochondrial flux and
CC net velocity in both anterograde and retrograde directions
CC (PubMed:20194754). {ECO:0000269|PubMed:18799731,
CC ECO:0000269|PubMed:20194754, ECO:0000269|PubMed:20869429,
CC ECO:0000269|PubMed:22396657, ECO:0000269|PubMed:24192653,
CC ECO:0000269|PubMed:26214738}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01055}.
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DR EMBL; AF355475; AAM00196.1; -; mRNA.
DR EMBL; AE014298; AAS65267.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF46162.2; -; Genomic_DNA.
DR EMBL; AY095019; AAM11347.2; -; mRNA.
DR EMBL; BT010027; AAQ22496.1; -; mRNA.
DR RefSeq; NP_572320.2; NM_132092.3. [Q7YU24-2]
DR RefSeq; NP_996357.1; NM_206634.2. [Q7YU24-1]
DR RefSeq; NP_996358.2; NM_206635.3. [Q7YU24-1]
DR AlphaFoldDB; Q7YU24; -.
DR SMR; Q7YU24; -.
DR BioGRID; 58068; 33.
DR DIP; DIP-58614N; -.
DR IntAct; Q7YU24; 4.
DR STRING; 7227.FBpp0070873; -.
DR iPTMnet; Q7YU24; -.
DR PaxDb; Q7YU24; -.
DR PRIDE; Q7YU24; -.
DR DNASU; 31581; -.
DR EnsemblMetazoa; FBtr0070909; FBpp0089222; FBgn0029870. [Q7YU24-1]
DR EnsemblMetazoa; FBtr0070910; FBpp0089221; FBgn0029870. [Q7YU24-1]
DR EnsemblMetazoa; FBtr0343373; FBpp0310030; FBgn0029870. [Q7YU24-2]
DR GeneID; 31581; -.
DR KEGG; dme:Dmel_CG3869; -.
DR CTD; 31581; -.
DR FlyBase; FBgn0029870; Marf.
DR VEuPathDB; VectorBase:FBgn0029870; -.
DR eggNOG; KOG0448; Eukaryota.
DR GeneTree; ENSGT00390000013727; -.
DR InParanoid; Q7YU24; -.
DR OMA; LEFRFSF; -.
DR PhylomeDB; Q7YU24; -.
DR Reactome; R-DME-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-DME-9013419; RHOT2 GTPase cycle.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q7YU24; -.
DR BioGRID-ORCS; 31581; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Marf; fly.
DR GenomeRNAi; 31581; -.
DR PRO; PR:Q7YU24; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029870; Expressed in spermathecum and 33 other tissues.
DR ExpressionAtlas; Q7YU24; baseline and differential.
DR Genevisible; Q7YU24; DM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031306; C:intrinsic component of mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005740; C:mitochondrial envelope; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IMP:FlyBase.
DR GO; GO:0006697; P:ecdysone biosynthetic process; IMP:FlyBase.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:FlyBase.
DR GO; GO:0034389; P:lipid droplet organization; IMP:FlyBase.
DR GO; GO:0035170; P:lymph gland crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:UniProtKB.
DR GO; GO:0051646; P:mitochondrion localization; IBA:GO_Central.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:FlyBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IMP:UniProtKB.
DR GO; GO:0090140; P:regulation of mitochondrial fission; IMP:FlyBase.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR006884; Fzo/mitofusin_HR2.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027088; Mitofusin-1.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10465; PTHR10465; 1.
DR PANTHER; PTHR10465:SF2; PTHR10465:SF2; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF04799; Fzo_mitofusin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; GTP-binding; Hydrolase; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..810
FT /note="Transmembrane GTPase Marf"
FT /id="PRO_0000127679"
FT TOPO_DOM 1..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..648
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..668
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..810
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 134..382
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 13..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..151
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 170..171
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 239..242
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 298..301
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 327
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 609..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 427..476
FT /evidence="ECO:0000255"
FT COILED 759..806
FT /evidence="ECO:0000255"
FT COMPBIAS 611..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT BINDING 298..301
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT BINDING 345
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 553
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 555
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 312
FT /note="S -> SELAK (in isoform 2)"
FT /id="VSP_058137"
FT MUTAGEN 221
FT /note="I->N: Shows high levels of reactive oxygen species
FT (ROS) and accumulation of lipid droplets in pigment and
FT epithelial glia. Lipid droplet accumulation occurs early,
FT prior to the onset of neurodegeneration."
FT /evidence="ECO:0000269|PubMed:25594180"
FT CONFLICT 621
FT /note="G -> Q (in Ref. 1; AAM00196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 810 AA; 91372 MW; 8A3362BE1DD2A115 CRC64;
MAAYLNRTIS MVTGQTGPAD DDRHASSTDT VDKSGPGSPL SRFNSSLQQS GSTMAANLLP
ESRLYQSNDK SPLQIFVRAK KKINDIYGEI EEYVHETTTF INALHAEAEI VDKAERELFE
SYVYKVAAIR EVLQRDHMKV AFFGRTSNGK SSVINAMLRE KILPSGIGHT TNCFCQVEGS
NGGEAYLMTE GSEEKLNVVN IKQLANALCQ EKLCESSLVR IFWPRERCSL LRDDVVFVDS
PGVDVSANLD DWIDNHCLNA DVFVLVLNAE STMTRAEKQF FHTVSQKLSK PNIFILNNRW
DASANEPECQ ESVKSQHTER CIDFLTKELK VSNEKEAAER VFFVSARETL QARIEEAKGN
PPHMGAIAEG FQIRYFEFQD FERKFEECIS QSAVKTKFQQ HSSRGKSVSG DMKSMLDNIY
ERITIFRNLK QDQKNLLTER IQGTETQMMQ VTREMKMKIH NMVEEVEEKV SKALNEEIWR
LGVLIDEFNM PFHPERLVLN IYKKELNAHV ESGLGSNLRA RLSMALAMNV ESAQTEMTDR
MHALVPNEQL LATSTKMVVR TQPFEMLYSL NCQNLCADFQ EDLEFKFSWG IAAMIQRFTG
KVRERSKKGQ PALVNRQSSI GHSVSTPTTT PVEATPVCLL PAPVVAGITP EQLSLISRFA
VSSIGSQGTV GGLVVAGVML KTIGWRVLVG VGALYGCIYL YERLSWTNSA KERTFKSQYV
RHATKKLKMI VDLTSANCSH QVQQELSSTF ARLCRTVDTA TTDMNDELKT LDSQLNILEA
NQKQLKLLRN KANYIQNELD IFEHNYISPQ
