ID   MFN1_MOUSE              Reviewed;         741 AA.
AC   Q811U4; Q3URC4; Q811D5; Q8CEY6; Q99M10; Q9D395;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Mitofusin-1;
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:Q8IWA4};
DE   AltName: Full=Transmembrane GTPase MFN1;
GN   Name=Mfn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, MULTIMERIZATION,
RP   SUBUNIT, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC   STRAIN=FVB/NJ;
RX   PubMed=12527753; DOI=10.1083/jcb.200211046;
RA   Chen H., Detmer S.A., Ewald A.J., Griffin E.E., Fraser S.E., Chan D.C.;
RT   "Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and
RT   are essential for embryonic development.";
RL   J. Cell Biol. 160:189-200(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, Medulla oblongata, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=11950885; DOI=10.1242/jcs.115.8.1663;
RA   Rojo M., Legros F., Chateau D., Lombes A.;
RT   "Membrane topology and mitochondrial targeting of mitofusins, ubiquitous
RT   mammalian homologs of the transmembrane GTPase Fzo.";
RL   J. Cell Sci. 115:1663-1674(2002).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12759376; DOI=10.1242/jcs.00479;
RA   Santel A., Frank S., Gaume B., Herrler M., Youle R.J., Fuller M.T.;
RT   "Mitofusin-1 protein is a generally expressed mediator of mitochondrial
RT   fusion in mammalian cells.";
RL   J. Cell Sci. 116:2763-2774(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION.
RX   PubMed=23921378; DOI=10.1074/jbc.m113.479873;
RA   Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D.,
RA   Ryan M.T.;
RT   "MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment
RT   and are specific for mitochondrial fission.";
RL   J. Biol. Chem. 288:27584-27593(2013).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23620051; DOI=10.1126/science.1231031;
RA   Chen Y., Dorn G.W. II;
RT   "PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged
RT   mitochondria.";
RL   Science 340:471-475(2013).
RN   [9]
RP   FUNCTION, UBIQUITINATION, AND DEUBIQUITINATION.
RX   PubMed=24513856; DOI=10.1038/cr.2014.20;
RA   Yue W., Chen Z., Liu H., Yan C., Chen M., Feng D., Yan C., Wu H., Du L.,
RA   Wang Y., Liu J., Huang X., Xia L., Liu L., Wang X., Jin H., Wang J.,
RA   Song Z., Hao X., Chen Q.;
RT   "A small natural molecule promotes mitochondrial fusion through inhibition
RT   of the deubiquitinase USP30.";
RL   Cell Res. 24:482-496(2014).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 660-735, FUNCTION, SUBUNIT, AND
RP   COILED-COIL DOMAINS.
RX   PubMed=15297672; DOI=10.1126/science.1099793;
RA   Koshiba T., Detmer S.A., Kaiser J.T., Chen H., McCaffery J.M., Chan D.C.;
RT   "Structural basis of mitochondrial tethering by mitofusin complexes.";
RL   Science 305:858-862(2004).
CC   -!- FUNCTION: Mitochondrial outer membrane GTPase that mediates
CC       mitochondrial clustering and fusion (PubMed:12527753, PubMed:23921378,
CC       PubMed:24513856, PubMed:15297672). Membrane clustering requires GTPase
CC       activity (By similarity). It may involve a major rearrangement of the
CC       coiled coil domains (PubMed:15297672). Mitochondria are highly dynamic
CC       organelles, and their morphology is determined by the equilibrium
CC       between mitochondrial fusion and fission events (PubMed:12527753).
CC       Overexpression induces the formation of mitochondrial networks (in
CC       vitro). Has low GTPase activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q8IWA4, ECO:0000269|PubMed:12527753,
CC       ECO:0000269|PubMed:15297672, ECO:0000269|PubMed:23921378,
CC       ECO:0000269|PubMed:24513856}.
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         Evidence={ECO:0000250|UniProtKB:Q8IWA4};
CC   -!- SUBUNIT: Homodimer, also in the absence of bound GTP (By similarity).
CC       Forms higher oligomers in the presence of a transition state GTP analog
CC       (By similarity). Forms homomultimers and heteromultimers with MFN2
CC       (PubMed:12527753). Oligomerization is essential for mitochondrion
CC       fusion (PubMed:15297672). Component of a high molecular weight
CC       multiprotein complex (By similarity). Interacts with VAT1 (By
CC       similarity). Interacts with THG1L; THG1L probably functions as a
CC       guanyl-nucleotide exchange factor/GEF, activating MFN1.
CC       {ECO:0000250|UniProtKB:Q8IWA4, ECO:0000250|UniProtKB:Q8R4Z9,
CC       ECO:0000269|PubMed:12527753, ECO:0000269|PubMed:15297672}.
CC   -!- INTERACTION:
CC       Q811U4; Q5S007: LRRK2; Xeno; NbExp=3; IntAct=EBI-9029118, EBI-5323863;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:12759376}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in adult heart (PubMed:12759376). Detected
CC       in embryos (at protein level) (PubMed:12527753). Widely expressed
CC       (PubMed:11950885). {ECO:0000269|PubMed:11950885,
CC       ECO:0000269|PubMed:12527753, ECO:0000269|PubMed:12759376}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in 8.5 dpc, 9.5 dpc, 10.5 dpc and 11.5
CC       dpc embryos. {ECO:0000269|PubMed:12527753}.
CC   -!- DOMAIN: A helix bundle is formed by helices from the N-terminal and the
CC       C-terminal part of the protein. The GTPase domain cannot be expressed
CC       by itself, without the helix bundle. Rearrangement of the helix bundle
CC       and/or of the coiled coil domains may bring membranes from adjacent
CC       mitochondria into close contact, and thereby play a role in
CC       mitochondrial fusion. {ECO:0000250|UniProtKB:Q8IWA4}.
CC   -!- PTM: Ubiquitinated by MARCHF5 (By similarity). When mitochondria are
CC       depolarized and dysfunctional, it is ubiquitinated by a SCF (SKP1-CUL1-
CC       F-box protein) E3 ubiquitin-protein ligase complex that contains FBXO7
CC       and PRKN. Ubiquitinated by non-degradative ubiquitin by PRKN, promoting
CC       mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial
CC       fusion (PubMed:24513856). {ECO:0000250|UniProtKB:Q8IWA4,
CC       ECO:0000269|PubMed:24513856}.
CC   -!- DISRUPTION PHENOTYPE: Full embryonic lethality; nearly 90% of the
CC       mutant embryos have been resorbed at 11.5 dpc (PubMed:12527753).
CC       Contrary to wild-type embryonic fibroblasts that have elongated,
CC       tubular mitochondria, mutant embryonic fibroblasts contain only
CC       fragmented mitochondria (PubMed:12527753). In cultured cells, mutant
CC       mitochondria show a strongly decreased frequency of mitochondrial
CC       fusion events (PubMed:12527753). In spite of the aberrant mitochondrial
CC       morphology, there seem to be no gross defects in respiration
CC       (PubMed:12527753). Heart-specific disruption of Mfn1 does not impair
CC       heart function and has no effect on cardiomyocyte mitochondrial
CC       morphometry or respiratory function (PubMed:23620051).
CC       {ECO:0000269|PubMed:12527753, ECO:0000269|PubMed:23620051}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU01055}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH47050.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC25260.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY174062; AAO34660.1; -; mRNA.
DR   EMBL; AK009490; BAC25260.1; ALT_INIT; mRNA.
DR   EMBL; AK018181; BAB31111.1; -; mRNA.
DR   EMBL; AK141611; BAE24764.1; -; mRNA.
DR   EMBL; BC002133; AAH02133.1; -; mRNA.
DR   EMBL; BC047050; AAH47050.1; ALT_INIT; mRNA.
DR   EMBL; BC056641; AAH56641.1; -; mRNA.
DR   CCDS; CCDS17296.1; -.
DR   RefSeq; NP_077162.2; NM_024200.4.
DR   PDB; 1T3J; X-ray; 2.50 A; A=660-735.
DR   PDBsum; 1T3J; -.
DR   AlphaFoldDB; Q811U4; -.
DR   SMR; Q811U4; -.
DR   BioGRID; 212170; 4.
DR   DIP; DIP-60969N; -.
DR   IntAct; Q811U4; 4.
DR   STRING; 10090.ENSMUSP00000088801; -.
DR   iPTMnet; Q811U4; -.
DR   PhosphoSitePlus; Q811U4; -.
DR   EPD; Q811U4; -.
DR   jPOST; Q811U4; -.
DR   MaxQB; Q811U4; -.
DR   PaxDb; 10090-ENSMUSP00000088801; -.
DR   PeptideAtlas; Q811U4; -.
DR   ProteomicsDB; 292227; -.
DR   Pumba; Q811U4; -.
DR   ABCD; Q811U4; 1 sequenced antibody.
DR   Antibodypedia; 33743; 618 antibodies from 40 providers.
DR   DNASU; 67414; -.
DR   Ensembl; ENSMUST00000091257.11; ENSMUSP00000088801.5; ENSMUSG00000027668.14.
DR   Ensembl; ENSMUST00000118286.8; ENSMUSP00000113251.2; ENSMUSG00000027668.14.
DR   GeneID; 67414; -.
DR   KEGG; mmu:67414; -.
DR   UCSC; uc008owi.2; mouse.
DR   AGR; MGI:1914664; -.
DR   CTD; 55669; -.
DR   MGI; MGI:1914664; Mfn1.
DR   VEuPathDB; HostDB:ENSMUSG00000027668; -.
DR   eggNOG; KOG0448; Eukaryota.
DR   GeneTree; ENSGT00390000013727; -.
DR   HOGENOM; CLU_021212_1_0_1; -.
DR   InParanoid; Q811U4; -.
DR   OMA; IMDTINV; -.
DR   OrthoDB; 3282693at2759; -.
DR   PhylomeDB; Q811U4; -.
DR   TreeFam; TF314289; -.
DR   Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR   Reactome; R-MMU-9013419; RHOT2 GTPase cycle.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 67414; 17 hits in 76 CRISPR screens.
DR   ChiTaRS; Mfn1; mouse.
DR   EvolutionaryTrace; Q811U4; -.
DR   PRO; PR:Q811U4; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q811U4; Protein.
DR   Bgee; ENSMUSG00000027668; Expressed in myocardium of ventricle and 259 other cell types or tissues.
DR   ExpressionAtlas; Q811U4; baseline and differential.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0098799; C:outer mitochondrial membrane protein complex; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR   GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
DR   GO; GO:0008053; P:mitochondrial fusion; IMP:UniProtKB.
DR   GO; GO:0051646; P:mitochondrion localization; ISS:UniProtKB.
DR   GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:MGI.
DR   GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI.
DR   GO; GO:0010636; P:positive regulation of mitochondrial fusion; ISO:MGI.
DR   GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IGI:CACAO.
DR   CDD; cd09912; DLP_2; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR006884; Fzo/mitofusin_HR2.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR027094; Mitofusin_fam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10465:SF2; MITOFUSIN-1; 1.
DR   PANTHER; PTHR10465; TRANSMEMBRANE GTPASE FZO1; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF04799; Fzo_mitofusin; 1.
DR   SUPFAM; SSF111479; Fzo-like conserved region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   Genevisible; Q811U4; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Developmental protein; GTP-binding; Hydrolase;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..741
FT                   /note="Mitofusin-1"
FT                   /id="PRO_0000127673"
FT   TOPO_DOM        1..584
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        585..605
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        606..608
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        609..629
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        630..741
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          72..321
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          9..73
FT                   /note="Part of a helix bundle domain, formed by helices
FT                   from N-terminal and C-terminal regions"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT   REGION          82..89
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          108..109
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          178..181
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          237..240
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          266
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          338..364
FT                   /note="Part of a helix bundle domain, formed by helices
FT                   from N-terminal and C-terminal regions"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT   REGION          703..734
FT                   /note="Part of a helix bundle domain, formed by helices
FT                   from N-terminal and C-terminal regions"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT   COILED          371..408
FT                   /evidence="ECO:0000269|PubMed:15297672"
FT   COILED          677..735
FT                   /evidence="ECO:0000269|PubMed:15297672"
FT   BINDING         85..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT   BINDING         237..240
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT   BINDING         284
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT   BINDING         286
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT   CONFLICT        209
FT                   /note="E -> G (in Ref. 2; BAB31111)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        328..329
FT                   /note="IS -> VL (in Ref. 2; BAB31111)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        335
FT                   /note="T -> A (in Ref. 2; BAB31111)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        521
FT                   /note="V -> A (in Ref. 2; BAB31111)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        588
FT                   /note="L -> W (in Ref. 2; BAB31111)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        619
FT                   /note="L -> S (in Ref. 2; BAB31111)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        718
FT                   /note="K -> R (in Ref. 2; BAB31111)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        720
FT                   /note="V -> I (in Ref. 3; AAH02133/AAH56641)"
FT                   /evidence="ECO:0000305"
FT   HELIX           676..733
FT                   /evidence="ECO:0007829|PDB:1T3J"
SQ   SEQUENCE   741 AA;  83726 MW;  36E5E90DB0C0D5A1 CRC64;
     MAETVSPLKH FVLAKKAITA IFGQLLEFVT EGSHFVEATY RNPELDRIAS EDDLVEIQGY
     RNKLAVIGEV LSRRHMKVAF FGRTSSGKSS VINAMLWDKV LPSGIGHTTN CFLSVEGTDG
     DKAYLMTEGS DEKKSVKTVN QLAHALHMDK DLKAGCLVHV FWPKAKCALL RDDLVLVDSP
     GTDVTTELDI WIDKFCLDAD VFVLVANSES TLMNTEKHFF HKVNERLSKP NIFILNNRWD
     ASASEPEYME DVRRQHMERC LHFLVEELKV VSPSEARNRI FFVSAKEVLN SRKHKAQGMP
     EGGGALAEGF QARLQEFQNF EQTFEECISQ SAVKTKFEQH TIRAKQILDT VKNILDSVNV
     AAAEKRVYSM EEREDQIDRL DFIRNQMNLL TLDVKKKIKE VTEEVANKVS CAMTDEICRL
     SVLVDEFCSE FHPTPSVLKV YKSELNKHIE DGMGRNLADR CTNEVNASIL QSQQEIIENL
     KPLLPAGIQN KLHTLIPCKK FDLSYDLNCH KLCSDFQEDI VFRFSLGWSS LVHRFLGSTN
     AQRVLLGLSE PIFQVPRSLA STPTAPSNPA APDNAAQEEL MITLITGLAS LTSRTSMGII
     VVGGVIWKTV GWKLISVTLS MYGALYLYER LTWTTRAKER AFKQQFVNYA TEKLQMIVSF
     TSANCSHQVQ QEMATTFARL CQQVDVTQKH LEEEIARLSK EIDQLEKIQN NSKLLRNKAV
     QLESELENFS KQFLHPSSGE S
//