MFN1_MOUSE
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 03-AUG-2022, entry version 149.
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, Pancreas,
RC 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; Q811U4; -.
DR PeptideAtlas; Q811U4; -.
DR PRIDE; Q811U4; -.
DR ProteomicsDB; 292227; -.
DR ABCD; Q811U4; 1 sequenced antibody.
DR Antibodypedia; 33743; 536 antibodies from 40 providers.
DR DNASU; 67414; -.
DR Ensembl; ENSMUST00000091257; ENSMUSP00000088801; ENSMUSG00000027668.
DR Ensembl; ENSMUST00000118286; ENSMUSP00000113251; ENSMUSG00000027668.
DR GeneID; 67414; -.
DR KEGG; mmu:67414; -.
DR UCSC; uc008owi.2; mouse.
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; HMERCLN; -.
DR OrthoDB; 216494at2759; -.
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 71 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 255 other tissues.
DR ExpressionAtlas; Q811U4; baseline and differential.
DR Genevisible; Q811U4; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0031306; C:intrinsic component of mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
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:0070584; P:mitochondrion morphogenesis; ISO:MGI.
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 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 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
