ID MID49_HUMAN Reviewed; 454 AA. AC Q96C03; J3KPT3; Q6ZRD4; Q96N07; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 146. DE RecName: Full=Mitochondrial dynamics protein MID49; DE AltName: Full=Mitochondrial dynamics protein of 49 kDa; DE AltName: Full=Mitochondrial elongation factor 2; DE AltName: Full=Smith-Magenis syndrome chromosomal region candidate gene 7 protein; GN Name=MIEF2; Synonyms=MID49, SMCR7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=11997338; DOI=10.1101/gr.73702; RA Bi W., Yan J., Stankiewicz P., Park S.-S., Walz K., Boerkoel C.F., RA Potocki L., Shaffer L.G., Devriendt K., Nowaczyk M.J.M., Inoue K., RA Lupski J.R.; RT "Genes in a refined Smith-Magenis syndrome critical deletion interval on RT chromosome 17p11.2 and the syntenic region of the mouse."; RL Genome Res. 12:713-728(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Teratocarcinoma, and Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH DNM1L. RX PubMed=21508961; DOI=10.1038/embor.2011.54; RA Palmer C.S., Osellame L.D., Laine D., Koutsopoulos O.S., Frazier A.E., RA Ryan M.T.; RT "MiD49 and MiD51, new components of the mitochondrial fission machinery."; RL EMBO Rep. 12:565-573(2011). RN [8] 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 [9] RP FUNCTION, AND INTERACTION WITH DNM1L. RX PubMed=23283981; DOI=10.1091/mbc.e12-10-0721; RA Loson O.C., Song Z., Chen H., Chan D.C.; RT "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial RT fission."; RL Mol. Biol. Cell 24:659-667(2013). RN [10] RP FUNCTION, INTERACTION WITH DNM1L, AND SUBUNIT. RX PubMed=23530241; DOI=10.1073/pnas.1300855110; RA Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.; RT "Interchangeable adaptors regulate mitochondrial dynamin assembly for RT membrane scission."; RL Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013). RN [11] RP FUNCTION, VARIANT COXPD49 81-GLN--LEU-454 DEL, AND INVOLVEMENT IN COXPD49. RX PubMed=29361167; DOI=10.1093/hmg/ddy033; RA Bartsakoulia M., Pyle A., Troncoso-Chandia D., Vial-Brizzi J., RA Paz-Fiblas M.V., Duff J., Griffin H., Boczonadi V., Lochmueller H., RA Kleinle S., Chinnery P.F., Gruenert S., Kirschner J., Eisner V., RA Horvath R.; RT "A novel mechanism causing imbalance of mitochondrial fusion and fission in RT human myopathies."; RL Hum. Mol. Genet. 27:1186-1195(2018). RN [12] {ECO:0007744|PDB:5WP9} RP STRUCTURE BY ELECTRON MICROSCOPY (4.22 ANGSTROMS) OF 126-454 IN COMPLEX RP WITH DNM1L, FUNCTION, AND MUTAGENESIS OF ARG-235. RX PubMed=29899447; DOI=10.1038/s41586-018-0211-2; RA Kalia R., Wang R.Y., Yusuf A., Thomas P.V., Agard D.A., Shaw J.M., RA Frost A.; RT "Structural basis of mitochondrial receptor binding and constriction by RT DRP1."; RL Nature 558:401-405(2018). CC -!- FUNCTION: Mitochondrial outer membrane protein involved in the CC regulation of mitochondrial organization (PubMed:29361167). It is CC required for mitochondrial fission and promotes the recruitment and CC association of the fission mediator dynamin-related protein 1 (DNM1L) CC to the mitochondrial surface independently of the mitochondrial fission CC FIS1 and MFF proteins. Regulates DNM1L GTPase activity. CC {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:23283981, CC ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23921378, CC ECO:0000269|PubMed:29361167, ECO:0000269|PubMed:29899447}. CC -!- SUBUNIT: Interacts with DNM1L. {ECO:0000269|PubMed:21508961, CC ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241, CC ECO:0000269|PubMed:29899447}. CC -!- INTERACTION: CC Q96C03; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-750153, EBI-741181; CC Q96C03; O00429: DNM1L; NbExp=5; IntAct=EBI-750153, EBI-724571; CC Q96C03; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-750153, EBI-712367; CC Q96C03; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-750153, EBI-741480; CC Q96C03; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-750153, EBI-10173939; CC Q96C03-3; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-11988931, EBI-11522760; CC Q96C03-3; P53365: ARFIP2; NbExp=3; IntAct=EBI-11988931, EBI-638194; CC Q96C03-3; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-11988931, EBI-714543; CC Q96C03-3; P18859: ATP5PF; NbExp=3; IntAct=EBI-11988931, EBI-2606700; CC Q96C03-3; P55212: CASP6; NbExp=3; IntAct=EBI-11988931, EBI-718729; CC Q96C03-3; Q8N5P9: CIDEA; NbExp=3; IntAct=EBI-11988931, EBI-12947393; CC Q96C03-3; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-11988931, EBI-10973142; CC Q96C03-3; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-11988931, EBI-14240149; CC Q96C03-3; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-11988931, EBI-3918971; CC Q96C03-3; Q2KHT4-3: GSG1; NbExp=3; IntAct=EBI-11988931, EBI-12951679; CC Q96C03-3; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-11988931, EBI-18053395; CC Q96C03-3; Q9H400: LIME1; NbExp=3; IntAct=EBI-11988931, EBI-2830566; CC Q96C03-3; P21741: MDK; NbExp=3; IntAct=EBI-11988931, EBI-722444; CC Q96C03-3; P61601: NCALD; NbExp=3; IntAct=EBI-11988931, EBI-749635; CC Q96C03-3; P62166: NCS1; NbExp=3; IntAct=EBI-11988931, EBI-746987; CC Q96C03-3; P02812: PRB2; NbExp=3; IntAct=EBI-11988931, EBI-19951389; CC Q96C03-3; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-11988931, EBI-712367; CC Q96C03-3; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-11988931, EBI-14065960; CC Q96C03-3; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-11988931, EBI-17589229; CC Q96C03-3; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-11988931, EBI-2854842; CC Q96C03-3; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-11988931, EBI-2623095; CC Q96C03-3; P08247: SYP; NbExp=3; IntAct=EBI-11988931, EBI-9071725; CC Q96C03-3; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-11988931, EBI-11528917; CC Q96C03-3; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-11988931, EBI-947187; CC Q96C03-3; O95070: YIF1A; NbExp=3; IntAct=EBI-11988931, EBI-2799703; CC Q96C03-3; Q5EBL2: ZNF628; NbExp=3; IntAct=EBI-11988931, EBI-13086230; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000269|PubMed:21508961}; Single-pass membrane protein CC {ECO:0000269|PubMed:21508961}. Note=Colocalizes with DNM1L at CC mitochondrial membrane. Forms foci and rings around mitochondria. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96C03-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96C03-2; Sequence=VSP_029358, VSP_029359; CC Name=3; CC IsoId=Q96C03-3; Sequence=VSP_047650; CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested with highest CC expression in heart and skeletal muscle. {ECO:0000269|PubMed:11997338}. CC -!- DISEASE: Combined oxidative phosphorylation deficiency 49 (COXPD49) CC [MIM:619024]: An autosomal recessive, mitochondrial myopathy CC characterized by progressive muscle weakness, intermittent muscle pain, CC exercise intolerance, elevated serum creatine kinase, and deficiencies CC of multiple respiratory chain enzymes. {ECO:0000269|PubMed:29361167}. CC Note=The disease may be caused by variants affecting the gene CC represented in this entry. CC -!- MISCELLANEOUS: Does not bind ADP or other nucleotides, in contrast to CC MIEF1. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MID49/MID51 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF467443; AAL78340.1; -; mRNA. DR EMBL; AK056165; BAB71108.1; -; mRNA. DR EMBL; AK128310; BAC87377.1; -; mRNA. DR EMBL; AC127537; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471196; EAW55651.1; -; Genomic_DNA. DR EMBL; CH471196; EAW55652.1; -; Genomic_DNA. DR EMBL; BC014973; AAH14973.1; -; mRNA. DR CCDS; CCDS11193.1; -. [Q96C03-1] DR CCDS; CCDS45624.1; -. [Q96C03-3] DR CCDS; CCDS45625.1; -. [Q96C03-2] DR RefSeq; NP_001138372.1; NM_001144900.1. [Q96C03-2] DR RefSeq; NP_631901.2; NM_139162.3. [Q96C03-1] DR RefSeq; NP_683684.2; NM_148886.1. [Q96C03-3] DR PDB; 5WP9; EM; 4.22 A; B/D/F/H/J/L/N/P=126-454. DR PDBsum; 5WP9; -. DR AlphaFoldDB; Q96C03; -. DR EMDB; EMD-8874; -. DR SMR; Q96C03; -. DR BioGRID; 125921; 34. DR IntAct; Q96C03; 30. DR MINT; Q96C03; -. DR STRING; 9606.ENSP00000379057; -. DR iPTMnet; Q96C03; -. DR PhosphoSitePlus; Q96C03; -. DR BioMuta; MIEF2; -. DR DMDM; 74731298; -. DR EPD; Q96C03; -. DR jPOST; Q96C03; -. DR MassIVE; Q96C03; -. DR PaxDb; 9606-ENSP00000379057; -. DR PeptideAtlas; Q96C03; -. DR ProteomicsDB; 76139; -. [Q96C03-1] DR ProteomicsDB; 76140; -. [Q96C03-2] DR Antibodypedia; 49918; 86 antibodies from 18 providers. DR DNASU; 125170; -. DR Ensembl; ENST00000323019.9; ENSP00000323591.4; ENSG00000177427.13. [Q96C03-1] DR Ensembl; ENST00000395704.8; ENSP00000379056.4; ENSG00000177427.13. [Q96C03-2] DR Ensembl; ENST00000395706.2; ENSP00000379057.2; ENSG00000177427.13. [Q96C03-3] DR Ensembl; ENST00000640122.2; ENSP00000491181.1; ENSG00000284495.2. [Q96C03-1] DR Ensembl; ENST00000640339.1; ENSP00000492195.1; ENSG00000284495.2. [Q96C03-3] DR Ensembl; ENST00000640637.1; ENSP00000490984.1; ENSG00000284495.2. [Q96C03-2] DR GeneID; 125170; -. DR KEGG; hsa:125170; -. DR MANE-Select; ENST00000323019.9; ENSP00000323591.4; NM_139162.4; NP_631901.2. DR UCSC; uc002gst.4; human. [Q96C03-1] DR AGR; HGNC:17920; -. DR CTD; 125170; -. DR DisGeNET; 125170; -. DR GeneCards; MIEF2; -. DR HGNC; HGNC:17920; MIEF2. DR HPA; ENSG00000177427; Low tissue specificity. DR MalaCards; MIEF2; -. DR MIM; 615498; gene. DR MIM; 619024; phenotype. DR neXtProt; NX_Q96C03; -. DR OpenTargets; ENSG00000177427; -. DR PharmGKB; PA38265; -. DR VEuPathDB; HostDB:ENSG00000177427; -. DR eggNOG; ENOG502QPJX; Eukaryota. DR GeneTree; ENSGT00390000013127; -. DR HOGENOM; CLU_046803_0_0_1; -. DR InParanoid; Q96C03; -. DR OMA; LQDWYPA; -. DR OrthoDB; 2897585at2759; -. DR PhylomeDB; Q96C03; -. DR TreeFam; TF331032; -. DR PathwayCommons; Q96C03; -. DR SignaLink; Q96C03; -. DR BioGRID-ORCS; 125170; 17 hits in 1141 CRISPR screens. DR ChiTaRS; MIEF2; human. DR GenomeRNAi; 125170; -. DR Pharos; Q96C03; Tbio. DR PRO; PR:Q96C03; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q96C03; Protein. DR Bgee; ENSG00000177427; Expressed in hindlimb stylopod muscle and 100 other cell types or tissues. DR ExpressionAtlas; Q96C03; baseline and differential. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0007005; P:mitochondrion organization; IDA:UniProtKB. DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IDA:UniProtKB. DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB. DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB. DR Gene3D; 1.10.1410.40; -; 1. DR Gene3D; 3.30.460.90; -; 1. DR InterPro; IPR024810; Mab-21-like. DR InterPro; IPR046906; Mab-21_HhH/H2TH-like. DR InterPro; IPR045909; MID49/MID51. DR InterPro; IPR049097; MID51-like_C. DR PANTHER; PTHR16451:SF11; MITOCHONDRIAL DYNAMICS PROTEIN MID49; 1. DR PANTHER; PTHR16451; MITOCHONDRIAL DYNAMICS PROTEINS 49/51 FAMILY MEMBER; 1. DR Pfam; PF20266; Mab-21_C; 1. DR Pfam; PF21297; MID51-like_C; 1. DR SMART; SM01265; Mab-21; 1. DR Genevisible; Q96C03; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disease variant; Membrane; KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein; KW Primary mitochondrial disease; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..454 FT /note="Mitochondrial dynamics protein MID49" FT /id="PRO_0000310445" FT TOPO_DOM 1..22 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 23..43 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 44..454 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 76..119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1 FT /note="M -> MGLSPNLDRQTM (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_047650" FT VAR_SEQ 104..205 FT /note="EGPAETDPEVTPQLSSPAPLCLTLQERLLAFERDRVTIPAAQVALAKQLAGD FT IALELQAYFRSKFPELPFGAFVPGGPLYDGLQAGAADHVRLLVPLVLEPG -> GEAAG FT LRAGPCDHPSSPGGFGQTAGWRHRPGAAGLLSEQVPGTALWGIRAWGAALRRAAGGGCG FT PCASPGATGAGAGPVEPGAGRGHCGEGPSLLGRAQDAA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_029358" FT VAR_SEQ 206..454 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_029359" FT VARIANT 81..454 FT /note="Missing (in COXPD49; patient cells have reduced FT MIEF2 protein levels and show elongated mitochondria and FT increased mitochondrial fusion events)" FT /evidence="ECO:0000269|PubMed:29361167" FT /id="VAR_081553" FT VARIANT 324 FT /note="G -> E (in dbSNP:rs12603700)" FT /id="VAR_037038" FT VARIANT 354 FT /note="R -> Q (in dbSNP:rs3751981)" FT /id="VAR_037039" FT MUTAGEN 235 FT /note="R->E: Unable to associate with DNM1L into filaments FT forming the tubular structures that wrap around the FT scission site." FT /evidence="ECO:0000269|PubMed:29899447" FT CONFLICT 249 FT /note="L -> F (in Ref. 2; BAB71108)" FT /evidence="ECO:0000305" SQ SEQUENCE 454 AA; 49269 MW; CEE9A444C0F8BC04 CRC64; MAEFSQKRGK RRSDEGLGSM VDFLLANARL VLGVGGAAVL GIATLAVKRF IDRATSPRDE DDTKADSWKE LSLLKATPHL QPRPPPAALS QPVLPLAPSS SAPEGPAETD PEVTPQLSSP APLCLTLQER LLAFERDRVT IPAAQVALAK QLAGDIALEL QAYFRSKFPE LPFGAFVPGG PLYDGLQAGA ADHVRLLVPL VLEPGLWSLV PGVDTVARDP RCWAVRRTQL EFCPRGSSPW DRFLVGGYLS SRVLLELLRK ALAASVNWPA IGSLLGCLIR PSMASEELLL EVQHERLELT VAVLVAVPGV DADDRLLLAW PLEGLAGNLW LQDLYPVEAA RLRALDDHDA GTRRRLLLLL CAVCRGCSAL GQLGRGHLTQ VVLRLGEDNV DWTEEALGER FLQALELLIG SLEQASLPCH FNPSVNLFSS LREEEIDDIG YALYSGLQEP EGLL //