MID49_HUMAN
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 03-AUG-2022, entry version 139.
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}.
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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 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; Q96C03; -.
DR PeptideAtlas; Q96C03; -.
DR PRIDE; Q96C03; -.
DR ProteomicsDB; 76139; -. [Q96C03-1]
DR ProteomicsDB; 76140; -. [Q96C03-2]
DR Antibodypedia; 49918; 73 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 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; CLTLQEK; -.
DR OrthoDB; 515815at2759; -.
DR PhylomeDB; Q96C03; -.
DR TreeFam; TF331032; -.
DR PathwayCommons; Q96C03; -.
DR SignaLink; Q96C03; -.
DR BioGRID-ORCS; 125170; 17 hits in 1064 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 99 other tissues.
DR ExpressionAtlas; Q96C03; baseline and differential.
DR Genevisible; Q96C03; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; 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 InterPro; IPR024810; Mab-21_dom.
DR InterPro; IPR045909; MID49/MID51.
DR PANTHER; PTHR16451; PTHR16451; 1.
DR Pfam; PF03281; Mab-21; 1.
DR SMART; SM01265; Mab-21; 1.
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
