MID49_MOUSE
ID MID49_MOUSE Reviewed; 454 AA.
AC Q5NCS9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Mitochondrial dynamics protein MID49;
DE AltName: Full=Mitochondrial dynamics protein of 49 kDa homolog;
DE AltName: Full=Mitochondrial elongation factor 2;
DE AltName: Full=Smith-Magenis syndrome chromosomal region candidate gene 7 protein homolog;
GN Name=Mief2; Synonyms=Gm11, Mid49, Smcr7;
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 [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION.
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 [5]
RP LACK OF NUCLEOTIDE-BINDING, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24508339; DOI=10.1016/j.str.2014.01.001;
RA Loson O.C., Liu R., Rome M.E., Meng S., Kaiser J.T., Shan S.O., Chan D.C.;
RT "The mitochondrial fission receptor Mid51 requires ADP as a cofactor.";
RL Structure 22:367-377(2014).
CC -!- FUNCTION: Mitochondrial outer membrane protein which regulates
CC mitochondrial organization. It is required for mitochondrial fission
CC and promotes the recruitment and association of the fission mediator
CC dynamin-related protein 1 (DNM1L) to the mitochondrial surface
CC independently of the mitochondrial fission FIS1 and MFF proteins.
CC Regulates DNM1L GTPase activity. {ECO:0000269|PubMed:23283981,
CC ECO:0000269|PubMed:24508339}.
CC -!- SUBUNIT: Interacts with DNM1L. {ECO:0000250}.
CC -!- INTERACTION:
CC Q5NCS9; Q8K1M6-3: Dnm1l; NbExp=2; IntAct=EBI-16092669, EBI-16092613;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:24508339}; Single-pass membrane protein
CC {ECO:0000269|PubMed:24508339}. Note=Colocalizes with DNM1L at
CC mitochondrial membrane. Forms foci and rings around mitochondria.
CC -!- MISCELLANEOUS: Does not bind ADP or other nucleotides, in contrast to
CC MIEF1.
CC -!- SIMILARITY: Belongs to the MID49/MID51 family. {ECO:0000305}.
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DR EMBL; AK156917; BAE33897.1; -; mRNA.
DR EMBL; AL596215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC088984; AAH88984.1; -; mRNA.
DR CCDS; CCDS24796.1; -.
DR RefSeq; NP_001009927.1; NM_001009927.2.
DR PDB; 4WOY; X-ray; 2.40 A; A/B=126-454.
DR PDBsum; 4WOY; -.
DR AlphaFoldDB; Q5NCS9; -.
DR SMR; Q5NCS9; -.
DR DIP; DIP-60661N; -.
DR IntAct; Q5NCS9; 1.
DR STRING; 10090.ENSMUSP00000018743; -.
DR iPTMnet; Q5NCS9; -.
DR PhosphoSitePlus; Q5NCS9; -.
DR EPD; Q5NCS9; -.
DR MaxQB; Q5NCS9; -.
DR PaxDb; Q5NCS9; -.
DR PRIDE; Q5NCS9; -.
DR ProteomicsDB; 292324; -.
DR Antibodypedia; 49918; 73 antibodies from 18 providers.
DR Ensembl; ENSMUST00000018743; ENSMUSP00000018743; ENSMUSG00000018599.
DR GeneID; 237781; -.
DR KEGG; mmu:237781; -.
DR UCSC; uc007jgj.1; mouse.
DR CTD; 125170; -.
DR MGI; MGI:2144199; Mief2.
DR VEuPathDB; HostDB:ENSMUSG00000018599; -.
DR eggNOG; ENOG502QPJX; Eukaryota.
DR GeneTree; ENSGT00390000013127; -.
DR HOGENOM; CLU_046803_0_0_1; -.
DR InParanoid; Q5NCS9; -.
DR OMA; CLTLQEK; -.
DR OrthoDB; 515815at2759; -.
DR PhylomeDB; Q5NCS9; -.
DR TreeFam; TF331032; -.
DR BioGRID-ORCS; 237781; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Mief2; mouse.
DR PRO; PR:Q5NCS9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5NCS9; protein.
DR Bgee; ENSMUSG00000018599; Expressed in knee joint and 189 other tissues.
DR Genevisible; Q5NCS9; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS: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; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..454
FT /note="Mitochondrial dynamics protein MID49"
FT /id="PRO_0000310446"
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..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 143..167
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4WOY"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4WOY"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 251..264
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:4WOY"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 298..307
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 335..349
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 353..366
FT /evidence="ECO:0007829|PDB:4WOY"
FT TURN 368..372
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 375..386
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 397..413
FT /evidence="ECO:0007829|PDB:4WOY"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:4WOY"
FT TURN 427..430
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 433..442
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:4WOY"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:4WOY"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:4WOY"
SQ SEQUENCE 454 AA; 49624 MW; 11CF1EF2C2CAB666 CRC64;
MAEFSQKQRK QSGSEGLGSV VDFLLANARL VLGVGGAAVL GIATLAVKRL IDRATSPPDE
DDTKGDSWKE LSLLRATSPQ KPQPPPAAFS QPLATGSPSP SVPVEPTPIH SPTTPKFSTI
APLCLTFQER LLAFERKHVI TPEAHVTLAK QLAGDIALEL QAYLRSKFPE LPFGALVPGG
PLYDGLQAGT AEHVRLLAPL ELEPGLWSLV PGVDTVAREP RCWAVRRTQL EFHPRGCSPW
DRFLVGGYLS SRVLLELLRK ALSASVNWPA IGSLLGCLIW PDVASEELLL KVQHECLEFT
LAVLMVVPGA STDDRLLLAW PLEGLASNLW LQDLYPVETA RLRALDDQDA GTRRRLLLLL
CGICRGHPAL VRLGWSHLTQ VVLHLGEEEV AWTEEALGER FLQALEFLVG SLEQASLPCH
FNPSVNLLGN FREEEIDDIG YVLYSGLQVP ESLF
