MID51_HUMAN
ID MID51_HUMAN Reviewed; 463 AA.
AC Q9NQG6; Q7L890; Q9BUI3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Mitochondrial dynamics protein MID51;
DE AltName: Full=Mitochondrial dynamics protein of 51 kDa;
DE AltName: Full=Mitochondrial elongation factor 1;
DE AltName: Full=Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like;
DE Short=SMCR7-like protein;
GN Name=MIEF1; Synonyms=MID51, SMCR7L;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-59, AND
RP IDENTIFICATION BY 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 [9]
RP SUBCELLULAR LOCATION, AND FUNCTION.
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 [10]
RP SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH DNM1L
RP AND FIS1, AND FUNCTION.
RX PubMed=21701560; DOI=10.1038/emboj.2011.198;
RA Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N.,
RA Shupliakov O., Lendahl U., Nister M.;
RT "Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes
RT mitochondrial fusion rather than fission.";
RL EMBO J. 30:2762-2778(2011).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
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 [14]
RP FUNCTION.
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP ALTERNATIVE INITIATION (ISOFORM 2).
RX PubMed=25621764; DOI=10.7554/elife.03971;
RA Andreev D.E., O'Connor P.B., Fahey C., Kenny E.M., Terenin I.M.,
RA Dmitriev S.E., Cormican P., Morris D.W., Shatsky I.N., Baranov P.V.;
RT "Translation of 5' leaders is pervasive in genes resistant to eIF2
RT repression.";
RL Elife 4:E03971-E03971(2015).
RN [17]
RP FUNCTION.
RX PubMed=29083303; DOI=10.7554/elife.27860;
RA Samandi S., Roy A.V., Delcourt V., Lucier J.F., Gagnon J., Beaudoin M.C.,
RA Vanderperre B., Breton M.A., Motard J., Jacques J.F., Brunelle M.,
RA Gagnon-Arsenault I., Fournier I., Ouangraoua A., Hunting D.J., Cohen A.A.,
RA Landry C.R., Scott M.S., Roucou X.;
RT "Deep transcriptome annotation enables the discovery and functional
RT characterization of cryptic small proteins.";
RL Elife 6:0-0(2017).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 119-463 IN COMPLEXES WITH ADP AND
RP GDP, NUCLEOTIDE-BINDING, FUNCTION, INTERACTION WITH DNM1L, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF HIS-201; ARG-235; 238-PRO--PRO-242; ARG-342;
RP LYS-368 AND LYS-372.
RX PubMed=24515348; DOI=10.1083/jcb.201311014;
RA Richter V., Palmer C.S., Osellame L.D., Singh A.P., Elgass K., Stroud D.A.,
RA Sesaki H., Kvansakul M., Ryan M.T.;
RT "Structural and functional analysis of MiD51, a dynamin receptor required
RT for mitochondrial fission.";
RL J. Cell Biol. 204:477-486(2014).
CC -!- FUNCTION: Mitochondrial outer membrane protein which regulates
CC mitochondrial fission. Promotes the recruitment and association of the
CC fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial
CC surface independently of the mitochondrial fission FIS1 and MFF
CC proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization.
CC Binds ADP and can also bind GDP, although with lower affinity. Does not
CC bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the
CC absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity
CC and the assembly of DNM1L into long, oligomeric tubules with a spiral
CC pattern, as opposed to the ring-like DNM1L oligomers observed in the
CC absence of bound ADP. Does not require ADP for its function in
CC recruiting DNM1L. {ECO:0000269|PubMed:21508961,
CC ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:23283981,
CC ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23921378,
CC ECO:0000269|PubMed:24515348, ECO:0000269|PubMed:29083303}.
CC -!- SUBUNIT: Homodimer. Interacts with DNM1L. {ECO:0000269|PubMed:21701560,
CC ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:24515348}.
CC -!- INTERACTION:
CC Q9NQG6; Q8WTS1: ABHD5; NbExp=5; IntAct=EBI-740987, EBI-2813554;
CC Q9NQG6; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-740987, EBI-741181;
CC Q9NQG6; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-740987, EBI-11522760;
CC Q9NQG6; P53365: ARFIP2; NbExp=3; IntAct=EBI-740987, EBI-638194;
CC Q9NQG6; O75915: ARL6IP5; NbExp=3; IntAct=EBI-740987, EBI-2860752;
CC Q9NQG6; P18859: ATP5PF; NbExp=3; IntAct=EBI-740987, EBI-2606700;
CC Q9NQG6; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-740987, EBI-11522780;
CC Q9NQG6; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-740987, EBI-1054315;
CC Q9NQG6; O00429: DNM1L; NbExp=11; IntAct=EBI-740987, EBI-724571;
CC Q9NQG6; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-740987, EBI-14240149;
CC Q9NQG6; Q9Y3D6: FIS1; NbExp=4; IntAct=EBI-740987, EBI-3385283;
CC Q9NQG6; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-740987, EBI-12937691;
CC Q9NQG6; P43355: MAGEA1; NbExp=7; IntAct=EBI-740987, EBI-740978;
CC Q9NQG6; Q969L2: MAL2; NbExp=3; IntAct=EBI-740987, EBI-944295;
CC Q9NQG6; Q13503: MED21; NbExp=3; IntAct=EBI-740987, EBI-394678;
CC Q9NQG6; Q9NQG6: MIEF1; NbExp=2; IntAct=EBI-740987, EBI-740987;
CC Q9NQG6; O60664: PLIN3; NbExp=3; IntAct=EBI-740987, EBI-725795;
CC Q9NQG6; O60831: PRAF2; NbExp=3; IntAct=EBI-740987, EBI-2506064;
CC Q9NQG6; Q16378: PRR4; NbExp=3; IntAct=EBI-740987, EBI-738624;
CC Q9NQG6; P25786: PSMA1; NbExp=3; IntAct=EBI-740987, EBI-359352;
CC Q9NQG6; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-740987, EBI-14065960;
CC Q9NQG6; P08247: SYP; NbExp=3; IntAct=EBI-740987, EBI-9071725;
CC Q9NQG6; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-740987, EBI-1044859;
CC Q9NQG6; P55327-2: TPD52; NbExp=3; IntAct=EBI-740987, EBI-12124194;
CC Q9NQG6; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-740987, EBI-10173939;
CC Q9NQG6; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-740987, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560,
CC ECO:0000269|PubMed:24515348}; Single-pass membrane protein
CC {ECO:0000269|PubMed:21508961, ECO:0000269|PubMed:21701560,
CC ECO:0000269|PubMed:24515348}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NQG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQG6-2; Sequence=VSP_056383, VSP_056384;
CC Name=3; Synonyms=uORF {ECO:0000303|PubMed:25621764}, AltMIEF1
CC {ECO:0000303|PubMed:29083303};
CC IsoId=L0R8F8-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expression is relatively high in heart, skeletal
CC muscle, pancreas and kidney. {ECO:0000269|PubMed:21701560}.
CC -!- SIMILARITY: Belongs to the SMCR7 family. {ECO:0000305}.
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DR EMBL; AL365515; CAB97211.1; -; mRNA.
DR EMBL; AK290954; BAF83643.1; -; mRNA.
DR EMBL; AL834205; CAD38892.2; -; mRNA.
DR EMBL; AL022312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60335.1; -; Genomic_DNA.
DR EMBL; BC002587; AAH02587.2; -; mRNA.
DR EMBL; BC008327; AAH08327.1; -; mRNA.
DR CCDS; CCDS13995.1; -. [Q9NQG6-1]
DR RefSeq; NP_001291493.1; NM_001304564.1.
DR RefSeq; NP_061881.2; NM_019008.5. [Q9NQG6-1]
DR RefSeq; XP_011528538.1; XM_011530236.1. [Q9NQG6-1]
DR RefSeq; XP_011528539.1; XM_011530237.1. [Q9NQG6-1]
DR RefSeq; XP_011528540.1; XM_011530238.1. [Q9NQG6-1]
DR RefSeq; XP_016884327.1; XM_017028838.1. [Q9NQG6-1]
DR PDB; 4NXT; X-ray; 2.12 A; A/B/C/D=119-463.
DR PDB; 4NXU; X-ray; 2.30 A; A/B/C/D=119-463.
DR PDB; 4NXV; X-ray; 2.30 A; A/B/C/D=119-463.
DR PDB; 4NXW; X-ray; 2.55 A; A=119-463.
DR PDB; 4NXX; X-ray; 2.55 A; A=119-463.
DR PDB; 5X9B; X-ray; 2.70 A; A=133-463.
DR PDB; 5X9C; X-ray; 1.85 A; A/B=133-463.
DR PDBsum; 4NXT; -.
DR PDBsum; 4NXU; -.
DR PDBsum; 4NXV; -.
DR PDBsum; 4NXW; -.
DR PDBsum; 4NXX; -.
DR PDBsum; 5X9B; -.
DR PDBsum; 5X9C; -.
DR AlphaFoldDB; Q9NQG6; -.
DR SMR; Q9NQG6; -.
DR BioGRID; 119977; 42.
DR IntAct; Q9NQG6; 35.
DR MINT; Q9NQG6; -.
DR STRING; 9606.ENSP00000327124; -.
DR iPTMnet; Q9NQG6; -.
DR PhosphoSitePlus; Q9NQG6; -.
DR BioMuta; MIEF1; -.
DR DMDM; 74752902; -.
DR EPD; Q9NQG6; -.
DR jPOST; Q9NQG6; -.
DR MassIVE; Q9NQG6; -.
DR MaxQB; Q9NQG6; -.
DR PaxDb; Q9NQG6; -.
DR PeptideAtlas; Q9NQG6; -.
DR PRIDE; Q9NQG6; -.
DR ProteomicsDB; 68833; -.
DR ProteomicsDB; 82149; -. [Q9NQG6-1]
DR Antibodypedia; 26626; 158 antibodies from 25 providers.
DR DNASU; 54471; -.
DR Ensembl; ENST00000325301.7; ENSP00000327124.2; ENSG00000100335.15. [Q9NQG6-1]
DR Ensembl; ENST00000404569.5; ENSP00000385191.1; ENSG00000100335.15. [Q9NQG6-1]
DR Ensembl; ENST00000428069.1; ENSP00000413730.1; ENSG00000100335.15. [Q9NQG6-2]
DR Ensembl; ENST00000433117.6; ENSP00000404096.2; ENSG00000100335.15. [Q9NQG6-2]
DR GeneID; 54471; -.
DR KEGG; hsa:54471; -.
DR MANE-Select; ENST00000325301.7; ENSP00000327124.2; NM_019008.6; NP_061881.2.
DR UCSC; uc003axx.4; human. [Q9NQG6-1]
DR CTD; 54471; -.
DR DisGeNET; 54471; -.
DR GeneCards; MIEF1; -.
DR HGNC; HGNC:25979; MIEF1.
DR HPA; ENSG00000100335; Low tissue specificity.
DR MIM; 615497; gene.
DR neXtProt; NX_Q9NQG6; -.
DR OpenTargets; ENSG00000100335; -.
DR PharmGKB; PA145148068; -.
DR VEuPathDB; HostDB:ENSG00000100335; -.
DR eggNOG; KOG4542; Eukaryota.
DR GeneTree; ENSGT00390000013127; -.
DR HOGENOM; CLU_1758184_0_0_1; -.
DR InParanoid; Q9NQG6; -.
DR OMA; CEKEGDW; -.
DR OrthoDB; 515815at2759; -.
DR PhylomeDB; Q9NQG6; -.
DR TreeFam; TF331032; -.
DR PathwayCommons; Q9NQG6; -.
DR SignaLink; Q9NQG6; -.
DR BioGRID-ORCS; 54471; 18 hits in 1068 CRISPR screens.
DR ChiTaRS; MIEF1; human.
DR GeneWiki; SMCR7L; -.
DR GenomeRNAi; 54471; -.
DR Pharos; Q9NQG6; Tbio.
DR PRO; PR:Q9NQG6; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NQG6; protein.
DR Bgee; ENSG00000100335; Expressed in sperm and 204 other tissues.
DR ExpressionAtlas; Q9NQG6; baseline and differential.
DR Genevisible; Q9NQG6; 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:0043531; F:ADP binding; IDA:MGI.
DR GO; GO:0019003; F:GDP binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0000266; P:mitochondrial fission; IMP: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 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 initiation; Alternative splicing; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..463
FT /note="Mitochondrial dynamics protein MID51"
FT /id="PRO_0000310448"
FT TOPO_DOM 1..23
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 49..195
FT /note="Dimerization"
FT REGION 57..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..169
FT /note="Important for interaction with DNM1L"
FT REGION 234..242
FT /note="Important for interaction with DNM1L"
FT BINDING 187
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 189
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 201
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 340
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 342
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT BINDING 368
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGV8"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 108..148
FT /note="DTFCPPRPKPVARKGQVDLKKSRLRMSLQEKLLTYYRNRAA -> GETSYLL
FT PEPGSHPCWRAGSGQASCCGHMCRAPELPAGQVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_056383"
FT VAR_SEQ 149..463
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_056384"
FT VARIANT 78
FT /note="G -> R (in dbSNP:rs2272830)"
FT /id="VAR_037040"
FT VARIANT 89
FT /note="T -> M (in dbSNP:rs17001213)"
FT /id="VAR_037041"
FT VARIANT 169
FT /note="R -> W (in dbSNP:rs2232088)"
FT /id="VAR_037042"
FT VARIANT 264
FT /note="D -> N (in dbSNP:rs2232091)"
FT /id="VAR_037043"
FT MUTAGEN 201
FT /note="H->D: Abolishes nucleotide-binding, but not DNM1L
FT recruitment; when associated with E-342; E-368 and E-372."
FT /evidence="ECO:0000269|PubMed:24515348"
FT MUTAGEN 235
FT /note="R->A: No effect on mitochondrial localization.
FT Impairs DNM1L recruitment."
FT /evidence="ECO:0000269|PubMed:24515348"
FT MUTAGEN 238..242
FT /note="Missing: No effect on mitochondrial localization.
FT Impairs DNM1L recruitment."
FT /evidence="ECO:0000269|PubMed:24515348"
FT MUTAGEN 342
FT /note="R->E: Abolishes nucleotide-binding, but not DNM1L
FT recruitment; when associated with D-201; E-368 and E-372."
FT /evidence="ECO:0000269|PubMed:24515348"
FT MUTAGEN 368
FT /note="K->E: Abolishes nucleotide-binding, but not DNM1L
FT recruitment; when associated with D-201; E-342 and E-372."
FT /evidence="ECO:0000269|PubMed:24515348"
FT MUTAGEN 372
FT /note="K->E: Abolishes nucleotide-binding, but not DNM1L
FT recruitment; when associated with D-201; E-342 and E-368."
FT /evidence="ECO:0000269|PubMed:24515348"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 151..175
FT /evidence="ECO:0007829|PDB:5X9C"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4NXT"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:5X9C"
FT TURN 189..193
FT /evidence="ECO:0007829|PDB:5X9C"
FT TURN 194..198
FT /evidence="ECO:0007829|PDB:5X9B"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:5X9C"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:5X9C"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5X9C"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4NXT"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:5X9C"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4NXW"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:5X9C"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:5X9C"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:5X9C"
FT STRAND 306..318
FT /evidence="ECO:0007829|PDB:5X9C"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:5X9C"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 382..395
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 404..421
FT /evidence="ECO:0007829|PDB:5X9C"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:5X9C"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 440..453
FT /evidence="ECO:0007829|PDB:5X9C"
FT HELIX 457..461
FT /evidence="ECO:0007829|PDB:5X9C"
SQ SEQUENCE 463 AA; 51293 MW; 0824AD44305C234D CRC64;
MAGAGERKGK KDDNGIGTAI DFVLSNARLV LGVGGAAMLG IATLAVKRMY DRAISAPTSP
TRLSHSGKRS WEEPNWMGSP RLLNRDMKTG LSRSLQTLPT DSSTFDTDTF CPPRPKPVAR
KGQVDLKKSR LRMSLQEKLL TYYRNRAAIP AGEQARAKQA AVDICAELRS FLRAKLPDMP
LRDMYLSGSL YDDLQVVTAD HIQLIVPLVL EQNLWSCIPG EDTIMNVPGF FLVRRENPEY
FPRGSSYWDR CVVGGYLSPK TVADTFEKVV AGSINWPAIG SLLDYVIRPA PPPEALTLEV
QYERDKHLFI DFLPSVTLGD TVLVAKPHRL AQYDNLWRLS LRPAETARLR ALDQADSGCR
SLCLKILKAI CKSTPALGHL TASQLTNVIL HLAQEEADWS PDMLADRFLQ ALRGLISYLE
AGVLPSALNP KVNLFAELTP EEIDELGYTL YCSLSEPEVL LQT
