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Dynamin-like GTPase MGM1, mitochondrial (Mitochondrial division and morphology protein 17) (Mitochondrial genome maintenance protein 1) [Cleaved into: Dynamin-like GTPase MGM1 large isoform (l-MGM1); Dynamin-like GTPase MGM1 small isoform (s-MGM1)]

 MGM1_YEAST              Reviewed;         881 AA.
P32266; D6W2R7; Q02609; Q08627;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 3.
22-NOV-2017, entry version 158.
RecName: Full=Dynamin-like GTPase MGM1, mitochondrial;
AltName: Full=Mitochondrial division and morphology protein 17;
AltName: Full=Mitochondrial genome maintenance protein 1;
Contains:
RecName: Full=Dynamin-like GTPase MGM1 large isoform;
Short=l-MGM1;
Contains:
RecName: Full=Dynamin-like GTPase MGM1 small isoform;
Short=s-MGM1;
Flags: Precursor;
Name=MGM1; Synonyms=MDM17; OrderedLocusNames=YOR211C;
ORFNames=YOR50-1;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BJ41-8C;
PubMed=1532158; DOI=10.1101/gad.6.3.380;
Jones B.A., Fangman W.L.;
"Mitochondrial DNA maintenance in yeast requires a protein containing
a region related to the GTP-binding domain of dynamin.";
Genes Dev. 6:380-389(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7916673; DOI=10.1007/BF00324678;
Guan K., Farh L., Marshall T., Deschenes R.J.;
"Normal mitochondrial structure and genome maintenance in yeast
requires the dynamin-like product of the MGM1 gene.";
Curr. Genet. 24:141-148(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-784.
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8840505;
DOI=10.1002/(SICI)1097-0061(199607)12:9<877::AID-YEA969>3.0.CO;2-S;
Galisson F., Dujon B.;
"Sequence and analysis of a 33 kb fragment from the right arm of
chromosome XV of the yeast Saccharomyces cerevisiae.";
Yeast 12:877-885(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 713-881.
STRAIN=ATCC 28383 / FL100 / VTT C-80102;
PubMed=8516295; DOI=10.1073/pnas.90.12.5524;
Lalo D., Carles C., Sentenac A., Thuriaux P.;
"Interactions between three common subunits of yeast RNA polymerases I
and III.";
Proc. Natl. Acad. Sci. U.S.A. 90:5524-5528(1993).
[7]
PROTEIN SEQUENCE OF 60-67 AND 140-147, FUNCTION, SUBCELLULAR LOCATION,
AND TOPOLOGY.
STRAIN=ATCC 200060 / W303;
PubMed=12707284; DOI=10.1074/jbc.M211311200;
Herlan M., Vogel F., Bornhoevd C., Neupert W., Reichert A.S.;
"Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for
maintenance of mitochondrial morphology and of mitochondrial DNA.";
J. Biol. Chem. 278:27781-27788(2003).
[8]
FUNCTION, SUBUNIT, MUTAGENESIS OF SER-224 AND GLU-294, AND
IDENTIFICATION OF THE TRANSLATION INITIATION CODON.
PubMed=10037792; DOI=10.1083/jcb.144.4.711;
Shepard K.A., Yaffe M.P.;
"The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial
outer membrane to mediate mitochondrial inheritance.";
J. Cell Biol. 144:711-720(1999).
[9]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-223;
SER-224; THR-244; ARG-824 AND LYS-854.
PubMed=12566426; DOI=10.1083/jcb.200209015;
Wong E.D., Wagner J.A., Scott S.V., Okreglak V., Holewinske T.J.,
Cassidy-Stone A., Nunnari J.;
"The intramitochondrial dynamin-related GTPase, Mgm1p, is a component
of a protein complex that mediates mitochondrial fusion.";
J. Cell Biol. 160:303-311(2003).
[10]
INTERACTION WITH FZO1 AND UGO1.
PubMed=12808034; DOI=10.1091/mbc.E02-12-0788;
Sesaki H., Southard S.M., Yaffe M.P., Jensen R.E.;
"Mgm1p, a dynamin-related GTPase, is essential for fusion of the
mitochondrial outer membrane.";
Mol. Biol. Cell 14:2342-2356(2003).
[11]
FUNCTION, AND INTERACTION WITH UGO1.
PubMed=15087460; DOI=10.1074/jbc.M401363200;
Sesaki H., Jensen R.E.;
"Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion.";
J. Biol. Chem. 279:28298-28303(2004).
[12]
PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
GLY-79.
PubMed=15096522; DOI=10.1083/jcb.200403022;
Herlan M., Bornhoevd C., Hell K., Neupert W., Reichert A.S.;
"Alternative topogenesis of Mgm1 and mitochondrial morphology depend
on ATP and a functional import motor.";
J. Cell Biol. 165:167-173(2004).
[13]
SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16407407; DOI=10.1091/mbc.E05-08-0740;
Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
"Proteomic analysis of the yeast mitochondrial outer membrane reveals
accumulation of a subclass of preproteins.";
Mol. Biol. Cell 17:1436-1450(2006).
-!- FUNCTION: Dynamin-related GTPase required for mitochondrial
fusion. Coordinates interaction between the inner and outer
mitochondrial membrane to promote the formation of the double
membrane. {ECO:0000269|PubMed:10037792,
ECO:0000269|PubMed:12566426, ECO:0000269|PubMed:12707284,
ECO:0000269|PubMed:15087460}.
-!- SUBUNIT: Homooligomer. Associates with FZO1 through interaction
with the intermembrane space domain of UGO1 which binds FZO1
through its cytoplasmic domain. {ECO:0000269|PubMed:10037792,
ECO:0000269|PubMed:12566426, ECO:0000269|PubMed:16407407}.
-!- INTERACTION:
P38297:FZO1; NbExp=2; IntAct=EBI-10865, EBI-20900;
Q03327:UGO1; NbExp=2; IntAct=EBI-10865, EBI-32955;
-!- SUBCELLULAR LOCATION: Dynamin-like GTPase MGM1 large isoform:
Mitochondrion inner membrane {ECO:0000269|PubMed:15096522};
Single-pass type II membrane protein {ECO:0000255}; Intermembrane
side {ECO:0000305|PubMed:15096522}.
-!- SUBCELLULAR LOCATION: Dynamin-like GTPase MGM1 small isoform:
Mitochondrion inner membrane {ECO:0000269|PubMed:15096522};
Peripheral membrane protein {ECO:0000269|PubMed:15096522};
Intermembrane side.
-!- PTM: Cleavage of the transit peptide by mitochondrial processing
protease (MPP) produces a long integral membrane form of MGM1 (l-
MGM1). Further processing by the rhomboid protease PCP1 produces a
short peripheral membrane form of MGM1 (s-MGM1). Both isoforms are
required for full activity. {ECO:0000269|PubMed:15096522}.
-!- MISCELLANEOUS: Deletion of MGM1 causes the mitochondria to
fragment and aggregate, and subsequently to lose their
mitochondrial DNA and become respiration deficient.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA44637.1; Type=Frameshift; Positions=4; Evidence={ECO:0000305};
Sequence=CAA63174.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA99426.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA99428.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X62834; CAA44637.1; ALT_FRAME; Genomic_DNA.
EMBL; L07419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z75119; CAA99426.1; ALT_INIT; Genomic_DNA.
EMBL; Z75120; CAA99428.1; ALT_INIT; Genomic_DNA.
EMBL; X92441; CAA63174.1; ALT_INIT; Genomic_DNA.
EMBL; L11274; AAB59316.1; -; Genomic_DNA.
EMBL; BK006948; DAA10983.1; -; Genomic_DNA.
PIR; S33918; S33918.
RefSeq; NP_014854.2; NM_001183630.1.
ProteinModelPortal; P32266; -.
SMR; P32266; -.
BioGrid; 34606; 233.
DIP; DIP-8008N; -.
IntAct; P32266; 6.
MINT; MINT-1354456; -.
STRING; 4932.YOR211C; -.
TCDB; 9.B.25.1.1; the mitochondrial inner/outer membrane fusion (mmf) family.
MaxQB; P32266; -.
PRIDE; P32266; -.
EnsemblFungi; YOR211C; YOR211C; YOR211C.
GeneID; 854386; -.
KEGG; sce:YOR211C; -.
EuPathDB; FungiDB:YOR211C; -.
SGD; S000005737; MGM1.
GeneTree; ENSGT00550000074851; -.
HOGENOM; HOG000206760; -.
InParanoid; P32266; -.
KO; K22140; -.
OMA; KNKYYCP; -.
OrthoDB; EOG092C0L57; -.
BioCyc; YEAST:G3O-33713-MONOMER; -.
Reactome; R-SCE-169911; Regulation of Apoptosis.
PMAP-CutDB; P32266; -.
PRO; PR:P32266; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IDA:SGD.
GO; GO:0030061; C:mitochondrial crista; IDA:SGD.
GO; GO:0097002; C:mitochondrial inner boundary membrane; IDA:SGD.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; ISA:SGD.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0061025; P:membrane fusion; IDA:SGD.
GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
GO; GO:0008053; P:mitochondrial fusion; IDA:UniProtKB.
GO; GO:0000002; P:mitochondrial genome maintenance; IDA:UniProtKB.
GO; GO:0007006; P:mitochondrial membrane organization; IDA:UniProtKB.
GO; GO:0000001; P:mitochondrion inheritance; IDA:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
GO; GO:0016559; P:peroxisome fission; IBA:GO_Central.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR019762; Dynamin_GTPase_CS.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR020850; GED_dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11566; PTHR11566; 1.
Pfam; PF00350; Dynamin_N; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; GTP-binding; Hydrolase;
Membrane; Mitochondrion; Mitochondrion inner membrane;
Nucleotide-binding; Reference proteome; Signal-anchor;
Transit peptide; Transmembrane; Transmembrane helix.
TRANSIT 1 59 Mitochondrion.
{ECO:0000269|PubMed:12707284}.
CHAIN 60 881 Dynamin-like GTPase MGM1 large isoform.
/FTId=PRO_0000007400.
CHAIN 140 881 Dynamin-like GTPase MGM1 small isoform.
/FTId=PRO_0000007401.
TOPO_DOM 60 72 Mitochondrial matrix. {ECO:0000255}.
TRANSMEM 73 92 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 93 881 Mitochondrial intermembrane.
{ECO:0000255}.
DOMAIN 207 505 Dynamin-type G.
DOMAIN 780 872 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 217 224 GTP. {ECO:0000255}.
NP_BIND 317 321 GTP. {ECO:0000255}.
NP_BIND 385 388 GTP. {ECO:0000255}.
COMPBIAS 149 178 Asp-rich (acidic).
MUTAGEN 1 1 M->A: Abolishes translation.
MUTAGEN 39 39 M->A: No effect on translation.
MUTAGEN 79 79 G->D,K: Loss of function; most MGM1
processed to s-MGM1.
{ECO:0000269|PubMed:15096522}.
MUTAGEN 81 81 M->A: No effect on translation.
MUTAGEN 92 92 M->A: No effect on translation.
MUTAGEN 223 223 K->A: Loss of stability.
{ECO:0000269|PubMed:12566426}.
MUTAGEN 224 224 S->A: Loss of GTPase activity.
{ECO:0000269|PubMed:10037792,
ECO:0000269|PubMed:12566426}.
MUTAGEN 224 224 S->N: Loss of GTPase activity.
{ECO:0000269|PubMed:10037792,
ECO:0000269|PubMed:12566426}.
MUTAGEN 244 244 T->A: Loss of GTPase activity.
{ECO:0000269|PubMed:12566426}.
MUTAGEN 294 294 E->K: In mdm17; loss of function at 37
degrees Celsius.
{ECO:0000269|PubMed:10037792}.
MUTAGEN 824 824 R->A: Loss of GED function.
{ECO:0000269|PubMed:12566426}.
MUTAGEN 854 854 K->A: Loss of GED function.
{ECO:0000269|PubMed:12566426}.
CONFLICT 4 4 S -> T (in Ref. 1; CAA44637).
{ECO:0000305}.
CONFLICT 129 129 G -> C (in Ref. 1; CAA44637).
{ECO:0000305}.
CONFLICT 170 170 E -> A (in Ref. 2; L07419).
{ECO:0000305}.
SEQUENCE 881 AA; 99178 MW; 31524B40C5350096 CRC64;
MNASPVRLLI LRRQLATHPA ILYSSPYIKS PLVHLHSRMS NVHRSAHANA LSFVITRRSI
SHFPKIISKI IRLPIYVGGG MAAAGSYIAY KMEEASSFTK DKLDRIKDLG ESMKEKFNKM
FSGDKSQDGG HGNDGTVPTA TLIAATSLDD DESKRQGDPK DDDDEDDDDE DDENDSVDTT
QDEMLNLTKQ MIEIRTILNK VDSSSAHLTL PSIVVIGSQS SGKSSVLESI VGREFLPKGS
NMVTRRPIEL TLVNTPNSNN VTADFPSMRL YNIKDFKEVK RMLMELNMAV PTSEAVSEEP
IQLTIKSSRV PDLSLVDLPG YIQVEAADQP IELKTKIRDL CEKYLTAPNI ILAISAADVD
LANSSALKAS KAADPKGLRT IGVITKLDLV DPEKARSILN NKKYPLSMGY VGVITKTPSS
INRKHLGLFG EAPSSSLSGI FSKGQHGQSS GEENTNGLKQ IVSHQFEKAY FKENKKYFTN
CQVSTKKLRE KLIKILEISM SNALEPTSTL IQQELDDTSY LFKVEFNDRH LTPKSYLLNN
IDVLKLGIKE FQEKFHRNEL KSILRAELDQ KVLDVLATRY WKDDNLQDLS SSKLESDTDM
LYWHKKLELA SSGLTKMGIG RLSTMLTTNA ILKELDNILE STQLKNHELI KDLVSNTAIN
VLNSKYYSTA DQVENCIKPF KYEIDLEERD WSLARQHSIN LIKEELRQCN SRYQAIKNAV
GSKKLANVMG YLENESNLQK ETLGMSKLLL ERGSEAIFLD KRCKVLSFRL KMLKNKCHST
IEKDRCPEVF LSAVSDKLTS TAVLFLNVEL LSDFFYNFPI ELDRRLTLLG DEQVEMFAKE
DPKISRHIEL QKRKELLELA LEKIDSILVF KKSYKGVSKN L


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