MDM34_MAGO7
ID MDM34_MAGO7 Reviewed; 550 AA.
AC A4QT54; G4N4Z7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Mitochondrial distribution and morphology protein 34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN Name=MDM34 {ECO:0000255|HAMAP-Rule:MF_03105}; ORFNames=MGG_05176;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
CC molecular tether to connect the endoplasmic reticulum (ER) and
CC mitochondria. Components of this complex are involved in the control of
CC mitochondrial shape and protein biogenesis, and function in
CC nonvesicular lipid trafficking between the ER and mitochondria. MDM34
CC is required for the interaction of the ER-resident membrane protein
CC MMM1 and the outer mitochondrial membrane-resident beta-barrel protein
CC MDM10. {ECO:0000255|HAMAP-Rule:MF_03105}.
CC -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34.
CC {ECO:0000255|HAMAP-Rule:MF_03105}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_03105}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03105}. Note=The ERMES/MDM complex localizes to a few discrete
CC foci (around 10 per single cell), that represent mitochondria-
CC endoplasmic reticulum junctions. These foci are often found next to
CC mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03105}.
CC -!- DOMAIN: Lacks alpha-helical transmembrane segments, suggesting that it
CC resides in the membrane via beta-sheet conformations similar to those
CC predicted for other outer membrane proteins and porin.
CC {ECO:0000255|HAMAP-Rule:MF_03105}.
CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind
CC various types of glycerophospholipids in its interior and mediate their
CC transfer between two adjacent bilayers. {ECO:0000255|HAMAP-
CC Rule:MF_03105}.
CC -!- SIMILARITY: Belongs to the MDM34 family. {ECO:0000255|HAMAP-
CC Rule:MF_03105}.
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DR EMBL; CM001233; EHA52908.1; -; Genomic_DNA.
DR RefSeq; XP_003712715.1; XM_003712667.1.
DR AlphaFoldDB; A4QT54; -.
DR SMR; A4QT54; -.
DR STRING; 318829.MGG_05176T0; -.
DR PRIDE; A4QT54; -.
DR EnsemblFungi; MGG_05176T0; MGG_05176T0; MGG_05176.
DR GeneID; 2675592; -.
DR KEGG; mgr:MGG_05176; -.
DR VEuPathDB; FungiDB:MGG_05176; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_036502_1_0_1; -.
DR InParanoid; A4QT54; -.
DR OMA; FKMSYAG; -.
DR OrthoDB; 1120952at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; ISS:PAMGO_MGG.
DR GO; GO:0032865; C:ERMES complex; IEA:UniProtKB-UniRule.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:PAMGO_MGG.
DR GO; GO:0005739; C:mitochondrion; ISS:PAMGO_MGG.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0007005; P:mitochondrion organization; ISS:PAMGO_MGG.
DR HAMAP; MF_03105; Mdm34; 1.
DR InterPro; IPR027536; Mdm34.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR28185; PTHR28185; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Lipid transport; Lipid-binding; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane beta strand; Transport.
FT CHAIN 1..550
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384347"
FT DOMAIN 1..208
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 294..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 60405 MW; 1F54769A2A60030F CRC64;
MAFNFNWSPL TADASFYKRA RDLLTTALNK SPKPPIIVDD ILVTEFNLGS VPPELEILEI
GDLAEDRFRG IFKMTYSGDA FLTLKTRVQA NPLNTYLYSK PSFTSPEPLA AASGLTIPLQ
ITLSEIKLSA FIILVFSKQK GLTLVFRNDP LESLKVSSTF DSIQFVRDYL QRTIEGKLRN
LMMDELPAII HKLSLQLWCP EQMSKEDHEK TNEMDEQAVN PFASPPLDAV DAHGNLLDPI
DISSIAVNGG AELQSLFSQK NLFRLGNLVN TQLTSSLFTP SVPEVIFRAK AGPVDKPEAS
STTPLTTPSL VKSHSFHGTS TVYTFSDTSS QNNGQLPSRP SLVSLGSATT GLGLAASRNA
KPYANRKKKT RVVNLRRKTD TAASSEMGDT MSDSASVQAS ESITMSDSIP EDPEEQPELT
MSGSSRVRFG LGGERSALPQ RPALRRDLFN PDEATASAEI SQPQVARSTP EKETAAPVRT
SENDKRSDSK RRGPRSETPS VILEQAWIMK MAGEIAKRVY DEKQRNPSFW DEREDSPPPA
YEAQPTTAAS
