MDM34_LACBS
ID MDM34_LACBS Reviewed; 376 AA.
AC B0CXH5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 52.
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=LACBIDRAFT_245888;
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX NCBI_TaxID=486041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686;
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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; DS547094; EDR12723.1; -; Genomic_DNA.
DR RefSeq; XP_001876987.1; XM_001876952.1.
DR AlphaFoldDB; B0CXH5; -.
DR STRING; 486041.B0CXH5; -.
DR EnsemblFungi; EDR12723; EDR12723; LACBIDRAFT_245888.
DR GeneID; 6072040; -.
DR KEGG; lbc:LACBIDRAFT_245888; -.
DR HOGENOM; CLU_036502_0_0_1; -.
DR InParanoid; B0CXH5; -.
DR OrthoDB; 895124at2759; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
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: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 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..376
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384344"
FT DOMAIN 1..194
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 207..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 42439 MW; 5A6800A70B214E7C CRC64;
MSFTFNWPRF SDQFHYDAMQ MLNTALNKGN KPPIIADKIE VVELEMGTQP PELEIRDIGD
LTVDQFRGIF RLTYAGDAHL VLKTKVQANP LNHKQPDIHL MVGSGGMLAA KQPLVVPMLL
RLSHFRLSSY VVLVVSKQKG ITLVFKTDPL QNVDINSTFD SIAVIQKFIQ REIEGQLRQM
FREDLPGIIH RLSQQWVKAK VEAPYLSKHP PPPIPPEEIS EPGDYGEEGE FPFGSPPNHH
SLDPDPKIVL RPSLNNASIH QLSTLSHSNH TLSPYTRSLS HFTVRSVPPR GIGPSGLSAS
FERQPVKAKR KRTYRLGGRK PPPESVPAVP DSPERASSPI PPSEFDESDM DRYFRSYDDH
SRPPNIRQYR SHLHPS
