MDM34_DEBHA
ID MDM34_DEBHA Reviewed; 556 AA.
AC Q6BUS9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Mitochondrial distribution and morphology protein 34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN Name=MDM34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN OrderedLocusNames=DEHA2C08338g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382135; CAG86107.1; -; Genomic_DNA.
DR RefSeq; XP_458040.1; XM_458040.1.
DR AlphaFoldDB; Q6BUS9; -.
DR STRING; 4959.XP_458040.1; -.
DR EnsemblFungi; CAG86107; CAG86107; DEHA2C08338g.
DR GeneID; 2900306; -.
DR KEGG; dha:DEHA2C08338g; -.
DR VEuPathDB; FungiDB:DEHA2C08338g; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_476594_0_0_1; -.
DR InParanoid; Q6BUS9; -.
DR OMA; PGCLERQ; -.
DR OrthoDB; 999167at2759; -.
DR Proteomes; UP000000599; Chromosome C.
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..556
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384341"
FT DOMAIN 1..205
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
SQ SEQUENCE 556 AA; 62871 MW; 5C6270B1DAC320CB CRC64;
MSFNVNWNSL ETESLSSWTK ELLTDALNSG KRPNILASGI QIKDLNFGKV GPSFEILEIG
ELDKDRFRGI FKINYEGDFH LTLHTKVQAN PLKIYSSNSL DREVNQFDEM NNFVTPDFLL
CNDPFALPLD LKLSDIKISG IGIIVFSQTK GLTLVFRNDP LDSIKVSSTF DTVQVLANFL
QSQIEDQIGD LFRETLPTLI HELSLKYTSL NESNFSDLQS KLKSKMNNLD TEDLEKISIN
DVNSEFNYSS TNLRKNMNLF NSRETLNLSI PKLKNIVQRS HLEKFNKHLP NLVSTLNLNL
NLPDVNVNNN IAPSQNNNCI PIDLLINNNN NLENILTEIS SIQTSSYYNK LNSNNNGSKP
NRRVIKLGGK KSKKASSANP LDQTPEYSEV STLIDDSMEH STIEHSTFES PVSLEHANLI
DLKQPKPMRC TRDISIDTSK PILSHSHFHA NGNSNTNSPH HPNSSLLRGV GLGNNYFNFT
SNQQISTSHI ENDEDRLMNK KSNNYIDIKS INNKSVDSKN IDQWKKLDFD KASLRQNCSS
PQHNVFEVPP PPPYQY
