MDM34_LACTC
ID MDM34_LACTC Reviewed; 542 AA.
AC C5DLL1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=KLTH0G01562g;
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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; CU928171; CAR24672.1; -; Genomic_DNA.
DR RefSeq; XP_002555109.1; XM_002555063.1.
DR AlphaFoldDB; C5DLL1; -.
DR STRING; 559295.C5DLL1; -.
DR EnsemblFungi; CAR24672; CAR24672; KLTH0G01562g.
DR GeneID; 8293367; -.
DR KEGG; lth:KLTH0G01562g; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_036329_0_0_1; -.
DR InParanoid; C5DLL1; -.
DR OMA; PGCLERQ; -.
DR OrthoDB; 888882at2759; -.
DR Proteomes; UP000002036; Chromosome G.
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..542
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384345"
FT DOMAIN 1..216
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 27..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 60252 MW; 23111B5DB5715B1C CRC64;
MSFRFNKGAF EDNSFNEQIR EALTSALNSK TQSSSQTAPA NTTNSAATDE VKQETRGPKR
LDILKSGISV SKVNFPSTPQ LEILDLDVSA QSRSLLKGIC KVSCKNAMLE INTEIEANLL
LLYTNDGPSF TTPRLISNDS FTVPITMTFN QIELEAITNI FVKNNSVGIS FNDVNLDFDF
DCSIKLLQSS IEKRLKGSME TVFKEVLPSV IFSMSQRWFT HGESTCNSAS DDKSAGRQVE
NHSHTPRTIL EDCDLEDLSP ANMLRLSTLV SSRQSLSLNP TAMNTLSTIP GCLERQNLHR
FNSRIPALSN FYPDFYEVES PHLKAFGRSV STNVISSGKL EHHNALPQRV LDERSYDLKT
IASVQSRIFE RSSGDGTAIR RRKIKMGKKS KSKKAQSQDI ENSSPTVVMP SSPSLEPSAV
STPEALHSPQ PTTAVQSPEL LAENSESVSI PALILPTQAD HYTLPVKTSA PKLNLLEEAH
YLNRKREFQK LRTSLYSPIR SNRFNLNKEM ERPILEHKGL NFVGLTHGLN WGSEDLPPPY
RG
