MDM34_ASHGO
ID MDM34_ASHGO Reviewed; 590 AA.
AC Q755S6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Mitochondrial distribution and morphology protein 34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN Name=MDM34 {ECO:0000255|HAMAP-Rule:MF_03105}; OrderedLocusNames=AER442W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS53121.1; -; Genomic_DNA.
DR RefSeq; NP_985297.1; NM_210651.2.
DR AlphaFoldDB; Q755S6; -.
DR STRING; 33169.AAS53121; -.
DR PRIDE; Q755S6; -.
DR EnsemblFungi; AAS53121; AAS53121; AGOS_AER442W.
DR GeneID; 4621517; -.
DR KEGG; ago:AGOS_AER442W; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_036329_0_0_1; -.
DR InParanoid; Q755S6; -.
DR OMA; PGCLERQ; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0032865; C:ERMES complex; IBA:GO_Central.
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:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
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..590
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384323"
FT DOMAIN 1..225
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 393..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 65696 MW; 71F1F49122AE3B2F CRC64;
MSFIFNRETF EDNSFNEVLR EKLMRALNLH DRTVGSSSGA MTTGTGAVEC SGAAAAGQRP
PRSKGGFSKV DILKSGIIVK KVEFPTIPKL EILDLDVSIQ SKSLIKGICK VSCRDAMVQI
TTEIESNLLL LHVNSSPKFT TPKLISNDSF TVPITMTFDK LHLEAITNIF VKNTGVGISF
NDVNLDFRLQ CSIKLLQSSI EKRLKASMEE VFKDVLPSVI FNMSQRWFTH GETVVPTVDK
SMVSSDTPVQ PRMILDESDL SDLSPANMLR LSTLVSSRQT LCLNPTAVDT ISTIPGCLER
QNLHRFNLRF PSLYNYYSNK EQQGAHNNEK NRVEHLKLWG RSSSNPIPTR ASFKVENTLP
KEVLDSNSYD VRVITAIQTK MYERASNDVV LRRRKIKMRS RKPSKANKDA VSPAQNDSGT
SSCSNVASEL PHASLQANPQ SDEIDPAPEG GPNAEDAYKE ELEDSGLRAP QDFPALENVT
PVLAQLPNQQ RSRLGSPLSA GRPTPLLSPL DDSHWLLQKR DPQDLRTTLY SPIRNGRFYV
MPQPQLDTKE ASAFLLENGK RFGFVGLLNN HNLKWGNDPP PPYREVSITQ
