MDM34_ASPFN
ID MDM34_ASPFN Reviewed; 566 AA.
AC B8N0Q7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=AFLA_025920;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963473; EED55320.1; -; Genomic_DNA.
DR RefSeq; XP_002374102.1; XM_002374061.1.
DR AlphaFoldDB; B8N0Q7; -.
DR SMR; B8N0Q7; -.
DR STRING; 5059.CADAFLAP00001967; -.
DR EnsemblFungi; EED55320; EED55320; AFLA_025920.
DR VEuPathDB; FungiDB:AFLA_025920; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_036502_1_0_1; -.
DR OMA; FKMSYAG; -.
DR Proteomes; UP000001875; 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; Transmembrane; Transmembrane beta strand;
KW Transport.
FT CHAIN 1..566
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384325"
FT DOMAIN 1..195
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 212..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 61987 MW; 7BDF7FA4193ACE32 CRC64;
MAFNFNWSPL MADASFYTRA QDLLTAALNK SPKPPIIVDD IIVTELNLGS IPPDLEILEI
GDLAEDRFRG IFKMSYTGDA FLTLKTRVQA NPLNTYLLTR PSFASPLPLA AATPLTIPLQ
ITLSDFKLSG FVILVFSKQK GITVVFRNDP LESLKVSSTF DSIPFVRDFL QREIEAQLRI
LFMDELPAII HRLSLRLWVP EYRAGEDIQT QPEQTAGEGP GQDPLASPPQ DPVDSLGNAL
DESEIASLSL DSSVEAHSLF SQKNLLRLGA LTDSQRTLSL FTPSIQEVVY RAWTSPSEQG
DANGISTAPL SPMLSRTHSQ VGSMSSFQDS ASIVSSQSRS SASTHTFSGY GLNLGAGRHS
KAHSRKRKKR VVDLRRPKTT SDTASVSDES AYTETASNPS VCSAPLPVVN EQPDPITPPL
SPESDFRLPA IPERRRASLS RPVPRRDIAT EMLRETGGPS AEPPRHRPQP ADVDATPRGS
LRAHITAQHD NEKQETGPSR QLPSTILPFT DEKSSSSTVD QALVERLAGE IARRMRDEKL
MPTSSCGGAF WGRPDHEEYP PPAYGQ
