MDM34_ASPCL
ID MDM34_ASPCL Reviewed; 572 AA.
AC A1CHU1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=ACLA_049180;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(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; DS027054; EAW10446.1; -; Genomic_DNA.
DR RefSeq; XP_001271872.1; XM_001271871.1.
DR AlphaFoldDB; A1CHU1; -.
DR STRING; 5057.CADACLAP00004894; -.
DR EnsemblFungi; EAW10446; EAW10446; ACLA_049180.
DR GeneID; 4704031; -.
DR KEGG; act:ACLA_049180; -.
DR VEuPathDB; FungiDB:ACLA_049180; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_036502_1_0_1; -.
DR OMA; FKMSYAG; -.
DR OrthoDB; 1120952at2759; -.
DR Proteomes; UP000006701; 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..572
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384324"
FT DOMAIN 1..195
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 210..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..373
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 62578 MW; CEF92EB5A9C3F18E CRC64;
MAFNFNWSPL MADASFYTRA QDLLTAALNK SPKPPIIVDD IIVTELNLGS IPPELEILEI
GDLAEDRFRG IFKMSYSGDA FLTLKTRVQA NPLNTYLLTR PSFATPLPLA AATPLTIPLQ
ITLSDIKLSG FVILVFSKQK GITVVFRNDP LESLKVSSTF DSIPFVRDFL QKEIEAQLRI
LFMDELPAII HRLSLRLWVP EYRAGEDFET QAEKAETANG EGPGQDPLAS PPQDPVDALG
HALDESDIAS LSLDSSVEAH SLFSQKNLLR LAALTDSQRT LSLFTPSIRE VVYRAWTSPT
DQTDAAGSVT SPVLSRTHSQ VGSMSSFQDS ASIASMQTRS STPSHTFSGY GLSLGAGRHS
KAHSRKRKKR VVDLRRPKTT DDAPSVSDES AFTESTSAPS VCSAPLPILN EQSDDPVTPP
LSPDNDLHLP IIPDRHRMSI SRPAPRRDIA AEMMRDMGGP SSTSDPATQA TQSEDTSATP
RATMRAQIPS IYLNEKQDAG SSTGVPRQLP SAILPFLNDN PMNRVVDQAL VERLAGEIAR
RMRDEKFMAT NACGSFWDRH SQEESPPPAY GH
