MDM34_ASPTN
ID MDM34_ASPTN Reviewed; 565 AA.
AC Q0CZY7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
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}; ORFNames=ATEG_00747;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU39393.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAU39393.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CH476594; EAU39393.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001210833.1; XM_001210833.1.
DR AlphaFoldDB; Q0CZY7; -.
DR SMR; Q0CZY7; -.
DR STRING; 341663.Q0CZY7; -.
DR GeneID; 4355502; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR OrthoDB; 1120952at2759; -.
DR Proteomes; UP000007963; 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..565
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000384330"
FT DOMAIN 1..195
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 207..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..504
FT /note="Disordered"
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..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 62340 MW; 30113F18EECF79F3 CRC64;
MAFNFNWSPL MADASFYTRA QDLLTAALNK SPKPPIIVDD IIVTELNLGS IPPELEILEI
GDLAEDRFRG IFKMSYSGDA FLTLKTRVQA NPLNTYLLTR PSFASPLPLA AATPLTIPLQ
ITLSDFKLSG FVILVFSKQK GITVVFRNDP LESLKVSSTF DSIPFVRDFL QREIEAQLRI
LFMDELPAII HRLSLRLWVP EYRAGEEDQD QNTNTAGEGP GQDPLASPPQ DPVDALGNAL
NESEIASLSL DSSVETHSLF SQKNLLRLAA LTDSQRTLSL FTPSIQEVVY RAWTSPSDQG
DISGGVTSPL SPALSRTQSQ VGGMSSFQDN ASTISSYSRT STSTHTFSTY GLNLGAGRHS
KAHARKRKKR VVDLRRPKQP ESETASVTDE SSFTETTSAP SVRSAPLPRV NEQPDDPVTP
PLSPDSDFHL PPIPERHRFS ISRPALRRDI ATEMLRETGE SSSEPARRHA EVDDIDATPR
TIIRHEPSRY EGEKQEAGPS RQLPSTILPF TEEKSTPGPV DQALVERIAG EIARRMREDK
LMGTNSCAFW NRPGHEESPP PAYGQ
