MD341_PENRW
ID MD341_PENRW Reviewed; 564 AA.
AC B6HQ08;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Mitochondrial distribution and morphology protein 34-1 {ECO:0000255|HAMAP-Rule:MF_03105};
GN Name=mdm34-1 {ECO:0000255|HAMAP-Rule:MF_03105}; ORFNames=Pc22g19660;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(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; AM920437; CAP99254.1; -; Genomic_DNA.
DR RefSeq; XP_002565868.1; XM_002565822.1.
DR AlphaFoldDB; B6HQ08; -.
DR SMR; B6HQ08; -.
DR STRING; 1108849.XP_002565868.1; -.
DR EnsemblFungi; CAP99254; CAP99254; PCH_Pc22g19660.
DR GeneID; 8315969; -.
DR KEGG; pcs:Pc22g19660; -.
DR VEuPathDB; FungiDB:PCH_Pc22g19660; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_036502_1_0_1; -.
DR OMA; QVVYRAW; -.
DR OrthoDB; 1120952at2759; -.
DR BioCyc; PCHR:PC22G19660-MON; -.
DR Proteomes; UP000000724; Contig Pc00c22.
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..564
FT /note="Mitochondrial distribution and morphology protein
FT 34-1"
FT /id="PRO_0000384354"
FT DOMAIN 1..195
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 297..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 61271 MW; 8C88171E71CD480F CRC64;
MAFKFNWSPL IADASFYTRA QDLLTAALNK SPKPPIIVGD ITVTELNLGS IPPELEILEI
GDLAEDRFRG IFKMSYTGDA FLTLKTRVQA NPLNTYLITR PSFASPLPLA AATPLTIPLQ
ITLSDFKLSG FVILVFSEQK GITLVFRNDP LESLKVSSTF DSIPFVRDFL QGEIEAQLRI
LFIDELPAII HRLSLQLWDP EYRAEEIQNQ MNTTLTPTKG PGHDPLVTPP QDPVDSLGNV
LDESDIASLS LDSAAETHSL FSQKNLLSLA TLTDSQRTLS LFTPSIQQVV YRAWSSPDQN
DSSASVMSPI SPPLSRTQSQ TGGIFASIDN ASTSSAQSRT PTGPTQSFSS YGLSLGASRH
SRAHARRRKK RVVDLRSRPT TPSDSASVSV SDESTYTESA SAPSVTSAPL QAIHEQPDDP
VTPPLSPESD QSLPAIVEER RLSLSRSLPR RDLSSEIVRD RAEPSEPRNP FNTDDVIVTV
GSVRPTPHQE ASPPLGPTRQ LSAAGLPFPH DSSTGSVVDQ VFLDTLAGEV ARRMRDEKLM
APNSCGTFCG HGLPEEPPPP AYGQ
