MD342_PENRW
ID MD342_PENRW Reviewed; 556 AA.
AC B6HR25;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Mitochondrial distribution and morphology protein 34-2 {ECO:0000255|HAMAP-Rule:MF_03105};
GN Name=mdm34-2 {ECO:0000255|HAMAP-Rule:MF_03105}; ORFNames=Pc22g12080;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP98496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM920437; CAP98496.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002565154.1; XM_002565108.1.
DR AlphaFoldDB; B6HR25; -.
DR SMR; B6HR25; -.
DR STRING; 1108849.XP_002565154.1; -.
DR EnsemblFungi; CAP98496; CAP98496; PCH_Pc22g12080.
DR GeneID; 8309543; -.
DR KEGG; pcs:Pc22g12080; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_036502_1_0_1; -.
DR OrthoDB; 1120952at2759; -.
DR BioCyc; PCHR:PC22G12080-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..556
FT /note="Mitochondrial distribution and morphology protein
FT 34-2"
FT /id="PRO_0000384355"
FT DOMAIN 1..195
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 206..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..377
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 61260 MW; BFEF196742654F59 CRC64;
MAFNFNWSPL MADASFYTRA QDLLTAALNK SPKPPIIVDD IHVTELNLGS IPPELEILEI
GDLAEDRFRG IFKMSYTGDA FLTLKTRVQA NPLNTFLLTR PTFGSPVPLA AATPLTIPLQ
ITLSDFKLSG FVILVFSKQK GITVVFRNDP LESLKVSSTF DSIPFVRDFL QKEIEAQLRI
LFMDELPAII HRLSLRLWVP EYRTGEEMND ETDNTAKSSE GPGQDPLASP PQDPVDSLGN
ALNESEIASL SLDSSVETHS LFSQKNLLRL AALTDSQRTL SLFTPSIQEV VYRAWTSPTD
TSEFPSSVIS PLSPTLSREQ SQMGSMSSLH ETASNASMQS RPSMSSHSFS TSTYGLSLGA
GRHSKAHARK RKKRVVDLRR PKTTDDAMSV SDESVMTESS RPPSIASAPL PIVNEPSDDP
VTPPLSPEVD CHLPIIPERH LPSFSRPTRR DADLSYSHET IRGPKAEDVD ATPRATMRGY
PQERAEAGPS SNQRTPLPAA VLPFSKDENA NVDPVLVDRL AGEIARRMRE DKLMTNACSG
FWSRQHEDSP PPAYGH
