ID MDM10_PENMQ Reviewed; 477 AA. AC B6Q6B6; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 24-NOV-2009, entry version 6. DE RecName: Full=Mitochondrial distribution and morphology protein 10; DE AltName: Full=Mitochondrial inheritance component mdm10; GN Name=mdm10; ORFNames=PMAA_033940; OS Penicillium marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; OC mitosporic Trichocomaceae; Penicillium. OX NCBI_TaxID=441960; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Fedorova N.D., Joardar V.S., Maiti R., Schobel S., Amedeo P., RA Galens K., Inman J.M., White O.R., Whitty B.R., Wortman J.R., RA Nierman W.C.; RT "Genome sequence of Penicillium marneffei strain ATCC 18224."; RL Submitted (OCT-2007) 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 and CC mitochondria. Components of this complex are involved in the CC control of mitochondrial shape and protein biogenesis and may CC function in phospholipid exchange. mdm10 is involved in the late CC assembly steps of the general translocase of the mitochondrial CC outer membrane (TOM complex). Functions in the tom40-specific CC route of the assembly of outer membrane beta-barrel proteins, CC including the association of tom40 with the receptor tom22 and CC small TOM proteins. Can associate with the SAM(core) complex as CC well as the mdm12-mmm1 complex, both involved in late steps of the CC major beta-barrel assembly pathway, that is responsible for CC biogenesis of all outer membrane beta-barrel proteins. May act as CC a switch that shuttles between both complexes and channels CC precursor proteins into the tom40-specific pathway. Plays a role CC in mitochondrial morphology and in the inheritance of mitochondria CC (By similarity). CC -!- SUBUNIT: Component of the ER-mitochondria encounter structure CC (ERMES) or MDM complex, composed of mmm1, mdm10, mdm12 and mdm34 CC (By similarity). Associates with the mitochondrial outer membrane CC sorting assembly machinery SAM(core) complex (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass CC membrane protein (By similarity). Note=The ERMES/MDM complex CC localizes to a few discrete foci (around 10 per single cell), that CC represent mitochondria-endoplasmic reticulum junctions. These foci CC are often found next to mtDNA nucleoids (By similarity). CC -!- DOMAIN: Lacks alpha-helical transmembrane segments, suggesting CC that it resides in the membrane via beta-sheet conformations CC similar to those predicted for other outer membrane proteins and CC porin. CC -!- SIMILARITY: Belongs to the MDM10 family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS995899; EEA28591.1; -; Genomic_DNA. DR RefSeq; XP_002145106.1; -. DR GeneID; 7022843; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell. PE 3: Inferred from homology; KW Membrane; Mitochondrion; Mitochondrion outer membrane; Transmembrane. FT CHAIN 1 477 Mitochondrial distribution and morphology FT protein 10. FT /FTId=PRO_0000384190. SQ SEQUENCE 477 AA; 50884 MW; 5B5935DD4F70A53E CRC64; MLEFMDYVQL AFAEATRWNQ DNSYSALTAT AESLLDFHVP ERLQVRLSSL STPHFATSYT LGTVGLIDGS VSYLFSTVPL NNTPSQSGLI PLRRLVRGYR QIEAPVPPRR NWGWDAIPSP NSLQNIDGAE NNDDVVRKAT LLHATLHLPP PSTLNALFLR RISPTTQITA SLVSTQAPPL VKSAPSAALL AQISHDTGTF SNEYLFSTDN ALFGWRGLWN IGLEPAPGKA STDKVSLLSA GAEAYYSPIS SLVGLSTGLK FTTLPAASRT PSSSSSGSTP NPISSFPYTL TLTLTPLTGS LSTTYSARAS PNLAFSSRFG FNVYSWESEM VAGCEIWRKS PRTEPVEVDD GLEWARRKMG IVKDLAAEKI SSLSSSNNPQ AIEEDEGDSV IKIRVDQSWN VRLLWEGRVK SLLVTAGVSL GPGSFTALSS IPSSPTSSSA PVAAAGTGSS QSSGGGAAPT SRPSYWQGVG VSILYSS //