MDM10_ASHGO
ID MDM10_ASHGO Reviewed; 465 AA.
AC Q758T7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Mitochondrial distribution and morphology protein 10 {ECO:0000255|HAMAP-Rule:MF_03102};
DE AltName: Full=Mitochondrial inheritance component MDM10 {ECO:0000255|HAMAP-Rule:MF_03102};
GN Name=MDM10 {ECO:0000255|HAMAP-Rule:MF_03102}; OrderedLocusNames=AEL335C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 464.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
CC molecular tether to connect the endoplasmic reticulum and mitochondria.
CC Components of this complex are involved in the control of mitochondrial
CC shape and protein biogenesis and may function in phospholipid exchange.
CC MDM10 is involved in the late assembly steps of the general translocase
CC of the mitochondrial outer membrane (TOM complex). Functions in the
CC TOM40-specific route of the assembly of outer membrane beta-barrel
CC proteins, including the association of TOM40 with the receptor TOM22
CC and 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 biogenesis
CC of all outer membrane beta-barrel proteins. May act as a switch that
CC shuttles between both complexes and channels precursor proteins into
CC the TOM40-specific pathway. Plays a role in mitochondrial morphology
CC and in the inheritance of mitochondria. {ECO:0000255|HAMAP-
CC Rule:MF_03102}.
CC -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. Associates
CC with the mitochondrial outer membrane sorting assembly machinery
CC SAM(core) complex. {ECO:0000255|HAMAP-Rule:MF_03102}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_03102}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03102}. 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_03102}.
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 -!- SIMILARITY: Belongs to the MDM10 family. {ECO:0000255|HAMAP-
CC Rule:MF_03102}.
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DR EMBL; AE016818; AAS52349.2; -; Genomic_DNA.
DR RefSeq; NP_984525.2; NM_209878.2.
DR AlphaFoldDB; Q758T7; -.
DR SMR; Q758T7; -.
DR STRING; 33169.AAS52349; -.
DR EnsemblFungi; AAS52349; AAS52349; AGOS_AEL335C.
DR GeneID; 4620695; -.
DR KEGG; ago:AGOS_AEL335C; -.
DR eggNOG; ENOG502QUN5; Eukaryota.
DR HOGENOM; CLU_026505_0_0_1; -.
DR InParanoid; Q758T7; -.
DR OMA; MLDFMDY; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0032865; C:ERMES complex; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0001401; C:SAM complex; IBA:GO_Central.
DR GO; GO:0051654; P:establishment of mitochondrion localization; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IBA:GO_Central.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IBA:GO_Central.
DR HAMAP; MF_03102; Mdm10; 1.
DR InterPro; IPR027539; Mdm10.
DR PANTHER; PTHR28035; PTHR28035; 1.
DR Pfam; PF12519; MDM10; 1.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transmembrane; Transmembrane beta strand.
FT CHAIN 1..465
FT /note="Mitochondrial distribution and morphology protein
FT 10"
FT /id="PRO_0000384160"
SQ SEQUENCE 465 AA; 52260 MW; 6DF27DBC5C418747 CRC64;
MIEYMEYVLR QFERTTSWDR DYSYENITAT SDNLLQFEIP DSLNLQISNQ STPNTFNTFE
LSNRSIINGS LSYLYTDCGQ LDKIVQNSLK VPLQQRVDTY QCLRPGRTLG TSFRSQMLLY
GRMYWPGSIL EAMYCKRLTP QSQLVLKSLL SAAGESSILT LYWQRNAPWG SQDIVFSTNE
LLLGYRFLHN LSPGRSHEGS PHGQSTLSLG AEFWLGISNL LPGCSTALRY CTHATNTGKP
ITLTLSLNPL FGHISSSYSV KFSPGTTFCS KYDFNVYSIE SNLSFGCEFW KSSAAAHKQA
TNEEETSIEV ATETPVSDPR YCGAVPGARS FDQIRPFAEL PSDNQLYHQL MMPNSSNALI
DNVNLPFPSP LLRYPPEKSV TDKFAAMIDA TQFTSVLKMS SSLRDKNLRL LWEGKYKGFL
VSAGAELTTI PLEAPKTINE ITAQQVPRPL WLRPAKFGIQ IQYST
