ID   MDM10_CRYNJ             Reviewed;         508 AA.
AC   P0CO66; Q55HP7; Q5K784;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 47.
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=CNN00750;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AE017356; AAW47220.1; -; Genomic_DNA.
DR   RefSeq; XP_568737.1; XM_568737.1.
DR   AlphaFoldDB; P0CO66; -.
DR   STRING; 5207.AAW47220; -.
DR   PaxDb; P0CO66; -.
DR   EnsemblFungi; AAW47220; AAW47220; CNN00750.
DR   VEuPathDB; FungiDB:CNN00750; -.
DR   eggNOG; ENOG502QUN5; Eukaryota.
DR   HOGENOM; CLU_026505_1_0_1; -.
DR   InParanoid; P0CO66; -.
DR   OMA; MLDFMDY; -.
DR   OrthoDB; 1463552at2759; -.
DR   Proteomes; UP000002149; Chromosome 14.
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..508
FT                   /note="Mitochondrial distribution and morphology protein
FT                   10"
FT                   /id="PRO_0000384177"
FT   REGION          160..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..191
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  56456 MW;  CC43FF6DB88C12F1 CRC64;
     MIGFSAFILR NYYAAIGWNE DNLYSSLTRT SSALLDFQLP QSLILQLANS PTPIFFTSYA
     LDALPQLNGS ISYITTSMPL DEIGSGRATA FKNVIERFRV FPPPKRPQPK DEVWLGGKRI
     EGRDYLLYSR LHLPSLHLSG LATTRLTPTL QAHLAFLSQP AHPTSTRPTP PQTPPSHTRQ
     PSEPSTPAPS PTPGNVFISL QHDTGRYCGE YTYSVQDGMV GLRTLYNFGW HGDEESEVDK
     KERREREGKR IDEEEMMEGG LKGRFSAGGE VYFSAKQRSF GISTGLRFTT VPPTLPLPLN
     APVPSPPTTL TLLYNPLIGF LSSAYSAQVS PTVALATRFG VNVYSYESDL SVGGEWWIGR
     RRGKRGLTTD AEPQLDAESR DPVVTGIEEN RELTEKMAQR ASLRQVTLRD EIGEDVHAEK
     ELYSPIPVMT DVNAGELAQQ ISPRLQPQQD LDDERDGVLK ARLSGNWQFA LLYEARIRNC
     LVSAGVLADL TGRQHPIRSI GLEVQYFS