ID   MDM10_SCHPO             Reviewed;         370 AA.
AC   O13814;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 118.
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; ORFNames=SPAC17H9.17c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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   -!- INTERACTION:
CC       O13814; P28040: pol1; NbExp=2; IntAct=EBI-849180, EBI-455823;
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; CU329670; CAB11226.1; -; Genomic_DNA.
DR   PIR; T37882; T37882.
DR   RefSeq; NP_593586.1; NM_001019018.2.
DR   AlphaFoldDB; O13814; -.
DR   SMR; O13814; -.
DR   BioGRID; 278847; 2.
DR   IntAct; O13814; 2.
DR   STRING; 4896.SPAC17H9.17c.1; -.
DR   SwissPalm; O13814; -.
DR   MaxQB; O13814; -.
DR   PaxDb; O13814; -.
DR   EnsemblFungi; SPAC17H9.17c.1; SPAC17H9.17c.1:pep; SPAC17H9.17c.
DR   GeneID; 2542383; -.
DR   KEGG; spo:SPAC17H9.17c; -.
DR   PomBase; SPAC17H9.17c; mdm10.
DR   VEuPathDB; FungiDB:SPAC17H9.17c; -.
DR   eggNOG; ENOG502QUN5; Eukaryota.
DR   HOGENOM; CLU_026505_0_0_1; -.
DR   InParanoid; O13814; -.
DR   OMA; MLDFMDY; -.
DR   PhylomeDB; O13814; -.
DR   PRO; PR:O13814; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0032865; C:ERMES complex; ISO:PomBase.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0001401; C:SAM complex; ISO:PomBase.
DR   GO; GO:0120014; F:phospholipid transfer activity; IC:PomBase.
DR   GO; GO:0051654; P:establishment of mitochondrion localization; IBA:GO_Central.
DR   GO; GO:0120010; P:intermembrane phospholipid transfer; IC:PomBase.
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; 2.
DR   Pfam; PF12519; MDM10; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW   Transmembrane; Transmembrane beta strand.
FT   CHAIN           1..370
FT                   /note="Mitochondrial distribution and morphology protein
FT                   10"
FT                   /id="PRO_0000372307"
SQ   SEQUENCE   370 AA;  42199 MW;  816B6B246DC51DAB CRC64;
     MMSFNDYIFY EYLKKTNWNI HNLYCNLTQT ADNILNFEIP SGVSCQLSSL TSSNFASGCK
     ISAMPILNGS MSYVYTNVNL ENLNRNITYN LQHFYEGYKH VDVPFVHYVN EFQDKKLPLR
     PTLLYGRMHL PSQHLDAIFA TRLSPWLLFF IQGVNEIEDG VGDNLCFNWQ YDTGKRCLEF
     VYESSGAMLG VRGLWNLNYR ELNTKINMEN KAPSNMRWSL GFETYYGVLT KCAGASLGMR
     LHSGPSHPYA PFILTCTLNP IVGHITSTFS TAEPRTKAFS AQYDFNIYSY ESQLKLGIEL
     WRSKQEMSQS TNDPTANSMS SLLKGTCSTS GDVSISWQAR IRNFLLTIGT EAQLTKIDPL
     FFGVHFEYSK