(data stored in ACNUC7421 zone)

SWISSPROT: MMM1_ASPFU

ID   MMM1_ASPFU              Reviewed;         496 AA.
AC   Q4WDE0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   11-DEC-2019, entry version 74.
DE   RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000255|HAMAP-Rule:MF_03103};
GN   Name=mmm1 {ECO:0000255|HAMAP-Rule:MF_03103}; ORFNames=AFUA_6G04420;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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. The
CC       mdm12-mmm1 subcomplex functions in the major beta-barrel assembly
CC       pathway that is responsible for biogenesis of all outer membrane beta-
CC       barrel proteins, and acts in a late step after the SAM complex. The
CC       mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway
CC       after the action of the mdm12-mmm1 complex. Essential for establishing
CC       and maintaining the structure of mitochondria and maintenance of mtDNA
CC       nucleoids. {ECO:0000255|HAMAP-Rule:MF_03103}.
CC   -!- SUBUNIT: Homodimer. Component of the ER-mitochondria encounter
CC       structure (ERMES) or MDM complex, composed of mmm1, mdm10, mdm12 and
CC       mdm34. A mmm1 homodimer associates with one molecule of mdm12 on each
CC       side in a pairwise head-to-tail manner, and the SMP-LTD domains of mmm1
CC       and mdm12 generate a continuous hydrophobic tunnel for phospholipid
CC       trafficking. {ECO:0000255|HAMAP-Rule:MF_03103}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03103}; Single-pass type I membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03103}. Note=The ERMES/MDM complex localizes
CC       to a few discrete foci (around 10 per single cell), that represent
CC       mitochondria-endoplasmic reticulum junctions. These foci are often
CC       found next to mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03103}.
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_03103}.
CC   -!- SIMILARITY: Belongs to the MMM1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03103}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL85598.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AAHF01000012; EAL85598.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_747636.1; XM_742543.1.
DR   SMR; Q4WDE0; -.
DR   STRING; 746128.CADAFUBP00009124; -.
DR   PRIDE; Q4WDE0; -.
DR   GeneID; 3505297; -.
DR   KEGG; afm:AFUA_6G04420; -.
DR   EuPathDB; FungiDB:Afu6g04420; -.
DR   HOGENOM; HOG000201075; -.
DR   InParanoid; Q4WDE0; -.
DR   KO; K17764; -.
DR   OrthoDB; 1248004at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0032865; C:ERMES complex; IBA:GO_Central.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IBA:GO_Central.
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_03103; Mmm1; 1.
DR   InterPro; IPR027537; Mmm1.
DR   InterPro; IPR019411; MMM1_dom.
DR   InterPro; IPR031468; SMP_LBD.
DR   PANTHER; PTHR13466:SF5; PTHR13466:SF5; 1.
DR   Pfam; PF10296; MMM1; 1.
DR   PROSITE; PS51847; SMP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WDE0.
DR   SWISS-2DPAGE; Q4WDE0.
KW   Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..496
FT                   /note="Maintenance of mitochondrial morphology protein 1"
FT                   /id="PRO_0000384214"
FT   TOPO_DOM        1..22
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   TOPO_DOM        44..496
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   DOMAIN          131..388
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
SQ   SEQUENCE   496 AA;  53664 MW;  EB10261E78BD005E CRC64;
     MSSQLNDPTP IPAQSSLSFT QGFLLGQLSV VLLIAAFIKF FIFGEAPPPP SRGLSHRSAT
     HRRSNSIFSS AQHDGSTRTL REKPSNSNVL RPVPSSATNT RSILRKTYYT AIPTNPSSKH
     GRHRIHHSSH QPESLDWFNV LIAQTIAQYR QTAYLLKDSP TSSILNSLTA ALNNPEKKPS
     FIDKITVTDI SLGEEFPIFS NCRIIAVDDP NSDGGRLQAL MDVDLSDDNL SIAVETQLLL
     NYPKPCSAIL PVALSISVVR FSGTLCISLV PASTPPLDTP SHSPSPPTAQ TTTAGRSKRE
     DQTSGSHSHA GGSSKEPSGE NPPKTSPKSN VAFSFLPDYR LDLSVRSLIG SRSRLQDVPK
     VAQLVEARVH AWFEERVVEP RVQVVGLPDL WPRMGRTGVR TGDDSETGSN VPRSSTAADA
     SGSARHEDSS REPEVLRFGS LLGTRPPFDL ASRTSSFNVE TGDLRSRSMT REESNGNLSD
     QFHMPGSLPG SGVATT
//

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