ID T5AFL7_OPHSC Unreviewed; 1030 AA.
AC T5AFL7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000256|HAMAP-Rule:MF_03103};
GN Name=MMM1 {ECO:0000256|HAMAP-Rule:MF_03103};
GN ORFNames=OCS_03087 {ECO:0000313|EMBL:EQL01201.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL01201.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQL01201.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQL01201.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
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:0000256|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:0000256|HAMAP-Rule:MF_03103}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03103}; Single-pass type I membrane protein
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_03103}.
CC -!- SIMILARITY: Belongs to the MMM1 family. {ECO:0000256|HAMAP-
CC Rule:MF_03103}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
CC {ECO:0000256|ARBA:ARBA00009884}.
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DR EMBL; KE652551; EQL01201.1; -; Genomic_DNA.
DR AlphaFoldDB; T5AFL7; -.
DR eggNOG; KOG1299; Eukaryota.
DR HOGENOM; CLU_294413_0_0_1; -.
DR Proteomes; UP000019374; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032865; C:ERMES complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd21671; SMP_Mmm1; 1.
DR Gene3D; 1.25.40.60; -; 1.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR HAMAP; MF_03103; Mmm1; 1.
DR InterPro; IPR027537; Mmm1.
DR InterPro; IPR019411; MMM1_dom.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR11679:SF3; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 45; 1.
DR PANTHER; PTHR11679; VESICLE PROTEIN SORTING-ASSOCIATED; 1.
DR Pfam; PF10296; MMM1; 1.
DR Pfam; PF00995; Sec1; 1.
DR SUPFAM; SSF56815; Sec1/munc18-like (SM) proteins; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03103};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03103};
KW Reference proteome {ECO:0000313|Proteomes:UP000019374};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_03103};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03103};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TOPO_DOM 1..638
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT TOPO_DOM 660..1030
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT DOMAIN 732..948
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 990..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 114595 MW; E2E3363DD9F86237 CRC64;
MDVSQAVADY ISRIVTPSGT SSSAKMKILL LDRETVSIVS TAVTQSSLLN YEVYLIDRLE
NATRDKMRHL RCICLVRPSP ETIQLLVDEL REPKYGEYHI YFTNVAKKSS LERLAEADDH
EVVKGVQEHF ADYTVINPDL FTLGFSLPQW RIWAGSPDTW NPEALQRCAE GLFAVLLSLK
KKPLVRFERS STLAKKLASE VRYLMSQEEQ LFDFRKVDTP PLLLILDRRE DPITPLLTQW
TYQAMVHHLL GIQNGRVDLS EVPDIRSELR EVVLSQDQDP FFKKNMFLNF GDLGGSIKEY
VEQYQSKTKT NTDIESISDM KRFIEEYPEF RKLSGNVSKH VTLVSELSRR VAAENLLEVS
ETEQSLACND NHSSDLKNIQ RLVQTPSVTA GAKVGLIALY ALRYDKHPSN ALPMLTELLV
TAGGVSPRHA DMPNKLLTYH SSLHTTQPNG GISEIFESAG IFSGASSRFK GLKGVENVYT
QHTTLLESTL QNLIKGRLKE QRYPFMEGSG STRDKPQDII VFMIGGATYE EAKMIAGINA
TTPGVRVVLG GTSMHNAATF LEEVEAVAGL RSRANQVGVV FGSRPEGPAT ETSSGWARAP
QEQQALIAWP EIYVGCFSRR EPDQADAQDS YKLSFTQGLI VGQLSVVLIL AAFIKFFIFG
DPPSSDATSS LRATERRART LAHKQSLLSL RSSSQRQGQA LSRKKSSVLR NQPALTIGSI
LSKTYYNVDS HQPESLDWFN VLVAQTIAQF RSDAQHDDAI LDSLTKALNG TSRPDFVDDI
RVTELSLGND FPIFSNCRII PVDEDGLTLG NGIKFDAASA ARDGTRLQAR MDVDLSDMLT
LAVETKLLLN YPKRLSAVLP VALSVSVVRF SGTLSISFIP SNPSQSSPTM MTFSFLDDYR
LDFSIRSLLG SRSRLQDVPK IAQLVEARLH RWFDERAVEP RFQEIALPSM WPRKKNTRGP
DDALADGVGS VGRARGREIG RDVRDEVPLG DNEWREATPS LRHRRPTNAR EEGDFTISGS
LPGAKIGAMS
//