GenomeNet

Database: UniProt
Entry: T5AFL7_OPHSC
LinkDB: T5AFL7_OPHSC
Original site: T5AFL7_OPHSC 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system