ID   MDM34_COPC7             Reviewed;         823 AA.
AC   A8NYS9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Mitochondrial distribution and morphology protein 34;
GN   Name=MDM34; ORFNames=CC1G_01424;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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. MDM34
CC       is required for the interaction of the ER-resident membrane protein
CC       MMM1 and the outer mitochondrial membrane-resident beta-barrel protein
CC       MDM10. {ECO:0000250|UniProtKB:P53083}.
CC   -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC       or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34.
CC       {ECO:0000250|UniProtKB:P53083}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P53083}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P53083}. Note=The ERMES/MDM complex localizes to
CC       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:0000250|UniProtKB:P53083}.
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       {ECO:0000250|UniProtKB:P53083}.
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|PROSITE-
CC       ProRule:PRU01194}.
CC   -!- SIMILARITY: Belongs to the MDM34 family. {ECO:0000305}.
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DR   EMBL; AACS02000005; EAU84428.2; -; Genomic_DNA.
DR   RefSeq; XP_001837512.2; XM_001837460.2.
DR   AlphaFoldDB; A8NYS9; -.
DR   STRING; 5346.XP_001837512.2; -.
DR   EnsemblFungi; EAU84428; EAU84428; CC1G_01424.
DR   GeneID; 6014069; -.
DR   KEGG; cci:CC1G_01424; -.
DR   VEuPathDB; FungiDB:CC1G_01424; -.
DR   eggNOG; ENOG502QT3W; Eukaryota.
DR   HOGENOM; CLU_010017_0_0_1; -.
DR   InParanoid; A8NYS9; -.
DR   OMA; RIPRMPP; -.
DR   OrthoDB; 895124at2759; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
DR   GO; GO:0032865; C:ERMES complex; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:InterPro.
DR   InterPro; IPR027536; Mdm34.
DR   InterPro; IPR031468; SMP_LBD.
DR   PANTHER; PTHR28185; PTHR28185; 1.
DR   PROSITE; PS51847; SMP; 1.
PE   3: Inferred from homology;
KW   Lipid transport; Lipid-binding; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   CHAIN           1..823
FT                   /note="Mitochondrial distribution and morphology protein
FT                   34"
FT                   /id="PRO_0000384339"
FT   DOMAIN          1..88
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT   REGION          97..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..823
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   823 AA;  88429 MW;  276AC396AD482103 CRC64;
     MLAAKQPLVV PMHLRLSHFR LSSYVVLVVS KQKGITIVFK TDPLQNVDIN STFDSIAVIQ
     SFIQREIEGQ LRQMFREDLP SIIHRLSQQW VKAKVETPYK KQNQDSLQKA PPPTPTEPVP
     RPLGISRSRS AGHALETMST PDLSAPQFDR RRTAASDIHG PAFLRPPLAT APRRPQSTTG
     ISVAGRGSPL SAPPITHPTN SSTSTITSTS TAAEPSTFPD LEHFDPTYGL RPEGLPTKPV
     FKGFSKLFAP NKGLADLAEE ISSQSSSVAD GDSDYLSSGS ATDEEEYERN SYDFVEWGST
     TGPNTTPPEP VVEYETIPAI GGGTITRPRV VHAQSQIQLP PGVSPVASSP SRNVATVLSR
     TGSGSNGSRS GAVTPGILSR NPSNPYFADR LAALPHIYRP QNISSGPLSA PPIASSSRRP
     FSLAGGYDGH EDVKMKQRAS YAYSVHEEAV YMQHTGGAVN RYPHPYDLER HRYQSESKYD
     DEDIEDYSDE EDNGRGPHHY HPRAHRTRHE AHDDYFTSRH PSASVPPSSP PRSSARPPST
     IKRRLSVSSN TTNRTSFSAS SAYKHHHPNH SSLSLDPSSS ISNHPGNDKA KIVLRPSLLN
     NSIHHLSTLS HSNHTLSPYT RSFEHFAVRS GPPRGSGAAS AVVKSGSGSG IPTPSTSGAG
     GGSGMAGGGI GLASGSGGGS LGRAKGLTTT AGIVGLGAAT SRLGKTKADV VPKARRKRVF
     RIGGKKPEDN SNAAPGETDT RNVSREEYGA DEIGEGYVEG LGHASGRAGS QMGKRPRPRH
     RKKPSYAASG TDFDEADMDR YFKSMHDAEE EATPVPRSKD RRP