ID   MDM34_USTMA             Reviewed;        1097 AA.
AC   Q4PFA7; A0A0D1E6T6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Mitochondrial distribution and morphology protein 34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN   Name=MDM34 {ECO:0000255|HAMAP-Rule:MF_03105}; ORFNames=UMAG_01206;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_03105}.
CC   -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC       or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34.
CC       {ECO:0000255|HAMAP-Rule:MF_03105}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03105}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_03105}. 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_03105}.
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:0000255|HAMAP-Rule:MF_03105}.
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_03105}.
CC   -!- SIMILARITY: Belongs to the MDM34 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03105}.
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; CM003141; KIS71306.1; -; Genomic_DNA.
DR   RefSeq; XP_011387143.1; XM_011388841.1.
DR   AlphaFoldDB; Q4PFA7; -.
DR   STRING; 5270.UM01206P0; -.
DR   EnsemblFungi; KIS71306; KIS71306; UMAG_01206.
DR   GeneID; 23562299; -.
DR   KEGG; uma:UMAG_01206; -.
DR   VEuPathDB; FungiDB:UMAG_01206; -.
DR   eggNOG; ENOG502QT3W; Eukaryota.
DR   HOGENOM; CLU_010017_0_0_1; -.
DR   InParanoid; Q4PFA7; -.
DR   OMA; MEHFTVR; -.
DR   OrthoDB; 307378at2759; -.
DR   Proteomes; UP000000561; Chromosome 2.
DR   GO; GO:0032865; C:ERMES complex; IBA:GO_Central.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR   GO; GO:0007005; P:mitochondrion organization; 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   HAMAP; MF_03105; Mdm34; 1.
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..1097
FT                   /note="Mitochondrial distribution and morphology protein
FT                   34"
FT                   /id="PRO_0000384367"
FT   DOMAIN          1..198
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT   REGION          204..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..672
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..800
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        923..949
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1025
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1062
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1097 AA;  116499 MW;  01DC5D1CA232E923 CRC64;
     MSFNFKWPTF SDEFHTSAAQ MLNSALNRGP KPKVIADDIL VEELGMGTIP PELEILEIGD
     LGTDRFRGIF RLTYAGDAHL VLKTKVQANP LSKPNRPDIG LFPSSNASRG ILFAAAPLIV
     PMHLRLSSVK LRAIVVLVVS KAKGITLVFK NDPLESVEVS STFDSVAVIQ KYLQQEIEGQ
     LREMFREDLP GIIHRLSQKW LSGEAKSEKD KVKQKAEAEE PPARSREPTL TRSTSEPLVA
     LETASAPGGT PRKSHSKAKK HSRSGASVAD FAASPCQSPQ RPRQSPRRPR HVAKAASTSA
     VPLHSEFSAT HASPFDAAFP DIENYDPTYG LRPDDLPTHS GFSGLGRLAQ RGLGGLKDLT
     ASPVFDLDTA LGAADVDLDG AAVFEDLNRQ SDDEGSEAEQ SQDAHSSSHD GKHDEGDATT
     DSDLDAVLHD VGDDVSDLDV QERDNLVDTS IDYSRFGYPP ASAAFSDAHE LTRASSIIFD
     DQPQLTRKHS KRGSVSGRSS TRARRPSSSR SDRSACTSSL RKREEAEVVY ETIPAVGGGI
     VTRPRVYHIA SKVQPPEVDW DDEDTARPSQ YGGTPSTRTG TTRFGSDYGS ATMGAQSSRT
     NTVRGIHDLP HLNSAFVSRD GSEESLIDLP PESYHSSDAS LPHALDAERS SVSGSDSRRG
     LTNPTSRESS YRDLSSQDLH WDHSASSTAP SSSQSLHWDM HSRNDAAART VNVKAGQNAE
     SNSGLSFRKN KSANHQRSIT LGGGGGGGFP LRRPGEGPGM SATPARTRAS AAASARSRPG
     FITYATSPPG DSSGWQRSPP LRASSDRDVA FSTSPGVAQD MLSISPFRDS SLHHGSPRET
     SNVAGAYASA SNSPYTSGHN KGTQGAGAAP THLSIDASAH FLDLVKSNHT LSPFTRSMEH
     FTVRSAPVTP GWQTASGNVS VVGSSAASGT GTTSGSSQTG ANAKSGKAGS DKTRSQDHLS
     VGHTVAEPKT HCQADSAAPS SGLPARRRRT FQLGGSSSRD DTASNKPNNT STGQGEDSQD
     NSAAPGSDDY GFARYAGSGP QPFRASGSSA SSAITDSSSK GNRLGSKDLR RRSRPGSMGP
     PSEAARLSAL RWEAIRE