ID   MDM34_CANAL             Reviewed;         623 AA.
AC   Q59MC8; A0A1D8PDR8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-MAY-2023, entry version 87.
DE   RecName: Full=Mitochondrial distribution and morphology protein 34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN   Name=MDM34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN   OrderedLocusNames=CAALFM_C106230CA; ORFNames=CaO19.1826, CaO19.9385;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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. 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}.
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DR   EMBL; CP017623; AOW26285.1; -; Genomic_DNA.
DR   RefSeq; XP_710877.2; XM_705785.2.
DR   AlphaFoldDB; Q59MC8; -.
DR   BioGRID; 1230606; 2.
DR   STRING; 237561.Q59MC8; -.
DR   EnsemblFungi; C1_06230C_A-T; C1_06230C_A-T-p1; C1_06230C_A.
DR   GeneID; 3647517; -.
DR   KEGG; cal:CAALFM_C106230CA; -.
DR   CGD; CAL0000184363; MDM34.
DR   VEuPathDB; FungiDB:C1_06230C_A; -.
DR   eggNOG; ENOG502QT3W; Eukaryota.
DR   HOGENOM; CLU_476594_0_0_1; -.
DR   InParanoid; Q59MC8; -.
DR   OrthoDB; 10496at2759; -.
DR   PRO; PR:Q59MC8; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0032865; C:ERMES complex; IBA:GO_Central.
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   CDD; cd21673; SMP_Mdm34; 1.
DR   HAMAP; MF_03105; Mdm34; 1.
DR   InterPro; IPR027536; Mdm34.
DR   InterPro; IPR031468; SMP_LBD.
DR   PANTHER; PTHR28185; MITOCHONDRIAL DISTRIBUTION AND MORPHOLOGY PROTEIN 34; 1.
DR   PANTHER; PTHR28185:SF1; MITOCHONDRIAL DISTRIBUTION AND MORPHOLOGY PROTEIN 34; 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..623
FT                   /note="Mitochondrial distribution and morphology protein
FT                   34"
FT                   /id="PRO_0000384333"
FT   DOMAIN          1..204
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT   REGION          364..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  70239 MW;  699AAAEA6DD3FD24 CRC64;
     MSFKVNWNSL ETEPLTNWTK ELLTSALNSG KSPNILALNI TIKDLNFGKI APDFEILEIG
     ELDRDRFRGI FKIDYQGDFH LTLHTKVQAN PLNIYYHNSL EKEVCNYSQD EFITPNFLLS
     NEQFAIPLDL KLSDIKINGI GIIVFSKSKG LTLVFRNDPL DSIKVSSTFD TVQVLANFLQ
     KQIENQIRDL FRETLPTLIH QLSLKYLSLD NNINEIKSKL SQQDSVSMTN NELASSLKLF
     DDEENEFPLI YSSKNLQKNM QLFKSRETFR LSAPKFKNIV QRTRLDKFTK SYPNLLNSLY
     ANNADLQHRF VNNINHGHNN NSNTSSTGIP IELLVSHDDK QHYGKTDNLL KDISSIQANN
     FYKYSNKDAP NKPKRRRIKV HKKSKVKQDD NTVKASELQN VDSTFMESRS ISPQETIDTT
     STLIESAPMT RNVSTNIKSP TLETMSTGSS SSASSQVIAH PTPKRAHQPA DSTVSTTTIN
     KENHIDYIKA RNLYQDFIQM SQSPGYYDKV ISNGRGIGLG NSGGNYFGFN GNGNGLERTM
     SASPIKHLNK DKKSINYIDT SKINEKLNQF RLDGGKNSAN TNNSSGGKNF RPGFTRNESN
     GQQGILFEAF NFPSVAPPPP PYC
//