ID   SHE9_LODEL              Reviewed;         508 AA.
AC   A5DVB1;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Sensitive to high expression protein 9 homolog, mitochondrial;
DE   Flags: Precursor;
GN   Name=SHE9; ORFNames=LELG_01297;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Required for the maintenance of the structure of the
CC       mitochondrial inner membrane. Involved in mitochondrial morphology.
CC       Causes growth arrest when highly overexpressed (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SHE9 family. {ECO:0000305}.
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DR   EMBL; CH981524; EDK43119.1; -; Genomic_DNA.
DR   RefSeq; XP_001528777.1; XM_001528727.1.
DR   AlphaFoldDB; A5DVB1; -.
DR   SMR; A5DVB1; -.
DR   STRING; 379508.A5DVB1; -.
DR   EnsemblFungi; EDK43119; EDK43119; LELG_01297.
DR   GeneID; 5235702; -.
DR   KEGG; lel:LELG_01297; -.
DR   eggNOG; ENOG502QQ1E; Eukaryota.
DR   HOGENOM; CLU_025632_5_0_1; -.
DR   InParanoid; A5DVB1; -.
DR   OMA; YRNDHEN; -.
DR   OrthoDB; 719853at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008839; MDM33_fungi.
DR   PANTHER; PTHR31961; PTHR31961; 1.
DR   Pfam; PF05546; She9_MDM33; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..508
FT                   /note="Sensitive to high expression protein 9 homolog,
FT                   mitochondrial"
FT                   /id="PRO_0000351059"
FT   TOPO_DOM        ?..318
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        340..484
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        485..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        506..508
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   REGION          54..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          49..98
FT                   /evidence="ECO:0000255"
FT   COILED          196..228
FT                   /evidence="ECO:0000255"
FT   COILED          266..301
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        54..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  58174 MW;  6F9F588267C0F4FC CRC64;
     MLLPVLRASS RIVMRHSVVF NCIRLQSNKP ERSQQINELK LREIIEGTNF GTEATKKRKL
     EEERKKLEKE REAERQREEK KEREAKLEEA NKQNEADFSS TKTGKLKGED SEVDHKKDEG
     LRIENKIIAT TDSSVDATDI PNIAEEVNET IQKEIGGLPS EKQKKQSALT KKITQYLDSA
     HDTILTVTRA LNDVTGYSAI ERLKKSIEEQ EEDLKNAKKY VKECKLTYGD AIQKRSHSQR
     EVNELLTRKH NWSPEDLERF TELYRNDHEN DVWEKECEKK LEEAELKVDA VQLKLTQLIL
     TRYHEEQIWS DKIRRSSTWG TWVLMGLNVL LFVFATFLVE PWKRKKLVLG FEDKVKTVLV
     GIAQENDAVL NPIIEKLDQE QKDGSTGHNL EKSGYLTLED EGGQTTSLPA SLDSTSSQPP
     SAPVLSKEQQ GSRILRAKAS IKFFILQAQY AIVSSWHRVR VTCVKSYTAL TTPSIEFLKL
     DKVEFGLYTF IISILSCGLG SLATIYCR