ID   SHE9_DEBHA              Reviewed;         462 AA.
AC   Q6BJ94;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Sensitive to high expression protein 9 homolog, mitochondrial;
DE   Flags: Precursor;
GN   Name=SHE9; OrderedLocusNames=DEHA2G04158g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}.
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; CR382139; CAG90180.2; -; Genomic_DNA.
DR   RefSeq; XP_461727.2; XM_461727.1.
DR   AlphaFoldDB; Q6BJ94; -.
DR   SMR; Q6BJ94; -.
DR   STRING; 4959.XP_461727.2; -.
DR   EnsemblFungi; CAG90180; CAG90180; DEHA2G04158g.
DR   GeneID; 2904600; -.
DR   KEGG; dha:DEHA2G04158g; -.
DR   VEuPathDB; FungiDB:DEHA2G04158g; -.
DR   eggNOG; ENOG502QQ1E; Eukaryota.
DR   HOGENOM; CLU_025632_5_0_1; -.
DR   InParanoid; Q6BJ94; -.
DR   OMA; YRNDHEN; -.
DR   OrthoDB; 719853at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
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           ?..462
FT                   /note="Sensitive to high expression protein 9 homolog,
FT                   mitochondrial"
FT                   /id="PRO_0000351056"
FT   TOPO_DOM        ?..309
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        331..438
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        460..462
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   REGION          93..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          188..222
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        93..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   462 AA;  53749 MW;  E16729E583AE2924 CRC64;
     MNVSTYNIRP IYRSHRLIRS RSCFCILNPL AVRFYSSKNF SSSNNPIANS NEKSSHHDEK
     LREIIETTNF GSELRKKKEM HDKKLHEQKA YEKYEKEAEG KETPQEKGQE EDSVSNSDKS
     TPEEEVKAND GSIIASEISE DIQREIGNLP SQKETRRYQL SKKLEEYLDS LQDTIFTATR
     ALNDVTGYSS IEQLKKSIND LEVQLKNEKD NVKKCKDLYS QAILRRSLSQ REINELLTRK
     HNWSPDDLER FTTLYRNDHV NEQEESNTHN ALNDAESKVD AIQLKLTQSI LTRYHEEQIW
     SDKIRRASTW GTWILMGINL FLFILATFLV EPWKRKRLVG SFEDKVKQAI FEMSEVQEGK
     WDQMILQQKE SAAQQSVSTL KSWWFNSDDD SEPNKSSVYP MILTPVDNSW QGLKTTIRSH
     YNALRSSTIS TLQFEKYEFA WFATTITILG CALGSILTVY FK