ID   SHE9_SCLS1              Reviewed;         527 AA.
AC   A7EEA6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Sensitive to high expression protein 9 homolog, mitochondrial;
DE   Flags: Precursor;
GN   Name=she9; ORFNames=SS1G_03646;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476624; EDO01172.1; -; Genomic_DNA.
DR   RefSeq; XP_001595557.1; XM_001595507.1.
DR   AlphaFoldDB; A7EEA6; -.
DR   SMR; A7EEA6; -.
DR   STRING; 665079.A7EEA6; -.
DR   EnsemblFungi; EDO01172; EDO01172; SS1G_03646.
DR   GeneID; 5491963; -.
DR   KEGG; ssl:SS1G_03646; -.
DR   VEuPathDB; FungiDB:sscle_09g074580; -.
DR   eggNOG; ENOG502QQ1E; Eukaryota.
DR   HOGENOM; CLU_025632_2_1_1; -.
DR   InParanoid; A7EEA6; -.
DR   OMA; QTHIFTA; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central.
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           ?..527
FT                   /note="Sensitive to high expression protein 9 homolog,
FT                   mitochondrial"
FT                   /id="PRO_0000351064"
FT   TOPO_DOM        ?..327
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        349..502
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        503..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        524..527
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   REGION          109..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          277..308
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        109..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  59050 MW;  F86A8BD593EF9B72 CRC64;
     MVSVIEAHNT QWSELHRAQH PNILSLSQYL ILPIDVRKRE KSSARHNSSE RGRQLSIAMQ
     PLTRLIPRFA IDSGSASISR SLRISPRPSL KSSICLQCRI YSPSLRRHFA DDQRPIIEPP
     PHLRPKVTPP EDPKPQPQPE EEKPASIPEY SKQDDSPSPQ LERDRELPST LESRRLAMTK
     KLSHLMDHMQ GNIFIASQRI NDLTGYSGIE ALKNKITNLE AQVASSKELV RSTRLHYKTT
     VADRASSQRE VTTLLARKDT WTPADLERFT HLYRMDHTNE QAVQEAATRL ADAEREAEKA
     AGELSSSILS RYHEEQIWSD KIRRMSTWGT WGLMGVNVLL FLVFQFGFEP WRRRRLVAGF
     EEKVREALEQ EKTLAMSTAI RGAEIGGGEG SEVSLDEIVA AEVQELKEEA LVEGLGEPAV
     EAVAATIEGE VPHHESNNEP AQEIGEAAAA MDTAELNIPY SRPPPFDYRN IESWKEKMEA
     GKAAAIDLWS TRQVSITKKD ITIIALEGAA GGAVLAGAIF TFIIRRS