SHE9_ASPTN
ID SHE9_ASPTN Reviewed; 466 AA.
AC Q0CFC0;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Sensitive to high expression protein 9 homolog, mitochondrial;
DE Flags: Precursor;
GN Name=she9; ORFNames=ATEG_07614;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476604; EAU31876.1; -; Genomic_DNA.
DR RefSeq; XP_001216235.1; XM_001216235.1.
DR AlphaFoldDB; Q0CFC0; -.
DR STRING; 341663.Q0CFC0; -.
DR EnsemblFungi; EAU31876; EAU31876; ATEG_07614.
DR GeneID; 4322576; -.
DR VEuPathDB; FungiDB:ATEG_07614; -.
DR eggNOG; ENOG502QQ1E; Eukaryota.
DR HOGENOM; CLU_025632_2_0_1; -.
DR OMA; TTQREVT; -.
DR OrthoDB; 719853at2759; -.
DR Proteomes; UP000007963; 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 ?..466
FT /note="Sensitive to high expression protein 9 homolog,
FT mitochondrial"
FT /id="PRO_0000351051"
FT TOPO_DOM ?..294
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..442
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..466
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT REGION 59..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 173..275
FT /evidence="ECO:0000255"
FT COMPBIAS 77..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 51684 MW; C338E03C161FF620 CRC64;
MHSLPLLLRQ SLRSTGALSR SAHRPIRAPP LPSHLLRLPT AHPRPFSVCL QCQFRTQSAS
YPPNKESDKP LDTETPSKHP DSTASFLEES LKTQAEAGTP ADSTTTTTTT TTSPPPQPTP
NEPKTADSSL RDTLPSYLDN RRSQFSKQFT TMMDNLQSNI FVAGQRLNDL TGYSEIEALK
KEIHTQEDRL RAARLHVRNA KEAYASAINR RSASQREVNE LLQRKHAWSP VDLERFTHLY
RNDHTNEVAE NEAQEALTAA EREAEEAAAQ LSKSILSRYH EEQVWSDKIR RMSTWGTWGL
MGVNVLLFLV FQIAVEPWRR KRLVKGFEEK VIEAIEKERE MNHVEILSPT AAAATAGAVA
PVEAAGEDAA PAPVEEETTS DGASVVEDTT GGVVEDRADL AHESYKAQLP SLPSTLSVDS
WRQYLHDLFS ERSMIITQRD LSSVALQSAA AGAAVMGLVI ALIRPR