SHE9_EMENI
ID SHE9_EMENI Reviewed; 471 AA.
AC Q5BAW7; C8VN62;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Sensitive to high expression protein 9 homolog, mitochondrial;
DE Flags: Precursor;
GN Name=she9; ORFNames=AN2313;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(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; AACD01000038; EAA64424.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF86588.1; -; Genomic_DNA.
DR RefSeq; XP_659917.1; XM_654825.1.
DR AlphaFoldDB; Q5BAW7; -.
DR SMR; Q5BAW7; -.
DR STRING; 162425.CADANIAP00009007; -.
DR EnsemblFungi; CBF86588; CBF86588; ANIA_02313.
DR EnsemblFungi; EAA64424; EAA64424; AN2313.2.
DR GeneID; 2875516; -.
DR KEGG; ani:AN2313.2; -.
DR VEuPathDB; FungiDB:AN2313; -.
DR eggNOG; ENOG502QQ1E; Eukaryota.
DR HOGENOM; CLU_025632_2_0_1; -.
DR InParanoid; Q5BAW7; -.
DR OMA; TTQREVT; -.
DR OrthoDB; 719853at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; 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 ?..471
FT /note="Sensitive to high expression protein 9 homolog,
FT mitochondrial"
FT /id="PRO_0000351057"
FT TOPO_DOM ?..289
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..447
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..471
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT REGION 84..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..269
FT /evidence="ECO:0000255"
FT COMPBIAS 92..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 52425 MW; 7EDE9F6D6C9C7C22 CRC64;
MQSMPWLFRQ SLRTGLNLSR TSLPGRSPIS PAPISKVHSK TARRNFSVCL RCHFRYQPSL
RSDEIKRSTD EKQDKKIEEP VIALGAPEST QAEPNAGAQD TSQTADTVHT QGQEGKKEDE
PGSTQNGGLP SYIEDRRSQF SKQFTTWMDN LQSNVFVAGQ RLNDLTGYSS IEALKRNIQE
QEKRLRAARH RVRTAKEAYA AAINRRSTSQ REVNELLQRK HAWSPADLER FTHLYRNDHT
NEVAENETQE ALSAAERESE EAAASLTKSI LSRYHEEQVW SDKIRRMSTW GTWGLMGVNV
LLFLIFQIAV EPWRRKRLVK GFEEKVLEAI EKEKILVHSQ PVPPVEFTAT QDAHSPTSGL
VTPSPGDNIA SEESSEATVA ANTPTTTAED EASGSMAPEN ITSSSLESYK PPSLQSLLSS
MSIECCRQYI HYLLSESPVT VTQRDISVVA ATSAAAGATL MGLVVALIRS Q
