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SHE9_ASPNC
ID   SHE9_ASPNC              Reviewed;         499 AA.
AC   A2R3F3;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Sensitive to high expression protein 9 homolog, mitochondrial;
DE   Flags: Precursor;
GN   Name=she9; ORFNames=An14g04090;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM270320; CAK46645.1; -; Genomic_DNA.
DR   RefSeq; XP_001401033.1; XM_001400996.2.
DR   AlphaFoldDB; A2R3F3; -.
DR   SMR; A2R3F3; -.
DR   PaxDb; A2R3F3; -.
DR   EnsemblFungi; CAK46645; CAK46645; An14g04090.
DR   GeneID; 4987266; -.
DR   KEGG; ang:ANI_1_1402124; -.
DR   VEuPathDB; FungiDB:An14g04090; -.
DR   HOGENOM; CLU_025632_2_0_1; -.
DR   Proteomes; UP000006706; Chromosome 1R.
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           ?..499
FT                   /note="Sensitive to high expression protein 9 homolog,
FT                   mitochondrial"
FT                   /id="PRO_0000351049"
FT   TOPO_DOM        ?..302
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..475
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        476..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        497..499
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   REGION          94..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          181..283
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        105..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  55681 MW;  23B011A594B93064 CRC64;
     MQSMPLLLRQ SFKSTLNLTR TTRPVQRRPL LPAVGPNSLY PAPRNFSICL QCQFRTQSSL
     YSSDSLKDGK PAEQPKEDAS PVIALPAGNA NLEADAGSQQ QAPPAAAEAG ESTQSQQQQQ
     QQQQQQEEKS EANGKGWGDG GLPSYIEQRR SQFTKRFSDV MDNLQSNIFV AGQRLNDLTG
     YSAIEMLKKE IHRQEERLRT ARLQVRTAKD AYAAAINNRS TSQREVNELL QRKHAWSPTD
     LERFTHLYRN DHTNEVAEHE AQEALSQAEH EAEEAAAQLS KSILSRYHEE QVWSDKIRQM
     STWGTWGLMG VNVLLFLIFQ IAVEPWRRKR LVKGFEEKVI EAIEKEKALD RIQIVTAQNQ
     MAQESSTTST ASTATPETAE TAETAEPSAS PADEPIADTD AIVTIESTEP EVFSSDPADA
     EPPANTIVSK PTPDNIREYI KFQLARVSPL LESLRQYLHD LFSDRQVVLT QRDLSTVALQ
     SAAAGAAVIG MLSMIIRQR
 
 
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