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MIA40_ASHGO
ID   MIA40_ASHGO             Reviewed;         266 AA.
AC   Q757A5;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Mitochondrial intermembrane space import and assembly protein 40;
DE   AltName: Full=Mitochondrial import inner membrane translocase TIM40;
DE   Flags: Precursor;
GN   Name=MIA40; Synonyms=TIM40; OrderedLocusNames=AER108C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Required for the import and folding of small cysteine-
CC       containing proteins (small Tim) in the mitochondrial intermembrane
CC       space (IMS). Forms a redox cycle with ERV1 that involves a disulfide
CC       relay system. Precursor proteins to be imported into the IMS are
CC       translocated in their reduced form into the mitochondria. The oxidized
CC       form of MIA40 forms a transient intermolecular disulfide bridge with
CC       the reduced precursor protein, resulting in oxidation of the precursor
CC       protein that now contains an intramolecular disulfide bond and is able
CC       to undergo folding in the IMS (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Cu(2+) or Zn(2+). {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}; Intermembrane side
CC       {ECO:0000250}.
CC   -!- DOMAIN: The CHCH domain contains a conserved twin Cys-X(9)-Cys motif
CC       which is required for import and stability of MIA40 in mitochondria.
CC       {ECO:0000250}.
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DR   EMBL; AE016818; AAS52792.1; -; Genomic_DNA.
DR   RefSeq; NP_984968.1; NM_210322.1.
DR   AlphaFoldDB; Q757A5; -.
DR   SMR; Q757A5; -.
DR   STRING; 33169.AAS52792; -.
DR   EnsemblFungi; AAS52792; AAS52792; AGOS_AER108C.
DR   GeneID; 4621173; -.
DR   KEGG; ago:AGOS_AER108C; -.
DR   eggNOG; KOG4149; Eukaryota.
DR   HOGENOM; CLU_054990_1_3_1; -.
DR   InParanoid; Q757A5; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0022417; P:protein maturation by protein folding; IBA:GO_Central.
DR   InterPro; IPR010625; CHCH.
DR   InterPro; IPR039289; CHCHD4.
DR   InterPro; IPR012891; GCK_dom.
DR   PANTHER; PTHR21622; PTHR21622; 1.
DR   Pfam; PF06747; CHCH; 1.
DR   SMART; SM01227; GCK; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Protein transport; Redox-active center; Reference proteome;
KW   Signal-anchor; Transit peptide; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..266
FT                   /note="Mitochondrial intermembrane space import and
FT                   assembly protein 40"
FT                   /id="PRO_0000235282"
FT   TOPO_DOM        29..44
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..61
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..266
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          195..239
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          87..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           198..208
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           221..231
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        187..189
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        198..231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        208..221
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   266 AA;  27790 MW;  027DF66E3A778EA6 CRC64;
     MFRQVSVRAL RRAAGRSVCA SRAQMVRHSS TLGGGKGSYN LDMPALALAA GVTLLAGYMV
     YPRAPKAKQA AVQSVAPVNE NVEQASASLQ ASAPVQATSE SAEAGEEEAY GEESGAVNEE
     AAGEPEEAAA EVGETQAEQA PAVETEQAAE AEQAAEAAAE DKASAGEAAQ GQQGAYNPDT
     GEINWDCPCL GGMAHGPCGE EFKAAFACFV YSEAEPKGID CVEKFQVMQD CFRQHPEHYA
     EQLESEEQAV RETEAAAESA KSDEGH
 
 
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