MIA40_CRYNB
ID MIA40_CRYNB Reviewed; 242 AA.
AC P0CM69; Q55RV1; Q5KGA4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 37.
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=CNBE4300;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL20510.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAEY01000028; EAL20510.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_775157.1; XM_770064.1.
DR AlphaFoldDB; P0CM69; -.
DR SMR; P0CM69; -.
DR EnsemblFungi; EAL20510; EAL20510; CNBE4300.
DR GeneID; 4936441; -.
DR KEGG; cnb:CNBE4300; -.
DR HOGENOM; CLU_054990_1_3_1; -.
DR Proteomes; UP000001435; Chromosome 5.
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:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IEA:InterPro.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR039289; CHCHD4.
DR PANTHER; PTHR21622; PTHR21622; 1.
DR Pfam; PF06747; CHCH; 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; Signal-anchor;
KW Transit peptide; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..242
FT /note="Mitochondrial intermembrane space import and
FT assembly protein 40"
FT /id="PRO_0000410037"
FT TOPO_DOM 19..34
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..242
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 152..196
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..165
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 178..188
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 75..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 144..146
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 155..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 165..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 242 AA; 26077 MW; F889325A3BF9A72E CRC64;
MFARSFSNAS RTIARRSLST RSGPAPSSLW SSRNAVIAGT TLAITALAVT SERRKVFNES
AQKATSPRDS IIAQDSLKEN VHKKSVRQDE FSGESTKPEA STSSDSVEKA ADDAAQILEE
KEAEASEPSQ GAYNPETGEI NWDCPCLGGM ATGPCGEQFK AAFSCFVYSE AEPKGVDCVE
LFKVMQDCFR EHPEIYGEVD TLGLVLMFYA EIDDDEAPPQ EGTMEEKVEA AKEETAAPAA
AP
