ID C5FPA7_ARTOC Unreviewed; 288 AA.
AC C5FPA7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Mitochondrial intermembrane space import and assembly protein 40 {ECO:0000256|ARBA:ARBA00013714};
DE AltName: Full=Mitochondrial import inner membrane translocase TIM40 {ECO:0000256|ARBA:ARBA00033150};
GN ORFNames=MCYG_04242 {ECO:0000313|EMBL:EEQ31423.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ31423.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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. {ECO:0000256|ARBA:ARBA00024980}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004164}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004164}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00004164}.
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DR EMBL; DS995704; EEQ31423.1; -; Genomic_DNA.
DR RefSeq; XP_002846505.1; XM_002846459.1.
DR AlphaFoldDB; C5FPA7; -.
DR STRING; 554155.C5FPA7; -.
DR GeneID; 9224575; -.
DR VEuPathDB; FungiDB:MCYG_04242; -.
DR eggNOG; KOG4149; Eukaryota.
DR HOGENOM; CLU_054990_2_0_1; -.
DR OMA; PRSWKNT; -.
DR OrthoDB; 1278at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
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 Gene3D; 1.10.287.2900; -; 1.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR039289; CHCHD4.
DR PANTHER; PTHR21622:SF0; CHCH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR21622; COILED-COIL-HELIX-COILED-COIL-HELIX DOMAIN CONTAINING 4; 1.
DR Pfam; PF06747; CHCH; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW Translocation {ECO:0000256|ARBA:ARBA00023010};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 177..213
FT /note="CHCH"
FT /evidence="ECO:0000259|Pfam:PF06747"
FT REGION 90..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 31270 MW; CFD17301D2269038 CRC64;
MFRSASRTLL RGTPATQQLR FAQSRRWISD ASSPVQKKQG WRSTVVRWGL AVGAVYYYNT
SPIFAEEPPL VNKTVSPSNL QDTVVSPTIE SLEAARKPKA RPTPPLSEPK KTPSDETSIA
ASAETGASPT GGEQSPVATG DSEQGEGHEG QEAAFNPETG EINWDCPCLG GMAHGPCGED
FRAAFSCFVY SQEEPKGMDC IDKFKAMQDC FRQHPDIYGN ELDDEEVDAQ LDEHIASEKE
AEQKPSTEGS DSAPATTNEQ LQPESGKDKL QEAITKELDA IQSNASKE
//
