MIA40_CANAL
ID MIA40_CANAL Reviewed; 252 AA.
AC O94030; A0A1D8PCV5; Q5AI77;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 97.
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=CAALFM_C102880CA;
GN ORFNames=Ca49C10.16, CaO19.10494, CaO19.2977;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1161;
RA Oliver K., Harris D., Barrell B.G., Rajandream M.A.;
RT "Candida albicans strain 1161 genome pilot sequencing project.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; AL033497; CAA21980.1; -; Genomic_DNA.
DR EMBL; CP017623; AOW25969.1; -; Genomic_DNA.
DR PIR; T52160; T52160.
DR RefSeq; XP_721476.1; XM_716383.2.
DR AlphaFoldDB; O94030; -.
DR SMR; O94030; -.
DR STRING; 237561.O94030; -.
DR PRIDE; O94030; -.
DR GeneID; 3636866; -.
DR KEGG; cal:CAALFM_C102880CA; -.
DR CGD; CAL0000191454; MIA40.
DR VEuPathDB; FungiDB:C1_02880C_A; -.
DR eggNOG; KOG4149; Eukaryota.
DR HOGENOM; CLU_054990_1_0_1; -.
DR InParanoid; O94030; -.
DR OMA; FENMRSC; -.
DR OrthoDB; 1491842at2759; -.
DR PRO; PR:O94030; -.
DR Proteomes; UP000000559; Chromosome 1.
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 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; Reference proteome;
KW Signal-anchor; Transit peptide; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..252
FT /note="Mitochondrial intermembrane space import and
FT assembly protein 40"
FT /id="PRO_0000235285"
FT TOPO_DOM 32..37
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..252
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 160..204
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 90..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 163..173
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 186..196
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 90..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 152..154
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 163..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 173..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT CONFLICT 24..25
FT /note="LS -> FF (in Ref. 1; CAA21980)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="V -> I (in Ref. 1; CAA21980)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="N -> D (in Ref. 1; CAA21980)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="P -> T (in Ref. 1; CAA21980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 27930 MW; 8036370CBEB316A8 CRC64;
MYRTISRSSS GLIRQSTARL TRQLSTTRTT PSQYNSKLLL GVLGTGALAF GYFSQQSSLI
QNASTAENIE KVFEEGNAVA KDAQESLDAR QEKVIKENEQ KTKKAEDAKT SSESKANVAD
KKSNSQPEGE PEGEGKQEAA FNPDTGEINW DCPCLGGMAH GPCGEEFKEA FSCFVFSETE
PKGIDCIKKF ENMRSCFKRY PEHYKDELYD DGEEEASTEV VEHVVLETSE PAIEQIEQGI
KEDKVKPNTK SD
