MIA40_SCHPO
ID MIA40_SCHPO Reviewed; 313 AA.
AC P87059;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
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; ORFNames=SPAC57A10.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAB08174.1; -; Genomic_DNA.
DR PIR; T38938; T38938.
DR RefSeq; NP_593316.1; NM_001018747.2.
DR AlphaFoldDB; P87059; -.
DR SMR; P87059; -.
DR STRING; 4896.SPAC57A10.11c.1; -.
DR iPTMnet; P87059; -.
DR MaxQB; P87059; -.
DR PaxDb; P87059; -.
DR PRIDE; P87059; -.
DR EnsemblFungi; SPAC57A10.11c.1; SPAC57A10.11c.1:pep; SPAC57A10.11c.
DR GeneID; 2542760; -.
DR KEGG; spo:SPAC57A10.11c; -.
DR PomBase; SPAC57A10.11c; mia40.
DR VEuPathDB; FungiDB:SPAC57A10.11c; -.
DR eggNOG; KOG4149; Eukaryota.
DR HOGENOM; CLU_054990_0_1_1; -.
DR InParanoid; P87059; -.
DR OMA; FQAMQAC; -.
DR PhylomeDB; P87059; -.
DR PRO; PR:P87059; -.
DR Proteomes; UP000002485; Chromosome I.
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:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0016972; F:thiol oxidase activity; ISO:PomBase.
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..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 62..313
FT /note="Mitochondrial intermembrane space import and
FT assembly protein 40"
FT /id="PRO_0000116636"
FT TOPO_DOM 62
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..73
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..313
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 207..251
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 116..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 210..220
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 233..243
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 116..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 199..201
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 210..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 220..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 313 AA; 34915 MW; 76D28DAA2C11C0D0 CRC64;
MFAKNLLFRF PKCIRINGYN NMRRSLLQRN GFQAGICRKF GTATKTDVWK GRFLPIVSGV
AAASLTAGYL LGKNTSNASS SQDNDHPVVG EHVHTETQSY NEPYMQRHRI EDAIEKKMTS
ETQPSTDEKG RKVSATENSA PKKTDKEKSS GETAGNILRE QIATGKDDDE YARKFEEVEE
ESSEESAFNP DTGEINWDCP CLGGMAHGPC GEEFKAAFSC FVYSKSEPKG MECLDKFQAM
QACFQKHPEI YQDMVGESEE EDAETNEKPS TTSDENNQPQ SPPSDNASNP EEDVMNMEKE
IVNLTPMSVI KEI
