TIM10_SCHPO
ID TIM10_SCHPO Reviewed; 89 AA.
AC Q9UTE9;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit tim10;
GN Name=tim10; ORFNames=SPAC222.03c;
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: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. Also required for the transfer of beta-
CC barrel precursors from the TOM complex to the sorting and assembly
CC machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC protein that protects the hydrophobic precursors from aggregation and
CC guide them through the mitochondrial intermembrane space (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIM9 and 3 copies of
CC TIM10, named soluble 70 kDa complex. Associates directly with the TIM22
CC complex, whose core is composed of TIM22 and TIM54. Interacts with the
CC transmembrane regions of multi-pass transmembrane proteins in transit
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC {ECO:0000250}.
CC -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC 2 disulfide bonds in the mitochondrial intermembrane space. However,
CC during the transit of TIM10 from cytoplasm into mitochondrion, the Cys
CC residues probably coordinate zinc, thereby preventing folding and
CC allowing its transfer across mitochondrial outer membrane (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; CU329670; CAB60695.1; -; Genomic_DNA.
DR PIR; T50144; T50144.
DR RefSeq; NP_593142.1; NM_001018539.2.
DR AlphaFoldDB; Q9UTE9; -.
DR SMR; Q9UTE9; -.
DR BioGRID; 278437; 2.
DR STRING; 4896.SPAC222.03c.1; -.
DR MaxQB; Q9UTE9; -.
DR PaxDb; Q9UTE9; -.
DR EnsemblFungi; SPAC222.03c.1; SPAC222.03c.1:pep; SPAC222.03c.
DR GeneID; 2541950; -.
DR KEGG; spo:SPAC222.03c; -.
DR PomBase; SPAC222.03c; tim10.
DR VEuPathDB; FungiDB:SPAC222.03c; -.
DR eggNOG; KOG3480; Eukaryota.
DR HOGENOM; CLU_162151_1_0_1; -.
DR InParanoid; Q9UTE9; -.
DR OMA; ELEIEMM; -.
DR PhylomeDB; Q9UTE9; -.
DR Reactome; R-SPO-1268020; Mitochondrial protein import.
DR PRO; PR:Q9UTE9; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISO:PomBase.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR027100; Tim10.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR PANTHER; PTHR11038:SF16; PTHR11038:SF16; 1.
DR Pfam; PF02953; zf-Tim10_DDP; 1.
DR SUPFAM; SSF144122; SSF144122; 1.
PE 3: Inferred from homology;
KW Chaperone; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transport; Zinc.
FT CHAIN 1..89
FT /note="Mitochondrial import inner membrane translocase
FT subunit tim10"
FT /id="PRO_0000193621"
FT MOTIF 39..64
FT /note="Twin CX3C motif"
FT DISULFID 39..64
FT /evidence="ECO:0000250"
FT DISULFID 43..60
FT /evidence="ECO:0000250"
SQ SEQUENCE 89 AA; 10195 MW; B84E4D9519046714 CRC64;
MSMFGIGKNN QTINPQNIAM AEQEVEMMSD IFNRLVMTCH KKCISPKYYE ADLTKGESVC
IDRCVSKYFE ANQSLSQHMQ KRGQENPTP
