TIM10_NEUCR
ID TIM10_NEUCR Reviewed; 90 AA.
AC Q9C0N3; Q7SFB7; V5IRP3;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit tim10;
GN Name=tim10; ORFNames=G17B7.020, NCU00930;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=14668492; DOI=10.1091/mbc.e03-05-0272;
RA Vasiljev A., Ahting U., Nargang F.E., Go N.E., Habib S.J., Kozany C.,
RA Panneels V., Sinning I., Prokisch H., Neupert W., Nussberger S.,
RA Rapaport D.;
RT "Reconstituted TOM core complex and Tim9/Tim10 complex of mitochondria are
RT sufficient for translocation of the ADP/ATP carrier across membranes.";
RL Mol. Biol. Cell 15:1445-1458(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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.
CC {ECO:0000269|PubMed:14668492}.
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 {ECO:0000269|PubMed:14668492}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14668492}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14668492}; Intermembrane side
CC {ECO:0000269|PubMed:14668492}.
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; AF343076; AAK26645.1; -; Genomic_DNA.
DR EMBL; AF343077; AAK26646.1; -; mRNA.
DR EMBL; BX842638; CAE76573.1; -; Genomic_DNA.
DR EMBL; CM002236; ESA44226.1; -; Genomic_DNA.
DR EMBL; CM002236; ESA44227.1; -; Genomic_DNA.
DR RefSeq; XP_011392857.1; XM_011394555.1.
DR RefSeq; XP_011392858.1; XM_011394556.1.
DR AlphaFoldDB; Q9C0N3; -.
DR SMR; Q9C0N3; -.
DR STRING; 5141.EFNCRP00000000515; -.
DR EnsemblFungi; ESA44226; ESA44226; NCU00930.
DR EnsemblFungi; ESA44227; ESA44227; NCU00930.
DR GeneID; 3880909; -.
DR KEGG; ncr:NCU00930; -.
DR VEuPathDB; FungiDB:NCU00930; -.
DR HOGENOM; CLU_162151_1_0_1; -.
DR InParanoid; Q9C0N3; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IEA:EnsemblFungi.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140318; F:protein transporter activity; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
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 1: Evidence at protein level;
KW Chaperone; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transport; Zinc.
FT CHAIN 1..90
FT /note="Mitochondrial import inner membrane translocase
FT subunit tim10"
FT /id="PRO_0000193620"
FT MOTIF 36..61
FT /note="Twin CX3C motif"
FT DISULFID 36..61
FT /evidence="ECO:0000250"
FT DISULFID 40..57
FT /evidence="ECO:0000250"
SQ SEQUENCE 90 AA; 9923 MW; D4EF6B33BC397774 CRC64;
MFGLGRPQPT SAEKIAAVEN ELKVVAEMHS RMVKICTLKC IDKSYREGDL SKGESVCLDR
CAAKFFETHQ KISDQLQKET QARGGGGFGM