TIM13_NEUCR
ID TIM13_NEUCR Reviewed; 86 AA.
AC Q7SBR3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit tim13;
GN Name=tim13; ORFNames=NCU06244;
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 [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).
RN [2]
RP FUNCTION IN TRANSFER OF BETA-BARREL PROTEINS, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=14722057; DOI=10.1074/jbc.m313037200;
RA Hoppins S.C., Nargang F.E.;
RT "The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of
RT proteins into both mitochondrial membranes.";
RL J. Biol. Chem. 279:12396-12405(2004).
CC -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of some multi-pass transmembrane proteins into
CC the mitochondrial inner membrane. Also required for the transfer of
CC beta-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. The tim8-
CC tim13 complex is non essential and only mediates the import of few
CC proteins, while the predominant tim9-tim10 70 kDa complex is crucial
CC and mediates the import of much more proteins.
CC {ECO:0000269|PubMed:14722057}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of tim8 and 3 copies of
CC tim13, named soluble 70 kDa complex. Associates with the TIM22 complex,
CC 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:14722057}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14722057}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14722057}; Intermembrane side
CC {ECO:0000269|PubMed:14722057}.
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 tim13 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; CM002238; EAA33859.1; -; Genomic_DNA.
DR RefSeq; XP_963095.1; XM_958002.2.
DR AlphaFoldDB; Q7SBR3; -.
DR SMR; Q7SBR3; -.
DR STRING; 5141.EFNCRP00000005940; -.
DR EnsemblFungi; EAA33859; EAA33859; NCU06244.
DR GeneID; 3879250; -.
DR KEGG; ncr:NCU06244; -.
DR VEuPathDB; FungiDB:NCU06244; -.
DR HOGENOM; CLU_141397_0_2_1; -.
DR InParanoid; Q7SBR3; -.
DR OMA; MAAWNQV; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140318; F:protein transporter activity; 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; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR InterPro; IPR039238; Tim8/13.
DR PANTHER; PTHR19338; PTHR19338; 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..86
FT /note="Mitochondrial import inner membrane translocase
FT subunit tim13"
FT /id="PRO_0000228078"
FT MOTIF 37..60
FT /note="Twin CX3C motif"
FT DISULFID 37..60
FT /evidence="ECO:0000250"
FT DISULFID 41..56
FT /evidence="ECO:0000250"
SQ SEQUENCE 86 AA; 9568 MW; 79DE418AFA8D2265 CRC64;
MSDSTSETVK KAIIKQVLIE SQSANARTLM EKIGENCFTS CVPKPGSSLS NSEKTCVTQC
TEKYMAAWNV VNTTYLRRIQ QEMGNQ
