ID TIM13_YEAST Reviewed; 105 AA. AC P53299; D6VUW5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 08-NOV-2023, entry version 182. DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM13; GN Name=TIM13; OrderedLocusNames=YGR181W; ORFNames=G7157; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9133739; RX DOI=10.1002/(sici)1097-0061(19970330)13:4<357::aid-yea77>3.0.co;2-j; RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M., RA Nombela C.; RT "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of RT Saccharomyces cerevisiae chromosome VII."; RL Yeast 13:357-363(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE TIM22 COMPLEX. RX PubMed=10469659; DOI=10.1093/emboj/18.17.4816; RA Leuenberger D., Bally N.A., Schatz G., Koehler C.M.; RT "Different import pathways through the mitochondrial intermembrane space RT for inner membrane proteins."; RL EMBO J. 18:4816-4822(1999). RN [6] RP FUNCTION. RX PubMed=11101512; DOI=10.1093/emboj/19.23.6392; RA Paschen S.A., Rothbauer U., Kaldi K., Bauer M.F., Neupert W., Brunner M.; RT "The role of the TIM8-13 complex in the import of Tim23 into RT mitochondria."; RL EMBO J. 19:6392-6400(2000). RN [7] RP FUNCTION. RX PubMed=10995434; DOI=10.1083/jcb.150.6.1271; RA Davis A.J., Sepuri N.B., Holder J., Johnson A.E., Jensen R.E.; RT "Two intermembrane space TIM complexes interact with different domains of RT Tim23p during its import into mitochondria."; RL J. Cell Biol. 150:1271-1282(2000). RN [8] RP FUNCTION. RX PubMed=11509656; DOI=10.1128/mcb.21.18.6132-6138.2001; RA Murphy M.P., Leuenberger D., Curran S.P., Oppliger W., Koehler C.M.; RT "The essential function of the small Tim proteins in the TIM22 import RT pathway does not depend on formation of the soluble 70-kilodalton RT complex."; RL Mol. Cell. Biol. 21:6132-6138(2001). RN [9] RP FUNCTION, SUBUNIT, PROBABLE DISULFIDE BONDS, AND LACK OF ZINC-BINDING WHEN RP PRESENT IN THE MITOCHONDRIAL INTERMEMBRANE SPACE. RX PubMed=12221072; DOI=10.1083/jcb.200205124; RA Curran S.P., Leuenberger D., Schmidt E., Koehler C.M.; RT "The role of the Tim8p-Tim13p complex in a conserved import pathway for RT mitochondrial polytopic inner membrane proteins."; RL J. Cell Biol. 158:1017-1027(2002). RN [10] RP ZINC-BINDING WHEN PRESENT IN THE CYTOSOL, DOMAIN, AND MUTAGENESIS OF RP CYS-57; CYS-61; CYS-73 AND CYS-77. RX PubMed=12941692; DOI=10.1093/emboj/cdg421; RA Lutz T., Neupert W., Herrmann J.M.; RT "Import of small Tim proteins into the mitochondrial intermembrane space."; RL EMBO J. 22:4400-4408(2003). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RX PubMed=22984289; DOI=10.1074/mcp.m112.021105; RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.; RT "Intermembrane space proteome of yeast mitochondria."; RL Mol. Cell. Proteomics 11:1840-1852(2012). 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 under precise conditions while the predominant TIM9-TIM10 70 CC kDa complex is crucial and mediates the import of much more proteins. CC Strictly required for import of TIM23 in some conditions, when a low CC membrane potential exists in the mitochondria. CC {ECO:0000269|PubMed:10469659, ECO:0000269|PubMed:10995434, CC ECO:0000269|PubMed:11101512, ECO:0000269|PubMed:11509656, CC ECO:0000269|PubMed:12221072}. 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 TIM18, TIM22 and TIM54. Interacts with the CC transmembrane regions of multi-pass transmembrane proteins in transit. CC {ECO:0000269|PubMed:10469659, ECO:0000269|PubMed:12221072}. CC -!- INTERACTION: CC P53299; P57744: TIM8; NbExp=4; IntAct=EBI-9121, EBI-9013892; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:10469659}; Peripheral membrane protein CC {ECO:0000269|PubMed:10469659}; Intermembrane side CC {ECO:0000269|PubMed:10469659}. Mitochondrion intermembrane space CC {ECO:0000269|PubMed:22984289}. 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. CC {ECO:0000269|PubMed:12941692}. CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X99074; CAA67526.1; -; Genomic_DNA. DR EMBL; Z72966; CAA97207.1; -; Genomic_DNA. DR EMBL; AY558508; AAS56834.1; -; Genomic_DNA. DR EMBL; BK006941; DAA08276.1; -; Genomic_DNA. DR PIR; S64495; S64495. DR RefSeq; NP_011697.3; NM_001181310.3. DR PDB; 3CJH; X-ray; 2.60 A; A/C/E/G/I/K=42-105. DR PDBsum; 3CJH; -. DR AlphaFoldDB; P53299; -. DR SASBDB; P53299; -. DR SMR; P53299; -. DR BioGRID; 33434; 176. DR ComplexPortal; CPX-2371; TIM8-TIM13 mitochondrial intermembrane space protein transporter complex. DR DIP; DIP-5547N; -. DR IntAct; P53299; 6. DR MINT; P53299; -. DR STRING; 4932.YGR181W; -. DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family. DR iPTMnet; P53299; -. DR MaxQB; P53299; -. DR PaxDb; 4932-YGR181W; -. DR PeptideAtlas; P53299; -. DR EnsemblFungi; YGR181W_mRNA; YGR181W; YGR181W. DR GeneID; 853093; -. DR KEGG; sce:YGR181W; -. DR AGR; SGD:S000003413; -. DR SGD; S000003413; TIM13. DR VEuPathDB; FungiDB:YGR181W; -. DR eggNOG; KOG1733; Eukaryota. DR GeneTree; ENSGT00390000014000; -. DR HOGENOM; CLU_141397_0_1_1; -. DR InParanoid; P53299; -. DR OMA; RCISQCM; -. DR OrthoDB; 226619at2759; -. DR BioCyc; YEAST:G3O-30873-MONOMER; -. DR BioGRID-ORCS; 853093; 4 hits in 10 CRISPR screens. DR EvolutionaryTrace; P53299; -. DR PRO; PR:P53299; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P53299; Protein. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD. DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0140318; F:protein transporter activity; IDA:SGD. DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:SGD. DR Gene3D; 1.10.287.810; Mitochondrial import inner membrane translocase subunit tim13 like domains; 1. DR InterPro; IPR004217; Tim10-like. DR InterPro; IPR035427; Tim10-like_dom_sf. DR Pfam; PF02953; zf-Tim10_DDP; 1. DR SUPFAM; SSF144122; Tim10-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Disulfide bond; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Protein transport; KW Reference proteome; Translocation; Transport; Zinc. FT CHAIN 1..105 FT /note="Mitochondrial import inner membrane translocase FT subunit TIM13" FT /id="PRO_0000193632" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 57..77 FT /note="Twin CX3C motif" FT COMPBIAS 8..27 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 57..77 FT /evidence="ECO:0000305" FT DISULFID 61..73 FT /evidence="ECO:0000305" FT MUTAGEN 57 FT /note="C->S: Abolishes import into mitochondrion; when FT associated with S-61." FT /evidence="ECO:0000269|PubMed:12941692" FT MUTAGEN 61 FT /note="C->S: Abolishes import into mitochondrion; when FT associated with S-57." FT /evidence="ECO:0000269|PubMed:12941692" FT MUTAGEN 73 FT /note="C->S: Abolishes import into mitochondrion; when FT associated with S-77." FT /evidence="ECO:0000269|PubMed:12941692" FT MUTAGEN 77 FT /note="C->S: Abolishes import into mitochondrion; when FT associated with S-73." FT /evidence="ECO:0000269|PubMed:12941692" FT HELIX 47..61 FT /evidence="ECO:0007829|PDB:3CJH" FT HELIX 71..93 FT /evidence="ECO:0007829|PDB:3CJH" SQ SEQUENCE 105 AA; 11286 MW; B1DDFE87AFDC52A3 CRC64; MGLSSIFGGG APSQQKEAAT TAKTTPNPIA KELKNQIAQE LAVANATELV NKISENCFEK CLTSPYATRN DACIDQCLAK YMRSWNVISK AYISRIQNAS ASGEI //