TIM13_YEAST
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 03-AUG-2022, entry version 177.
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}.
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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; 174.
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; P53299; -.
DR PRIDE; P53299; -.
DR EnsemblFungi; YGR181W_mRNA; YGR181W; YGR181W.
DR GeneID; 853093; -.
DR KEGG; sce:YGR181W; -.
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 BioCyc; YEAST:G3O-30873-MON; -.
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; -; 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 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
