TCM62_YEAST
ID TCM62_YEAST Reviewed; 572 AA.
AC P38228; D6VQ44; Q9Y793;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Mitochondrial chaperone TCM62;
DE Flags: Precursor;
GN Name=TCM62; OrderedLocusNames=YBR044C; ORFNames=YBR0414;
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], CHARACTERIZATION, SUBCELLULAR LOCATION,
RP AND TOPOLOGY.
RC STRAIN=S288c / GRF88;
RX PubMed=9822678; DOI=10.1074/jbc.273.48.32042;
RA Dibrov E., Fu S., Lemire B.D.;
RT "The Saccharomyces cerevisiae TCM62 gene encodes a chaperone necessary for
RT the assembly of the mitochondrial succinate dehydrogenase (complex II).";
RL J. Biol. Chem. 273:32042-32048(1998).
RN [2]
RP SEQUENCE REVISION TO 566.
RA Lemire B.D.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 566.
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 [5]
RP CHARACTERIZATION.
RX PubMed=10745098; DOI=10.1016/s0014-5793(00)01322-3;
RA Klanner C., Neupert W., Langer T.;
RT "The chaperonin-related protein Tcm62p ensures mitochondrial gene
RT expression under heat stress.";
RL FEBS Lett. 470:365-369(2000).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: Chaperone. Required for the assembly of succinate
CC dehydrogenase subunits. Ensures mitochondrial gene expression at
CC elevated temperatures and prevents heat-aggregation of the ribosomal
CC subunit VAR1.
CC -!- SUBUNIT: Forms a high molecular mass protein complex of approximately
CC 850 kDa.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:9822678}; Single-pass
CC membrane protein {ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:9822678}; Matrix side {ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:9822678}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA84986.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF125155; AAD24466.1; -; Genomic_DNA.
DR EMBL; Z35913; CAA84986.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006936; DAA07164.2; -; Genomic_DNA.
DR PIR; S45902; S45902.
DR RefSeq; NP_009600.2; NM_001178392.2.
DR AlphaFoldDB; P38228; -.
DR SMR; P38228; -.
DR BioGRID; 32745; 106.
DR DIP; DIP-2609N; -.
DR IntAct; P38228; 4.
DR MINT; P38228; -.
DR STRING; 4932.YBR044C; -.
DR MaxQB; P38228; -.
DR PaxDb; P38228; -.
DR PRIDE; P38228; -.
DR EnsemblFungi; YBR044C_mRNA; YBR044C; YBR044C.
DR GeneID; 852332; -.
DR KEGG; sce:YBR044C; -.
DR SGD; S000000248; TCM62.
DR VEuPathDB; FungiDB:YBR044C; -.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_485763_0_0_1; -.
DR InParanoid; P38228; -.
DR OMA; YYGSIES; -.
DR BioCyc; YEAST:G3O-29017-MON; -.
DR PRO; PR:P38228; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38228; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; ISS:SGD.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:SGD.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IMP:SGD.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR SUPFAM; SSF52029; SSF52029; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Stress response; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..572
FT /note="Mitochondrial chaperone TCM62"
FT /id="PRO_0000063639"
FT TOPO_DOM 17..471
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..572
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
SQ SEQUENCE 572 AA; 64252 MW; 1AAE3CD22AD8D5BD CRC64;
MLRNCLRKLG NHQTKCSVKT LHTPIYRTKN LQVLRDTLSG IKLLEKIITS SSYNKTLIYE
PKYKSKPQVV SSHDTMRLHN VMRELLDSLQ VDEATNTRLQ SNRPRKLGRV GLQLFMDCIQ
DNLTATSTSL TCSLLEHYFK YPEKEVTNGI KAGLRYIRDF LAKNKIIVKS QNDVDALVEQ
LTMSSSDSQS IKRVLKAINY ELFSDDIVRV INGNKTYDEV DVSKGWKYPA GILDSNEAYL
RSLELPTKKL VSIDKDMLVL MYDGTLRDAN KILPTITYAR KLRKSVLLIV NGDCTGDALT
SVTINNNRNK RENNESRIVV LKYSKKANND LAPQENLDFI KFLRLPCGYD SIYSPEYSPL
VPSKMCADKY YGSIESIKAT TGEAFLYNSI DAEAIPNKVP KSFLQNTVTL SIGGHNEIEI
DRRRNAIDNC LNNVLCHGLA KGFIPGYGIS LLKAIPGLNE LKANEPNFMT KVGINAVLSA
VILPSEVAFK NAYGYNYYEI NSLIAGAINE KSFPMAKFSP NSEPVNTVKD GNLEPWSKMD
SCLAGVETFI ELLTSCNTII TCVYKKPERH KA
