TIM21_YEAST
ID TIM21_YEAST Reviewed; 239 AA.
AC P53220; D6VUG9; Q45U51;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM21;
DE Flags: Precursor;
GN Name=TIM21; OrderedLocusNames=YGR033C;
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=SK1;
RA Deutschbauer A.M., Davis R.W.;
RT "Molecular genetic dissection of a quantitative trait in yeast.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE TIM23 COMPLEX,
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH TIM23 AND
RP TOM22.
RX PubMed=15797382; DOI=10.1016/j.cell.2005.01.011;
RA Chacinska A., Lind M., Frazier A.E., Dudek J., Meisinger C., Geissler A.,
RA Sickmann A., Meyer H.E., Truscott K.N., Guiard B., Pfanner N., Rehling P.;
RT "Mitochondrial presequence translocase: switching between TOM tethering and
RT motor recruitment involves Tim21 and Tim17.";
RL Cell 120:817-829(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE TIM23 COMPLEX,
RP AND FUNCTION.
RX PubMed=15878866; DOI=10.1074/jbc.c500135200;
RA Mokranjac D., Popov-Celeketic D., Hell K., Neupert W.;
RT "Role of Tim21 in mitochondrial translocation contact sites.";
RL J. Biol. Chem. 280:23437-23440(2005).
CC -!- FUNCTION: Essential component of the TIM23 complex, a complex that
CC mediates the translocation of transit peptide-containing proteins
CC across the mitochondrial inner membrane. Required to keep the TOM and
CC the TIM23 complexes in close contact. At some point, it is released
CC from the TOM23 complex to allow protein translocation into the
CC mitochondrial matrix. In the complex, it acts as an antagonist of TIM50
CC by reducing preprotein accumulation at the TOM23 complex and promotes
CC dissociation of the PAM complex from the TIM23 complex.
CC {ECO:0000269|PubMed:15797382, ECO:0000269|PubMed:15878866}.
CC -!- SUBUNIT: Component of the TIM23 complex, at least composed of TIM23,
CC TIM17, TIM50 and TIM21. Interacts directly with TIM23. Interacts with
CC TOM22 component of the TOM complex. Released from the TOM23 complex by
CC the PAM complex, leading to protein translocation into the
CC mitochondrial matrix. {ECO:0000269|PubMed:15797382,
CC ECO:0000269|PubMed:15878866}.
CC -!- INTERACTION:
CC P53220; Q12328: TIM22; NbExp=2; IntAct=EBI-23128, EBI-9132;
CC P53220; P32897: TIM23; NbExp=16; IntAct=EBI-23128, EBI-9136;
CC P53220; Q02776: TIM50; NbExp=10; IntAct=EBI-23128, EBI-30302;
CC P53220; P49334: TOM22; NbExp=2; IntAct=EBI-23128, EBI-12527;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15797382}; Single-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15797382}.
CC -!- MISCELLANEOUS: Present with 3770 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TIM21 family. {ECO:0000305}.
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DR EMBL; DQ115390; AAZ22448.1; -; Genomic_DNA.
DR EMBL; Z72818; CAA97021.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08130.1; -; Genomic_DNA.
DR PIR; S64324; S64324.
DR RefSeq; NP_011547.3; NM_001181162.3.
DR PDB; 2CIU; X-ray; 1.60 A; A=103-225.
DR PDB; 2MF7; NMR; -; A=103-225.
DR PDB; 6K7D; X-ray; 2.00 A; A=105-217.
DR PDB; 6K7E; X-ray; 1.53 A; A=105-217.
DR PDB; 6K7F; X-ray; 1.80 A; A=105-217.
DR PDB; 6K8Q; NMR; -; A=105-217.
DR PDBsum; 2CIU; -.
DR PDBsum; 2MF7; -.
DR PDBsum; 6K7D; -.
DR PDBsum; 6K7E; -.
DR PDBsum; 6K7F; -.
DR PDBsum; 6K8Q; -.
DR AlphaFoldDB; P53220; -.
DR BMRB; P53220; -.
DR SMR; P53220; -.
DR BioGRID; 33278; 179.
DR ComplexPortal; CPX-6127; TIM23 mitochondrial inner membrane pre-sequence translocase complex, sort variant.
DR DIP; DIP-3940N; -.
DR IntAct; P53220; 12.
DR MINT; P53220; -.
DR STRING; 4932.YGR033C; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR MaxQB; P53220; -.
DR PaxDb; P53220; -.
DR PRIDE; P53220; -.
DR EnsemblFungi; YGR033C_mRNA; YGR033C; YGR033C.
DR GeneID; 852921; -.
DR KEGG; sce:YGR033C; -.
DR SGD; S000003265; TIM21.
DR VEuPathDB; FungiDB:YGR033C; -.
DR eggNOG; KOG4836; Eukaryota.
DR HOGENOM; CLU_089043_1_0_1; -.
DR InParanoid; P53220; -.
DR OMA; YEWGELS; -.
DR BioCyc; YEAST:G3O-30755-MON; -.
DR EvolutionaryTrace; P53220; -.
DR PRO; PR:P53220; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53220; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IDA:SGD.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IC:ComplexPortal.
DR Gene3D; 3.10.450.320; -; 1.
DR InterPro; IPR013261; Tim21.
DR InterPro; IPR038552; Tim21_IMS_sf.
DR PANTHER; PTHR13032; PTHR13032; 1.
DR Pfam; PF08294; TIM21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Transit peptide; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..70
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 71..239
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM21"
FT /id="PRO_0000043166"
FT TOPO_DOM 71..75
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..239
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT CONFLICT 39
FT /note="T -> A (in Ref. 1; AAZ22448)"
FT /evidence="ECO:0000305"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:6K7E"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:6K7E"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6K7E"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6K7E"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2CIU"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6K7E"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:6K7E"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:6K7E"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6K7F"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:6K7E"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:6K7E"
SQ SEQUENCE 239 AA; 27206 MW; FC140F3034E5B5BB CRC64;
MSSSLPRSLL RLGHRKPLFP RYNTFVNSSV ITHTSLLRTR LYSNGTGATS GKKDDKTRNK
PKPLWPQVKS ASTFTFSGIL VIGAVGISAI VIYLILSELF SPSGDTQLFN RAVSMVEKNK
DIRSLLQCDD GITGKERLKA YGELITNDKW TRNRPIVSTK KLDKEGRTHH YMRFHVESKK
KIALVHLEAK ESKQNYQPDF INMYVDVPGE KRYYLIKPKL HPVSNSKGFL GIRWGPRKD
