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   24-JAN-2024, entry version 171.
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; 181.
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; 4932-YGR033C; -.
DR   PeptideAtlas; P53220; -.
DR   EnsemblFungi; YGR033C_mRNA; YGR033C; YGR033C.
DR   GeneID; 852921; -.
DR   KEGG; sce:YGR033C; -.
DR   AGR; SGD:S000003265; -.
DR   SGD; S000003265; TIM21.
DR   VEuPathDB; FungiDB:YGR033C; -.
DR   eggNOG; KOG4836; Eukaryota.
DR   HOGENOM; CLU_089043_1_0_1; -.
DR   InParanoid; P53220; -.
DR   OMA; HVESKQK; -.
DR   OrthoDB; 1386256at2759; -.
DR   BioCyc; YEAST:G3O-30755-MONOMER; -.
DR   BioGRID-ORCS; 852921; 2 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P53220; -.
DR   PRO; PR:P53220; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53220; Protein.
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; NAS:ComplexPortal.
DR   Gene3D; 3.10.450.320; Mitochondrial import inner membrane translocase subunit Tim21; 1.
DR   InterPro; IPR013261; Tim21.
DR   InterPro; IPR038552; Tim21_IMS_sf.
DR   PANTHER; PTHR13032; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM21; 1.
DR   PANTHER; PTHR13032:SF6; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM21; 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
//