ID   TOM22_YEAST             Reviewed;         152 AA.
AC   P49334; D6W151; Q36757;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 196.
DE   RecName: Full=Mitochondrial import receptor subunit TOM22;
DE   AltName: Full=Mitochondrial 17 kDa assembly protein;
DE   AltName: Full=Mitochondrial 22 kDa outer membrane protein;
DE   AltName: Full=Protein MAS17;
DE   AltName: Full=Translocase of outer membrane 22 kDa subunit;
GN   Name=TOM22; Synonyms=MAS17, MAS22, MOM22; OrderedLocusNames=YNL131W;
GN   ORFNames=N1217, N1862;
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], PROTEIN SEQUENCE OF 2-17, AND FUNCTION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7760834; DOI=10.1128/mcb.15.6.3382;
RA   Hoenlinger A., Kuebrich M., Moczko M., Gaertner F., Mallet L.,
RA   Bussereau F., Eckerskorn C., Lottspeich F., Dietmeier K., Jacquet M.,
RA   Pfanner N.;
RT   "The mitochondrial receptor complex: Mom22 is essential for cell viability
RT   and directly interacts with preproteins.";
RL   Mol. Cell. Biol. 15:3382-3389(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SP1;
RX   PubMed=7805891; DOI=10.1016/0014-5793(94)01362-5;
RA   Nakai M., Endo T.;
RT   "Identification of yeast MAS17 encoding the functional counterpart of the
RT   mitochondrial receptor complex protein MOM22 of Neurospora crassa.";
RL   FEBS Lett. 357:202-206(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7991567; DOI=10.1073/pnas.91.25.11973;
RA   Lithgow T., Junne T., Suda K., Gratzer S., Schatz G.;
RT   "The mitochondrial outer membrane protein Mas22p is essential for protein
RT   import and viability of yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:11973-11977(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8619318; DOI=10.1002/yea.320111210;
RA   Mallet L., Bussereau F., Jacquet M.;
RT   "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT   CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT   deaminase gene and 14 new open reading frames.";
RL   Yeast 11:1195-1209(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [6]
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   [7]
RP   IDENTIFICATION IN THE TOM COMPLEX.
RX   PubMed=9774667; DOI=10.1128/mcb.18.11.6515;
RA   Dekker P.J.T., Ryan M.T., Brix J., Mueller H., Hoenlinger A., Pfanner N.;
RT   "Preprotein translocase of the outer mitochondrial membrane: molecular
RT   dissection and assembly of the general import pore complex.";
RL   Mol. Cell. Biol. 18:6515-6524(1998).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH TOM20 AND TOM70.
RX   PubMed=10519552; DOI=10.1038/46802;
RA   van Wilpe S., Ryan M.T., Hill K., Maarse A.C., Meisinger C., Brix J.,
RA   Dekker P.J.T., Moczko M., Wagner R., Meijer M., Guiard B., Hoenlinger A.,
RA   Pfanner N.;
RT   "Tom22 is a multifunctional organizer of the mitochondrial preprotein
RT   translocase.";
RL   Nature 401:485-489(1999).
RN   [9]
RP   FUNCTION.
RX   PubMed=11276259; DOI=10.1038/86253;
RA   Model K., Meisinger C., Prinz T., Wiedemann N., Truscott K.N., Pfanner N.,
RA   Ryan M.T.;
RT   "Multistep assembly of the protein import channel of the mitochondrial
RT   outer membrane.";
RL   Nat. Struct. Biol. 8:361-370(2001).
RN   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [13]
RP   INTERACTION WITH FCJ1.
RX   PubMed=21944719; DOI=10.1016/j.devcel.2011.08.026;
RA   von der Malsburg K., Muller J.M., Bohnert M., Oeljeklaus S.,
RA   Kwiatkowska P., Becker T., Loniewska-Lwowska A., Wiese S., Rao S.,
RA   Milenkovic D., Hutu D.P., Zerbes R.M., Schulze-Specking A., Meyer H.E.,
RA   Martinou J.C., Rospert S., Rehling P., Meisinger C., Veenhuis M.,
RA   Warscheid B., van der Klei I.J., Pfanner N., Chacinska A., van der Laan M.;
RT   "Dual role of mitofilin in mitochondrial membrane organization and protein
RT   biogenesis.";
RL   Dev. Cell 21:694-707(2011).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Central component of the TOM (translocase of outer membrane)
CC       receptor complex responsible for the recognition and translocation of
CC       cytosolically synthesized mitochondrial preproteins. Together with
CC       TOM20 and TOM70 functions as the transit peptide receptor at the
CC       surface of the mitochondrion outer membrane and facilitates the
CC       movement of preproteins into the TOM40 translocation pore. Docks TOM20
CC       and TOM70 for interaction with the general TOM40 import pore (GIP)
CC       complex. May regulate the TOM machinery organization, stability and
CC       channel gating. {ECO:0000269|PubMed:10519552,
CC       ECO:0000269|PubMed:11276259, ECO:0000269|PubMed:7760834}.
CC   -!- SUBUNIT: Forms part of the preprotein translocase complex of the outer
CC       mitochondrial membrane (TOM complex) which consists of at least 7
CC       different proteins (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40 and TOM70).
CC       Interacts with TOM20 and TOM70. Interacts with FCJ1.
CC       {ECO:0000269|PubMed:10519552, ECO:0000269|PubMed:21944719,
CC       ECO:0000269|PubMed:9774667}.
CC   -!- INTERACTION:
CC       P49334; P53969: SAM50; NbExp=6; IntAct=EBI-12527, EBI-28646;
CC       P49334; P53220: TIM21; NbExp=2; IntAct=EBI-12527, EBI-23128;
CC       P49334; P35180: TOM20; NbExp=5; IntAct=EBI-12527, EBI-12522;
CC       P49334; P23644: TOM40; NbExp=9; IntAct=EBI-12527, EBI-12539;
CC       P49334; Q07812: BAX; Xeno; NbExp=3; IntAct=EBI-12527, EBI-516580;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type II
CC       membrane protein.
CC   -!- DOMAIN: Its cytoplasmic domain associates with the cytoplasmic domains
CC       of TOM20 and TOM70. Its intermembrane space domain provides a trans
CC       binding site for presequences and the single membrane anchor is
CC       required for a stable interaction between the GIP complex proteins.
CC   -!- MISCELLANEOUS: Present with 6610 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the Tom22 family. {ECO:0000305}.
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DR   EMBL; Z46843; CAA86894.1; -; Genomic_DNA.
DR   EMBL; X82405; CAA57799.1; -; Genomic_DNA.
DR   EMBL; X80348; CAA56588.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; Z71407; CAA96013.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10417.1; -; Genomic_DNA.
DR   PIR; S50250; S50250.
DR   RefSeq; NP_014268.1; NM_001182969.1.
DR   PDB; 6JNF; EM; 3.81 A; C/H=1-152.
DR   PDB; 6UCU; EM; 3.06 A; B/J=1-152.
DR   PDB; 6UCV; EM; 4.10 A; B/J/b/j=1-152.
DR   PDB; 8HCO; EM; 4.10 A; B/J=1-152.
DR   PDB; 8W5J; EM; 4.40 A; B/J=1-152.
DR   PDB; 8W5K; EM; 3.60 A; B/J=1-152.
DR   PDB; 8XKW; EM; 3.64 A; B/G=1-152.
DR   PDB; 8XKX; EM; 3.70 A; B/G=1-152.
DR   PDB; 8XKY; EM; 3.42 A; B/G=1-152.
DR   PDB; 9J99; EM; 2.94 A; B/J=1-152.
DR   AlphaFoldDB; P49334; -.
DR   EMDB; EMD-20728; -.
DR   EMDB; EMD-20729; -.
DR   EMDB; EMD-34660; -.
DR   EMDB; EMD-37294; -.
DR   EMDB; EMD-37295; -.
DR   EMDB; EMD-38429; -.
DR   EMDB; EMD-38430; -.
DR   EMDB; EMD-38431; -.
DR   EMDB; EMD-61256; -.
DR   EMDB; EMD-9851; -.
DR   SMR; P49334; -.
DR   BioGRID; 35696; 351.
DR   ComplexPortal; CPX-473; TOM40 mitochondrial outer membrane translocase core complex.
DR   ComplexPortal; CPX-474; TOM40 mitochondrial outer membrane translocase holocomplex.
DR   DIP; DIP-2302N; -.
DR   FunCoup; P49334; 367.
DR   IntAct; P49334; 45.
DR   MINT; P49334; -.
DR   STRING; 4932.YNL131W; -.
DR   TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR   iPTMnet; P49334; -.
DR   PaxDb; 4932-YNL131W; -.
DR   PeptideAtlas; P49334; -.
DR   EnsemblFungi; YNL131W_mRNA; YNL131W; YNL131W.
DR   GeneID; 855592; -.
DR   KEGG; sce:YNL131W; -.
DR   AGR; SGD:S000005075; -.
DR   SGD; S000005075; TOM22.
DR   VEuPathDB; FungiDB:YNL131W; -.
DR   eggNOG; KOG4111; Eukaryota.
DR   HOGENOM; CLU_094333_2_0_1; -.
DR   InParanoid; P49334; -.
DR   OMA; LVWIVTT; -.
DR   OrthoDB; 10016939at2759; -.
DR   BioCyc; YEAST:G3O-33151-MONOMER; -.
DR   BioGRID-ORCS; 855592; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P49334; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P49334; protein.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR   GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR   GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IDA:ComplexPortal.
DR   CDD; cd22884; TOM22; 1.
DR   InterPro; IPR005683; Tom22.
DR   InterPro; IPR020951; Tom22_fungi.
DR   NCBIfam; TIGR00986; 3a0801s05tom22; 1.
DR   PANTHER; PTHR12504; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM22; 1.
DR   PANTHER; PTHR12504:SF0; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM22 HOMOLOG; 1.
DR   Pfam; PF04281; Tom22; 1.
DR   PDBsum; 6JNF; -.
DR   PDBsum; 6UCU; -.
DR   PDBsum; 6UCV; -.
DR   PDBsum; 8HCO; -.
DR   PDBsum; 8W5J; -.
DR   PDBsum; 8W5K; -.
DR   PDBsum; 8XKW; -.
DR   PDBsum; 8XKX; -.
DR   PDBsum; 8XKY; -.
DR   PDBsum; 9J99; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; Protein transport; Receptor;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7760834"
FT   CHAIN           2..152
FT                   /note="Mitochondrial import receptor subunit TOM22"
FT                   /id="PRO_0000076113"
FT   TOPO_DOM        2..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..152
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          27..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..49
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   HELIX           88..134
FT                   /evidence="ECO:0007829|PDB:9J99"
SQ   SEQUENCE   152 AA;  16790 MW;  6ACEC5D37D143CD3 CRC64;
     MVELTEIKDD VVQLDEPQFS RNQAIVEEKA SATNNDVVDD EDDSDSDFED EFDENETLLD
     RIVALKDIVP PGKRQTISNF FGFTSSFVRN AFTKSGNLAW TLTTTALLLG VPLSLSILAE
     QQLIEMEKTF DLQSDANNIL AQGEKDAAAT AN
//