TOM22_YEAST
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 03-AUG-2022, entry version 180.
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;
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=4; IntAct=EBI-12527, EBI-12522;
CC P49334; P23644: TOM40; NbExp=8; 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 PDBsum; 6JNF; -.
DR PDBsum; 6UCU; -.
DR PDBsum; 6UCV; -.
DR AlphaFoldDB; P49334; -.
DR SMR; P49334; -.
DR BioGRID; 35696; 331.
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 IntAct; P49334; 19.
DR MINT; P49334; -.
DR STRING; 4932.YNL131W; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR iPTMnet; P49334; -.
DR MaxQB; P49334; -.
DR PaxDb; P49334; -.
DR PRIDE; P49334; -.
DR EnsemblFungi; YNL131W_mRNA; YNL131W; YNL131W.
DR GeneID; 855592; -.
DR KEGG; sce:YNL131W; -.
DR SGD; S000005075; TOM22.
DR VEuPathDB; FungiDB:YNL131W; -.
DR eggNOG; KOG4111; Eukaryota.
DR GeneTree; ENSGT00390000016475; -.
DR HOGENOM; CLU_094333_2_0_1; -.
DR InParanoid; P49334; -.
DR OMA; VGNLVWI; -.
DR BioCyc; YEAST:G3O-33151-MON; -.
DR PRO; PR:P49334; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P49334; protein.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:ComplexPortal.
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 InterPro; IPR005683; Tom22.
DR InterPro; IPR020951; Tom22_fungi.
DR PANTHER; PTHR12504; PTHR12504; 1.
DR Pfam; PF04281; Tom22; 1.
DR TIGRFAMs; TIGR00986; 3a0801s05tom22; 1.
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 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 87..134
FT /evidence="ECO:0007829|PDB:6UCU"
SQ SEQUENCE 152 AA; 16790 MW; 6ACEC5D37D143CD3 CRC64;
MVELTEIKDD VVQLDEPQFS RNQAIVEEKA SATNNDVVDD EDDSDSDFED EFDENETLLD
RIVALKDIVP PGKRQTISNF FGFTSSFVRN AFTKSGNLAW TLTTTALLLG VPLSLSILAE
QQLIEMEKTF DLQSDANNIL AQGEKDAAAT AN
