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Mitochondrial import receptor subunit TOM22 (Mitochondrial 17 kDa assembly protein) (Mitochondrial 22 kDa outer membrane protein) (Protein MAS17) (Translocase of outer membrane 22 kDa subunit)

 TOM22_YEAST             Reviewed;         152 AA.
P49334; D6W151; Q36757;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 160.
RecName: Full=Mitochondrial import receptor subunit TOM22;
AltName: Full=Mitochondrial 17 kDa assembly protein;
AltName: Full=Mitochondrial 22 kDa outer membrane protein;
AltName: Full=Protein MAS17;
AltName: Full=Translocase of outer membrane 22 kDa subunit;
Name=TOM22; Synonyms=MAS17, MAS22, MOM22; OrderedLocusNames=YNL131W;
ORFNames=N1217, N1862;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-17, AND
FUNCTION.
STRAIN=ATCC 204508 / S288c;
PubMed=7760834; DOI=10.1128/MCB.15.6.3382;
Hoenlinger A., Kuebrich M., Moczko M., Gaertner F., Mallet L.,
Bussereau F., Eckerskorn C., Lottspeich F., Dietmeier K., Jacquet M.,
Pfanner N.;
"The mitochondrial receptor complex: Mom22 is essential for cell
viability and directly interacts with preproteins.";
Mol. Cell. Biol. 15:3382-3389(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SP1;
PubMed=7805891; DOI=10.1016/0014-5793(94)01362-5;
Nakai M., Endo T.;
"Identification of yeast MAS17 encoding the functional counterpart of
the mitochondrial receptor complex protein MOM22 of Neurospora
crassa.";
FEBS Lett. 357:202-206(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7991567; DOI=10.1073/pnas.91.25.11973;
Lithgow T., Junne T., Suda K., Gratzer S., Schatz G.;
"The mitochondrial outer membrane protein Mas22p is essential for
protein import and viability of yeast.";
Proc. Natl. Acad. Sci. U.S.A. 91:11973-11977(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8619318; DOI=10.1002/yea.320111210;
Mallet L., Bussereau F., Jacquet M.;
"A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
deaminase gene and 14 new open reading frames.";
Yeast 11:1195-1209(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[6]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[7]
IDENTIFICATION IN THE TOM COMPLEX.
PubMed=9774667; DOI=10.1128/MCB.18.11.6515;
Dekker P.J.T., Ryan M.T., Brix J., Mueller H., Hoenlinger A.,
Pfanner N.;
"Preprotein translocase of the outer mitochondrial membrane: molecular
dissection and assembly of the general import pore complex.";
Mol. Cell. Biol. 18:6515-6524(1998).
[8]
FUNCTION, AND INTERACTION WITH TOM20 AND TOM70.
PubMed=10519552; DOI=10.1038/46802;
van Wilpe S., Ryan M.T., Hill K., Maarse A.C., Meisinger C., Brix J.,
Dekker P.J.T., Moczko M., Wagner R., Meijer M., Guiard B.,
Hoenlinger A., Pfanner N.;
"Tom22 is a multifunctional organizer of the mitochondrial preprotein
translocase.";
Nature 401:485-489(1999).
[9]
FUNCTION.
PubMed=11276259; DOI=10.1038/86253;
Model K., Meisinger C., Prinz T., Wiedemann N., Truscott K.N.,
Pfanner N., Ryan M.T.;
"Multistep assembly of the protein import channel of the mitochondrial
outer membrane.";
Nat. Struct. Biol. 8:361-370(2001).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[13]
INTERACTION WITH FCJ1.
PubMed=21944719; DOI=10.1016/j.devcel.2011.08.026;
von der Malsburg K., Muller J.M., Bohnert M., Oeljeklaus S.,
Kwiatkowska P., Becker T., Loniewska-Lwowska A., Wiese S., Rao S.,
Milenkovic D., Hutu D.P., Zerbes R.M., Schulze-Specking A.,
Meyer H.E., Martinou J.C., Rospert S., Rehling P., Meisinger C.,
Veenhuis M., Warscheid B., van der Klei I.J., Pfanner N.,
Chacinska A., van der Laan M.;
"Dual role of mitofilin in mitochondrial membrane organization and
protein biogenesis.";
Dev. Cell 21:694-707(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Central component of the TOM (translocase of outer
membrane) receptor complex responsible for the recognition and
translocation of cytosolically synthesized mitochondrial
preproteins. Together with TOM20 and TOM70 functions as the
transit peptide receptor at the surface of the mitochondrion outer
membrane and facilitates the movement of preproteins into the
TOM40 translocation pore. Docks TOM20 and TOM70 for interaction
with the general TOM40 import pore (GIP) complex. May regulate the
TOM machinery organization, stability and channel gating.
{ECO:0000269|PubMed:10519552, ECO:0000269|PubMed:11276259,
ECO:0000269|PubMed:7760834}.
-!- SUBUNIT: Forms part of the preprotein translocase complex of the
outer mitochondrial membrane (TOM complex) which consists of at
least 7 different proteins (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40
and TOM70). Interacts with TOM20 and TOM70. Interacts with FCJ1.
{ECO:0000269|PubMed:10519552, ECO:0000269|PubMed:21944719,
ECO:0000269|PubMed:9774667}.
-!- INTERACTION:
Q07812:BAX (xeno); NbExp=3; IntAct=EBI-12527, EBI-516580;
P53969:SAM50; NbExp=6; IntAct=EBI-12527, EBI-28646;
P53220:TIM21; NbExp=2; IntAct=EBI-12527, EBI-23128;
P35180:TOM20; NbExp=4; IntAct=EBI-12527, EBI-12522;
P23644:TOM40; NbExp=8; IntAct=EBI-12527, EBI-12539;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
type II membrane protein.
-!- DOMAIN: Its cytoplasmic domain associates with the cytoplasmic
domains of TOM20 and TOM70. Its intermembrane space domain
provides a trans binding site for presequences and the single
membrane anchor is required for a stable interaction between the
GIP complex proteins.
-!- MISCELLANEOUS: Present with 6610 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the Tom22 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z46843; CAA86894.1; -; Genomic_DNA.
EMBL; X82405; CAA57799.1; -; Genomic_DNA.
EMBL; X80348; CAA56588.1; ALT_SEQ; Genomic_DNA.
EMBL; Z71407; CAA96013.1; -; Genomic_DNA.
EMBL; BK006947; DAA10417.1; -; Genomic_DNA.
PIR; S50250; S50250.
RefSeq; NP_014268.1; NM_001182969.1.
ProteinModelPortal; P49334; -.
BioGrid; 35696; 71.
ComplexPortal; CPX-473; Mitochondrial outer membrane translocase core complex.
ComplexPortal; CPX-474; Mitochondrial outer membrane translocase holocomplex.
DIP; DIP-2302N; -.
IntAct; P49334; 19.
MINT; P49334; -.
STRING; 4932.YNL131W; -.
TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
iPTMnet; P49334; -.
MaxQB; P49334; -.
PaxDb; P49334; -.
PRIDE; P49334; -.
EnsemblFungi; YNL131W_mRNA; YNL131W_mRNA; YNL131W.
GeneID; 855592; -.
KEGG; sce:YNL131W; -.
SGD; S000005075; TOM22.
GeneTree; ENSGT00390000016475; -.
HOGENOM; HOG000206849; -.
InParanoid; P49334; -.
KO; K17769; -.
OMA; TAMEQEY; -.
OrthoDB; EOG092C5OM9; -.
BioCyc; YEAST:G3O-33151-MONOMER; -.
PRO; PR:P49334; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IDA:SGD.
GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
GO; GO:0045040; P:protein import into mitochondrial outer membrane; IMP:SGD.
InterPro; IPR005683; Tom22.
InterPro; IPR020951; Tom22_fungi.
PANTHER; PTHR12504:SF0; PTHR12504:SF0; 1.
Pfam; PF04281; Tom22; 1.
TIGRFAMs; TIGR00986; 3a0801s05tom22; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Membrane; Mitochondrion;
Mitochondrion outer membrane; Phosphoprotein; Protein transport;
Receptor; Reference proteome; Translocation; Transmembrane;
Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7760834}.
CHAIN 2 152 Mitochondrial import receptor subunit
TOM22.
/FTId=PRO_0000076113.
TOPO_DOM 2 97 Cytoplasmic. {ECO:0000255}.
TRANSMEM 98 119 Helical. {ECO:0000255}.
TOPO_DOM 120 152 Mitochondrial intermembrane.
{ECO:0000255}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
SEQUENCE 152 AA; 16790 MW; 6ACEC5D37D143CD3 CRC64;
MVELTEIKDD VVQLDEPQFS RNQAIVEEKA SATNNDVVDD EDDSDSDFED EFDENETLLD
RIVALKDIVP PGKRQTISNF FGFTSSFVRN AFTKSGNLAW TLTTTALLLG VPLSLSILAE
QQLIEMEKTF DLQSDANNIL AQGEKDAAAT AN


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