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P49334 (TOM22_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial import receptor subunit TOM22
Alternative name(s):
Mitochondrial 17 kDa assembly protein
Mitochondrial 22 kDa outer membrane protein
Protein MAS17
Translocase of outer membrane 22 kDa subunit
Gene names
Name:TOM22
Synonyms:MAS17, MAS22, MOM22
Ordered Locus Names:YNL131W
ORF Names:N1217, N1862
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.8 Ref.9

Subunit structure

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. Ref.7 Ref.8 Ref.13

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.

Sequence similarities

Belongs to the Tom22 family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 152151Mitochondrial import receptor subunit TOM22
PRO_0000076113

Regions

Topological domain2 – 9796Cytoplasmic Potential
Transmembrane98 – 11922Helical; Potential
Topological domain120 – 15233Mitochondrial intermembrane Potential

Amino acid modifications

Modified residue441Phosphoserine Ref.11 Ref.12
Modified residue461Phosphoserine Ref.11 Ref.12

Sequences

Sequence LengthMass (Da)Tools
P49334 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6ACEC5D37D143CD3

FASTA15216,790
        10         20         30         40         50         60 
MVELTEIKDD VVQLDEPQFS RNQAIVEEKA SATNNDVVDD EDDSDSDFED EFDENETLLD 

        70         80         90        100        110        120 
RIVALKDIVP PGKRQTISNF FGFTSSFVRN AFTKSGNLAW TLTTTALLLG VPLSLSILAE 

       130        140        150 
QQLIEMEKTF DLQSDANNIL AQGEKDAAAT AN 

« Hide

References

« Hide 'large scale' references
[1]"The mitochondrial receptor complex: Mom22 is essential for cell viability and directly interacts with preproteins."
Hoenlinger A., Kuebrich M., Moczko M., Gaertner F., Mallet L., Bussereau F., Eckerskorn C., Lottspeich F., Dietmeier K., Jacquet M., Pfanner N.
Mol. Cell. Biol. 15:3382-3389(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-17, FUNCTION.
Strain: ATCC 204508 / S288c.
[2]"Identification of yeast MAS17 encoding the functional counterpart of the mitochondrial receptor complex protein MOM22 of Neurospora crassa."
Nakai M., Endo T.
FEBS Lett. 357:202-206(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SP1.
[3]"The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast."
Lithgow T., Junne T., Suda K., Gratzer S., Schatz G.
Proc. Natl. Acad. Sci. U.S.A. 91:11973-11977(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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."
Mallet L., Bussereau F., Jacquet M.
Yeast 11:1195-1209(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
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. expand/collapse author list , 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.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex."
Dekker P.J.T., Ryan M.T., Brix J., Mueller H., Hoenlinger A., Pfanner N.
Mol. Cell. Biol. 18:6515-6524(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TOM COMPLEX.
[8]"Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase."
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.
Nature 401:485-489(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TOM20 AND TOM70.
[9]"Multistep assembly of the protein import channel of the mitochondrial outer membrane."
Model K., Meisinger C., Prinz T., Wiedemann N., Truscott K.N., Pfanner N., Ryan M.T.
Nat. Struct. Biol. 8:361-370(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Dual role of mitofilin in mitochondrial membrane organization and protein biogenesis."
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. expand/collapse author list , Veenhuis M., Warscheid B., van der Klei I.J., Pfanner N., Chacinska A., van der Laan M.
Dev. Cell 21:694-707(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCJ1.
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46843 Genomic DNA. Translation: CAA86894.1.
X82405 Genomic DNA. Translation: CAA57799.1.
X80348 Genomic DNA. Translation: CAA56588.1. Sequence problems.
Z71407 Genomic DNA. Translation: CAA96013.1.
BK006947 Genomic DNA. Translation: DAA10417.1.
PIRS50250.
RefSeqNP_014268.1. NM_001182969.1.

3D structure databases

ProteinModelPortalP49334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35696. 64 interactions.
DIPDIP-2302N.
IntActP49334. 14 interactions.
MINTMINT-478366.
STRING4932.YNL131W.

Protein family/group databases

TCDB3.A.8.1.1. the mitochondrial protein translocase (mpt) family.

Proteomic databases

MaxQBP49334.
PaxDbP49334.
PeptideAtlasP49334.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL131W; YNL131W; YNL131W.
GeneID855592.
KEGGsce:YNL131W.

Organism-specific databases

SGDS000005075. TOM22.

Phylogenomic databases

eggNOGNOG321322.
HOGENOMHOG000206849.
KOK17769.
OMALTQIDDE.
OrthoDBEOG7D8694.

Enzyme and pathway databases

BioCycYEAST:G3O-33151-MONOMER.
ReactomeREACT_118590. Mitochondrial Protein Import (yeast).

Gene expression databases

GenevestigatorP49334.

Family and domain databases

InterProIPR005683. Tom22.
IPR020951. Tom22_fun.
[Graphical view]
PfamPF04281. Tom22. 1 hit.
[Graphical view]
TIGRFAMsTIGR00986. 3a0801s05tom22. 1 hit.
ProtoNetSearch...

Other

NextBio979738.

Entry information

Entry nameTOM22_YEAST
AccessionPrimary (citable) accession number: P49334
Secondary accession number(s): D6W151, Q36757
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families