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Q9CPQ3 (TOM22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial import receptor subunit TOM22 homolog
Alternative name(s):
Translocase of outer membrane 22 kDa subunit homolog
Gene names
Name:Tomm22
Synonyms:Tom22
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the movement of preproteins into the translocation pore By similarity.

Subunit structure

Forms part of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) which consists of at least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and TOMM70). Interacts with PPP2R2B and TOMM40 By similarity.

Subcellular location

Mitochondrion outer membrane; Single-pass membrane protein By similarity.

Domain

The N-terminal domain (residues 1-62) is important for binding to the unfolded mature imported proteins. Residues (49-71) of the cytoplasmic domain interacts with TOMM20 while the C-terminal segment (residues 63-82) binds presequence of preproteins. Requires the transmembrane domain (TMD), a short segment (the import sequence) in the cytoplasmic domain localizing separately from the TMD and the C-tail signal in the C-terminal domain for efficient targeting and integration into the TOM complex By similarity.

Sequence similarities

Belongs to the Tom22 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 142141Mitochondrial import receptor subunit TOM22 homolog
PRO_0000076108

Regions

Topological domain2 – 8382Cytoplasmic Potential
Transmembrane84 – 10320Helical; Potential
Topological domain104 – 14239Mitochondrial intermembrane Potential
Region41 – 5010Import sequence; necessary for mitochondrion outer membrane localization and integration in the TOM complex By similarity
Region83 – 10321TMD; necessary for mitochondrion outer membrane localization and integration in the TOM complex By similarity
Region123 – 14220C-tail signal; necessary for mitochondrion outer membrane localization and integration in the TOM complex By similarity
Compositional bias35 – 384Poly-Asp
Compositional bias110 – 1189Poly-Gln

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue151Phosphoserine By similarity
Modified residue431Phosphothreonine By similarity

Experimental info

Sequence conflict381D → H in BAB25482. Ref.1
Sequence conflict651A → T in BAB25482. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CPQ3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A5182A39B6EBBFDA

FASTA14215,537
        10         20         30         40         50         60 
MAAAVAAAGA GEPLSPEELL PKAEAEKAEE ELEEDDDDEL DETLSERLWG LTEMFPERVR 

        70         80         90        100        110        120 
SAAGATFDLS LFVAQKMYRF SRAALWIGTT SFMILVLPVV FETEKLQMEQ QQQLQQRQIL 

       130        140 
LGPNTGLSGG MPGALPPLPG KM 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and DBA/2.
Tissue: Bone marrow, Hippocampus, Small intestine and Tongue.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK008133 mRNA. Translation: BAB25482.1.
AK009868 mRNA. Translation: BAB26553.1.
AK013471 mRNA. Translation: BAB28871.1.
AK049442 mRNA. Translation: BAC33752.1.
AK150360 mRNA. Translation: BAE29495.1.
AK152843 mRNA. Translation: BAE31536.1.
AK167803 mRNA. Translation: BAE39830.1.
BC056920 mRNA. Translation: AAH56920.1.
RefSeqNP_766197.2. NM_172609.3.
UniGeneMm.246435.
Mm.485795.

3D structure databases

ProteinModelPortalQ9CPQ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230178. 2 interactions.
IntActQ9CPQ3. 2 interactions.
MINTMINT-1844683.
STRING10090.ENSMUSP00000023062.

PTM databases

PhosphoSiteQ9CPQ3.

Proteomic databases

PaxDbQ9CPQ3.
PRIDEQ9CPQ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023062; ENSMUSP00000023062; ENSMUSG00000022427.
GeneID223696.
KEGGmmu:223696.
UCSCuc007wud.1. mouse.

Organism-specific databases

CTD56993.
MGIMGI:2450248. Tomm22.

Phylogenomic databases

eggNOGNOG263720.
GeneTreeENSGT00390000016475.
HOGENOMHOG000067816.
HOVERGENHBG061819.
InParanoidQ9CPQ3.
KOK17769.
OMAMMPPAPG.
OrthoDBEOG7KWSKG.
PhylomeDBQ9CPQ3.
TreeFamTF106201.

Gene expression databases

BgeeQ9CPQ3.
GenevestigatorQ9CPQ3.

Family and domain databases

InterProIPR005683. Tom22.
[Graphical view]
PfamPF04281. Tom22. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio376826.
PROQ9CPQ3.
SOURCESearch...

Entry information

Entry nameTOM22_MOUSE
AccessionPrimary (citable) accession number: Q9CPQ3
Secondary accession number(s): Q543M4, Q9D8D3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot