TOM22_MOUSE
ID TOM22_MOUSE Reviewed; 142 AA.
AC Q9CPQ3; Q543M4; Q9D8D3;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Mitochondrial import receptor subunit TOM22 homolog;
DE AltName: Full=Translocase of outer membrane 22 kDa subunit homolog;
GN Name=Tomm22; Synonyms=Tom22;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Bone marrow, Hippocampus, Small intestine, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Central receptor component of the translocase of the outer
CC membrane of mitochondria (TOM complex) responsible for the recognition
CC and translocation of cytosolically synthesized mitochondrial
CC preproteins. Together with the peripheral receptor TOM20 functions as
CC the transit peptide receptor and facilitates the movement of
CC preproteins into the translocation pore (By similarity). Required for
CC the translocation across the mitochondrial outer membrane of cytochrome
CC P450 monooxygenases (By similarity). {ECO:0000250|UniProtKB:Q75Q41,
CC ECO:0000250|UniProtKB:Q9NS69}.
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 (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and
CC TOMM70). Interacts with PPP2R2B and TOMM40 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The N-terminal domain (residues 1-62) is important for binding
CC to the unfolded mature imported proteins. Residues (49-71) of the
CC cytoplasmic domain interacts with TOMM20 while the C-terminal segment
CC (residues 63-82) binds presequence of preproteins. Requires the
CC transmembrane domain (TMD), a short segment (the import sequence) in
CC the cytoplasmic domain localizing separately from the TMD and the C-
CC tail signal in the C-terminal domain for efficient targeting and
CC integration into the TOM complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Tom22 family. {ECO:0000305}.
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DR EMBL; AK008133; BAB25482.1; -; mRNA.
DR EMBL; AK009868; BAB26553.1; -; mRNA.
DR EMBL; AK013471; BAB28871.1; -; mRNA.
DR EMBL; AK049442; BAC33752.1; -; mRNA.
DR EMBL; AK150360; BAE29495.1; -; mRNA.
DR EMBL; AK152843; BAE31536.1; -; mRNA.
DR EMBL; AK167803; BAE39830.1; -; mRNA.
DR EMBL; BC056920; AAH56920.1; -; mRNA.
DR CCDS; CCDS27646.1; -.
DR RefSeq; NP_766197.2; NM_172609.3.
DR AlphaFoldDB; Q9CPQ3; -.
DR SMR; Q9CPQ3; -.
DR BioGRID; 230178; 6.
DR IntAct; Q9CPQ3; 2.
DR MINT; Q9CPQ3; -.
DR STRING; 10090.ENSMUSP00000023062; -.
DR iPTMnet; Q9CPQ3; -.
DR PhosphoSitePlus; Q9CPQ3; -.
DR SwissPalm; Q9CPQ3; -.
DR EPD; Q9CPQ3; -.
DR jPOST; Q9CPQ3; -.
DR MaxQB; Q9CPQ3; -.
DR PaxDb; Q9CPQ3; -.
DR PeptideAtlas; Q9CPQ3; -.
DR PRIDE; Q9CPQ3; -.
DR ProteomicsDB; 260720; -.
DR TopDownProteomics; Q9CPQ3; -.
DR Antibodypedia; 291; 123 antibodies from 28 providers.
DR DNASU; 223696; -.
DR Ensembl; ENSMUST00000023062; ENSMUSP00000023062; ENSMUSG00000022427.
DR GeneID; 223696; -.
DR KEGG; mmu:223696; -.
DR UCSC; uc007wud.1; mouse.
DR CTD; 56993; -.
DR MGI; MGI:2450248; Tomm22.
DR VEuPathDB; HostDB:ENSMUSG00000022427; -.
DR eggNOG; KOG4111; Eukaryota.
DR GeneTree; ENSGT00390000016475; -.
DR HOGENOM; CLU_108175_1_0_1; -.
DR InParanoid; Q9CPQ3; -.
DR OMA; IKGLYAY; -.
DR OrthoDB; 1625053at2759; -.
DR PhylomeDB; Q9CPQ3; -.
DR TreeFam; TF106201; -.
DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR BioGRID-ORCS; 223696; 23 hits in 72 CRISPR screens.
DR ChiTaRS; Tomm22; mouse.
DR PRO; PR:Q9CPQ3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9CPQ3; protein.
DR Bgee; ENSMUSG00000022427; Expressed in spermatid and 70 other tissues.
DR ExpressionAtlas; Q9CPQ3; baseline and differential.
DR Genevisible; Q9CPQ3; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008320; F:protein transmembrane transporter activity; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051204; P:protein insertion into mitochondrial membrane; ISO:MGI.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR InterPro; IPR005683; Tom22.
DR PANTHER; PTHR12504; PTHR12504; 1.
DR Pfam; PF04281; Tom22; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Protein transport; Receptor; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NS69"
FT CHAIN 2..142
FT /note="Mitochondrial import receptor subunit TOM22 homolog"
FT /id="PRO_0000076108"
FT TOPO_DOM 2..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..142
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..50
FT /note="Import sequence; necessary for mitochondrion outer
FT membrane localization and integration in the TOM complex"
FT /evidence="ECO:0000250"
FT REGION 83..103
FT /note="TMD; necessary for mitochondrion outer membrane
FT localization and integration in the TOM complex"
FT /evidence="ECO:0000250"
FT REGION 123..142
FT /note="C-tail signal; necessary for mitochondrion outer
FT membrane localization and integration in the TOM complex"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS69"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS69"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS69"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 38
FT /note="D -> H (in Ref. 1; BAB25482)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="A -> T (in Ref. 1; BAB25482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 15537 MW; A5182A39B6EBBFDA CRC64;
MAAAVAAAGA GEPLSPEELL PKAEAEKAEE ELEEDDDDEL DETLSERLWG LTEMFPERVR
SAAGATFDLS LFVAQKMYRF SRAALWIGTT SFMILVLPVV FETEKLQMEQ QQQLQQRQIL
LGPNTGLSGG MPGALPPLPG KM
