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   27-MAR-2024, entry version 151.
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,
RC   Pancreas, 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; 7.
DR   IntAct; Q9CPQ3; 2.
DR   MINT; Q9CPQ3; -.
DR   STRING; 10090.ENSMUSP00000023062; -.
DR   GlyGen; Q9CPQ3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9CPQ3; -.
DR   PhosphoSitePlus; Q9CPQ3; -.
DR   SwissPalm; Q9CPQ3; -.
DR   EPD; Q9CPQ3; -.
DR   jPOST; Q9CPQ3; -.
DR   MaxQB; Q9CPQ3; -.
DR   PaxDb; 10090-ENSMUSP00000023062; -.
DR   PeptideAtlas; Q9CPQ3; -.
DR   ProteomicsDB; 260720; -.
DR   Pumba; Q9CPQ3; -.
DR   TopDownProteomics; Q9CPQ3; -.
DR   Antibodypedia; 291; 157 antibodies from 28 providers.
DR   DNASU; 223696; -.
DR   Ensembl; ENSMUST00000023062.5; ENSMUSP00000023062.4; ENSMUSG00000022427.5.
DR   GeneID; 223696; -.
DR   KEGG; mmu:223696; -.
DR   UCSC; uc007wud.1; mouse.
DR   AGR; MGI:2450248; -.
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; DKDSGME; -.
DR   OrthoDB; 5404341at2759; -.
DR   PhylomeDB; Q9CPQ3; -.
DR   TreeFam; TF106201; -.
DR   Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR   BioGRID-ORCS; 223696; 23 hits in 77 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 73 other cell types or tissues.
DR   ExpressionAtlas; Q9CPQ3; baseline and differential.
DR   GO; GO:0016020; C: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   CDD; cd22884; TOM22; 1.
DR   InterPro; IPR005683; Tom22.
DR   PANTHER; PTHR12504; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM22; 1.
DR   PANTHER; PTHR12504:SF0; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM22 HOMOLOG; 1.
DR   Pfam; PF04281; Tom22; 1.
DR   Genevisible; Q9CPQ3; MM.
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
//