TOM22_RAT
ID TOM22_RAT Reviewed; 142 AA.
AC Q75Q41;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Mitochondrial import receptor subunit TOM22 homolog;
DE Short=rTOM22;
DE AltName: Full=Translocase of outer membrane 22 kDa subunit homolog;
GN Name=Tomm22; Synonyms=Tom22;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14985332; DOI=10.1074/jbc.m314156200;
RA Nakamura Y., Suzuki H., Sakaguchi M., Mihara K.;
RT "Targeting and assembly of rat mitochondrial translocase of outer membrane
RT 22 (TOM22) into the TOM complex.";
RL J. Biol. Chem. 279:21223-21232(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [4]
RP IDENTIFICATION IN THE TOM COMPLEX, INTERACTION WITH PPP2R2B, AND
RP MUTAGENESIS OF GLU-42; GLU-46; TRP-49 AND PRO-98.
RX PubMed=15923182; DOI=10.1074/jbc.m503693200;
RA Dagda R.K., Barwacz C.A., Cribbs J.T., Strack S.;
RT "Unfolding-resistant translocase targeting: a novel mechanism for outer
RT mitochondrial membrane localization exemplified by the Bbeta2 regulatory
RT subunit of protein phosphatase 2A.";
RL J. Biol. Chem. 280:27375-27382(2005).
RN [5]
RP FUNCTION.
RX PubMed=19401463; DOI=10.1074/jbc.m109.007492;
RA Anandatheerthavarada H.K., Sepuri N.B., Avadhani N.G.;
RT "Mitochondrial targeting of cytochrome P450 proteins containing NH2-
RT terminal chimeric signals involves an unusual TOM20/TOM22 bypass
RT mechanism.";
RL J. Biol. Chem. 284:17352-17363(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (PubMed:19401463). {ECO:0000250|UniProtKB:Q9NS69,
CC ECO:0000269|PubMed:19401463}.
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 TOMM40 (By similarity). Interacts with PPP2R2B.
CC {ECO:0000250, ECO:0000269|PubMed:15923182}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC membrane protein.
CC -!- DOMAIN: The N-terminal domain (residues 1-60) is important for binding
CC to the unfolded mature imported proteins. Residues (47-69) of the
CC cytoplasmic domain interacts with TOMM20 while the C-terminal segment
CC (residues 61-80) binds presequence of preproteins (By similarity).
CC Requires the transmembrane domain (TMD), a short segment (the import
CC sequence) in the cytoplasmic domain localizing separately from the TMD
CC and the C-tail signal in the C-terminal domain for efficient targeting
CC and integration into the TOM complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Tom22 family. {ECO:0000305}.
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DR EMBL; AB162854; BAD11364.1; -; mRNA.
DR EMBL; CH473950; EDM15790.1; -; Genomic_DNA.
DR EMBL; BC098639; AAH98639.1; -; mRNA.
DR RefSeq; NP_997679.1; NM_212514.2.
DR AlphaFoldDB; Q75Q41; -.
DR SMR; Q75Q41; -.
DR CORUM; Q75Q41; -.
DR IntAct; Q75Q41; 1.
DR STRING; 10116.ENSRNOP00000019323; -.
DR iPTMnet; Q75Q41; -.
DR PhosphoSitePlus; Q75Q41; -.
DR jPOST; Q75Q41; -.
DR PaxDb; Q75Q41; -.
DR PRIDE; Q75Q41; -.
DR GeneID; 300075; -.
DR KEGG; rno:300075; -.
DR UCSC; RGD:1303260; rat.
DR CTD; 56993; -.
DR RGD; 1303260; Tomm22.
DR VEuPathDB; HostDB:ENSRNOG00000014058; -.
DR eggNOG; KOG4111; Eukaryota.
DR HOGENOM; CLU_108175_1_0_1; -.
DR InParanoid; Q75Q41; -.
DR OMA; IKGLYAY; -.
DR OrthoDB; 1625053at2759; -.
DR PhylomeDB; Q75Q41; -.
DR TreeFam; TF106201; -.
DR Reactome; R-RNO-5205685; PINK1-PRKN Mediated Mitophagy.
DR PRO; PR:Q75Q41; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000014058; Expressed in thymus and 20 other tissues.
DR Genevisible; Q75Q41; RN.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IMP:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0051204; P:protein insertion into mitochondrial membrane; IMP:RGD.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP: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_0000383359"
FT TOPO_DOM 2..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..142
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 1..40
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 REGION 83..103
FT /note="TMD; necessary for mitochondrion outer membrane
FT localization and integration in the TOM complex"
FT REGION 123..142
FT /note="C-tail signal; necessary for mitochondrion outer
FT membrane localization and integration in the TOM complex"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS69"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS69"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPQ3"
FT MUTAGEN 42
FT /note="E->Q: Inhibits localization to the mitochondrion
FT outer membrane."
FT /evidence="ECO:0000269|PubMed:15923182"
FT MUTAGEN 46
FT /note="E->P: Inhibits localization to the mitochondrion
FT outer membrane."
FT /evidence="ECO:0000269|PubMed:15923182"
FT MUTAGEN 49
FT /note="W->P: Inhibits localization to the mitochondrion
FT outer membrane."
FT /evidence="ECO:0000269|PubMed:15923182"
FT MUTAGEN 98
FT /note="P->A: Inhibits localization to the mitochondrion
FT outer membrane."
FT /evidence="ECO:0000269|PubMed:15923182"
SQ SEQUENCE 142 AA; 15491 MW; C1259302C15CA3AB CRC64;
MAAAVAAAGA GEPLSPEELV PKAEAEKAEE DLEEDDDDEL DETLSERLWG LTEMFPERVR
SAAGATFDLS LFVAQKMYRF SRAALWIGTT SFMILVLPVV FETEKLQMEQ QQQLQQRQIL
LGPNTGLSGG MPGALPPLPG KI
