TOM40_CAEEL
ID TOM40_CAEEL Reviewed; 301 AA.
AC Q18090;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Mitochondrial import receptor subunit TOM40 homolog;
DE AltName: Full=Translocase of outer membrane 40 kDa subunit homolog;
GN Name=tomm-40 {ECO:0000312|WormBase:C18E9.6};
GN ORFNames=C18E9.6 {ECO:0000312|WormBase:C18E9.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21264209; DOI=10.1371/journal.pone.0014507;
RA Billing O., Kao G., Naredi P.;
RT "Mitochondrial function is required for secretion of DAF-28/insulin in C.
RT elegans.";
RL PLoS ONE 6:E14507-E14507(2011).
CC -!- FUNCTION: Channel-forming protein essential for import of protein
CC precursors into mitochondria. Specifically required for nnt-1
CC accumulation in the mitochondria and may be involved in the secretion
CC of daf-28/insulin from the mitochondria. Required for embryonic and
CC larval development. {ECO:0000269|PubMed:21264209}.
CC -!- SUBUNIT: Forms part of the preprotein translocase complex of the outer
CC mitochondrial membrane (TOM complex). Interacts with mitochondrial
CC targeting sequences. {ECO:0000250|UniProtKB:O96008}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:21264209}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21264209}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, but highly expressed in the
CC pharyngeal muscles, the nerve ring, the intestine, gonadal sheath and
CC in the tail hypodermis. {ECO:0000269|PubMed:21264209}.
CC -!- DISRUPTION PHENOTYPE: Mutants arrest during the larval developmental
CC stage. Impaired mitochondrial homeostasis with the up-regulation of the
CC mitochondrial unfolded protein chaperone hsp-6. RNAi-mediated knockdown
CC results in embryonic lethality or larval lethality between the L1 and
CC L3 stage of larval development. Surviving progeny are growth retarded.
CC No localization of the mitochondrial targeted protein nnt-1 to the
CC mitochondria of intestinal cells. {ECO:0000269|PubMed:21264209}.
CC -!- SIMILARITY: Belongs to the Tom40 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z70034; CAA93850.1; -; Genomic_DNA.
DR PIR; T19399; T19399.
DR RefSeq; NP_495912.1; NM_063511.3.
DR AlphaFoldDB; Q18090; -.
DR SMR; Q18090; -.
DR BioGRID; 39758; 15.
DR DIP; DIP-25856N; -.
DR IntAct; Q18090; 1.
DR STRING; 6239.C18E9.6; -.
DR TCDB; 1.B.8.2.8; the mitochondrial and plastid porin (mpp) family.
DR EPD; Q18090; -.
DR PaxDb; Q18090; -.
DR PeptideAtlas; Q18090; -.
DR EnsemblMetazoa; C18E9.6.1; C18E9.6.1; WBGene00007686.
DR GeneID; 174431; -.
DR KEGG; cel:CELE_C18E9.6; -.
DR UCSC; C18E9.6; c. elegans.
DR CTD; 174431; -.
DR WormBase; C18E9.6; CE05298; WBGene00007686; tomm-40.
DR eggNOG; KOG3296; Eukaryota.
DR GeneTree; ENSGT00390000003308; -.
DR HOGENOM; CLU_054399_0_0_1; -.
DR InParanoid; Q18090; -.
DR OMA; SHQFAMG; -.
DR OrthoDB; 1346842at2759; -.
DR PhylomeDB; Q18090; -.
DR SignaLink; Q18090; -.
DR PRO; PR:Q18090; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007686; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:WormBase.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IBA:GO_Central.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:UniProtKB.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR CDD; cd07305; Porin3_Tom40; 1.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR027246; Porin_Euk/Tom40.
DR InterPro; IPR037930; Tom40.
DR PANTHER; PTHR10802; PTHR10802; 1.
DR Pfam; PF01459; Porin_3; 1.
PE 2: Evidence at transcript level;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Porin; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane beta strand; Transport.
FT CHAIN 1..301
FT /note="Mitochondrial import receptor subunit TOM40 homolog"
FT /id="PRO_0000051529"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 32386 MW; 4247A3593B5EEC57 CRC64;
MATPTESELA SPIPQTNPGS YEELHRKARD VFPTCFEGAK LMVNKGLSSH FQVSHTLSLS
AMNTGYRFGA TYVGTNQVGP AEAYPILLGD TDVNGNTTAT ILHQLGIYRT KLQGQIQQGK
LAGAQATIER KGRLSTLGLT LANIDLVNEA GILVGQFLRR LTPRLDVGTE MVYQYGKNIP
GGQISVLSYA ARYTANHFIA AATLGASGVH LTYYHKQNEN LAFGVEFECN ANVGEAVTTL
AYQTELPEEG VTMRASFDTN WTVGGVFEKR LSQQLPFTLA LSGTLNHVKA AGKFGIGLII
G