TIM9_CAEEL
ID TIM9_CAEEL Reviewed; 90 AA.
AC Q17754; Q86B35;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim9;
GN Name=tin-9.1; Synonyms=tim9a, tin-9; ORFNames=C06G3.11;
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 [MRNA] (ISOFORM A).
RX PubMed=10611480; DOI=10.1016/s0014-5793(99)01665-8;
RA Bauer M.F., Rothbauer U., Muehlenbein N., Smith R.J.H., Gerbitz K.-D.,
RA Neupert W., Brunner M., Hofmann S.;
RT "The mitochondrial TIM22 preprotein translocase is highly conserved
RT throughout the eukaryotic kingdom.";
RL FEBS Lett. 464:41-47(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15485840; DOI=10.1074/jbc.m409618200;
RA Curran S.P., Leverich E.P., Koehler C.M., Larsen P.L.;
RT "Defective mitochondrial protein translocation precludes normal
RT Caenorhabditis elegans development.";
RL J. Biol. Chem. 279:54655-54662(2004).
CC -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. May also be required for the transfer of
CC beta-barrel precursors from the TOM complex to the sorting and assembly
CC machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC protein that protects the hydrophobic precursors from aggregation and
CC guide them through the mitochondrial intermembrane space (Probable).
CC {ECO:0000305|PubMed:15485840}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of tim-9/tin-9.1 and 3
CC copies of tim-10/tin-10, named soluble 70 kDa complex. The complex
CC associates with the tim-22 component of the TIM22 complex. Interacts
CC with multi-pass transmembrane proteins in transit (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q17754-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q17754-2; Sequence=VSP_015407;
CC -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC 2 disulfide bonds in the mitochondrial intermembrane space. However,
CC during the transit of tim-9/tin-9.1 from cytoplasm into mitochondrion,
CC the Cys residues probably coordinate zinc, thereby preventing folding
CC and allowing its transfer across mitochondrial outer membrane (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Worms display a small body size, reduced number
CC of progeny produced and partial embryonic lethality due to defects in
CC import of proteins into mitochondria. {ECO:0000269|PubMed:15485840}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; AF150108; AAD40014.1; -; mRNA.
DR EMBL; FO080396; CCD83559.1; -; Genomic_DNA.
DR EMBL; FO080396; CCD83560.1; -; Genomic_DNA.
DR PIR; T30100; T30100.
DR RefSeq; NP_001021307.1; NM_001026136.3. [Q17754-2]
DR RefSeq; NP_501094.1; NM_068693.1.
DR AlphaFoldDB; Q17754; -.
DR SMR; Q17754; -.
DR BioGRID; 42594; 3.
DR STRING; 6239.C06G3.11a; -.
DR EPD; Q17754; -.
DR PaxDb; Q17754; -.
DR PeptideAtlas; Q17754; -.
DR EnsemblMetazoa; C06G3.11.1; C06G3.11.1; WBGene00006572. [Q17754-2]
DR GeneID; 177475; -.
DR KEGG; cel:CELE_C06G3.11; -.
DR UCSC; C06G3.11a; c. elegans. [Q17754-1]
DR CTD; 177475; -.
DR WormBase; C06G3.11; CE33518; WBGene00006572; tin-9.1. [Q17754-2]
DR eggNOG; KOG3479; Eukaryota.
DR GeneTree; ENSGT00940000160102; -.
DR InParanoid; Q17754; -.
DR OMA; QDFLRMY; -.
DR OrthoDB; 1627953at2759; -.
DR PhylomeDB; Q17754; -.
DR PRO; PR:Q17754; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006572; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IMP:WormBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR Pfam; PF02953; zf-Tim10_DDP; 1.
DR SUPFAM; SSF144122; SSF144122; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Chaperone; Disulfide bond; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW Reference proteome; Translocation; Transport; Zinc.
FT CHAIN 1..90
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim9"
FT /id="PRO_0000193601"
FT MOTIF 24..48
FT /note="Twin CX3C motif"
FT DISULFID 24..48
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
FT VAR_SEQ 78..90
FT /note="IKVENGGKINKIQ -> M (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_015407"
SQ SEQUENCE 90 AA; 10193 MW; 1CAD15DFD58A1DE4 CRC64;
MTSEQNIQTF RDFLTQYNLV AEQCFNSCVN EFGSRTVSGK EESCANNCLD KFLKMTQRVS
QRFQEHQLLN AQANGAAIKV ENGGKINKIQ
