TIM14_DEBHA
ID TIM14_DEBHA Reviewed; 172 AA.
AC Q6BH37;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM14;
DE AltName: Full=Presequence translocated-associated motor subunit PAM18;
GN Name=PAM18; Synonyms=TIM14; OrderedLocusNames=DEHA2G21648g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Essential component of the PAM complex, a complex required
CC for the translocation of transit peptide-containing proteins from the
CC inner membrane into the mitochondrial matrix in an ATP-dependent
CC manner. In the complex, it is required to stimulate activity of mtHSP70
CC (SSC1) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with PAM16. Component of the PAM complex, at least
CC composed of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The J domain is essential for co-chaperone activity and
CC mediates the heterodimerization with the J-like domain of PAM16.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TIM14 family. {ECO:0000305}.
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DR EMBL; CR382139; CAG90994.2; -; Genomic_DNA.
DR RefSeq; XP_462484.2; XM_462484.1.
DR AlphaFoldDB; Q6BH37; -.
DR SMR; Q6BH37; -.
DR STRING; 4959.XP_462484.2; -.
DR EnsemblFungi; CAG90994; CAG90994; DEHA2G21648g.
DR GeneID; 2905434; -.
DR KEGG; dha:DEHA2G21648g; -.
DR VEuPathDB; FungiDB:DEHA2G21648g; -.
DR eggNOG; KOG0723; Eukaryota.
DR HOGENOM; CLU_017633_13_0_1; -.
DR InParanoid; Q6BH37; -.
DR OMA; EGSAEWY; -.
DR OrthoDB; 1600166at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..172
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM14"
FT /id="PRO_0000071111"
FT TOPO_DOM 1..71
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..172
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT DOMAIN 114..172
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 172 AA; 19094 MW; 29224465F8FA77AD CRC64;
MAPFNMDIPT LAIPGDRNQS QAIELSQQAQ QPQQPQQSQQ AYTGHLQRKQ ADEGSAEYYF
DKGCEWMGNH PWMTGMGVLG VAYFASGFVK SKQPGINGKA FVKGPFGQKM TPKEALQILN
LKETNLSQAK LKEQHRKLMM ANHPDKGGSS YLATKVNEAK DILEKRGGLK KK
